Cancer Diagnostics Solutions
It recognizes a transcription factor of 64-67kDa, identified as c-myc. Its epitope spans between aa 410-419 (EQKLISEEDL) which is a specific portion of an alpha helical region of human c-myc protein. This MAb shows no cross-reaction with v-myc. c-myc is involved in the control of cell proliferation and differentiation and is amplified and/or overexpressed in a variety of tumors. Over-expression of c-myc protein occurs frequently in luminal cells of prostate intraepithelial neoplasia as well as in most primary carcinomas and metastatic disease.
The oncogene-encoded proteins c-Myc, n-Myc, and l-Myc play critical roles in cell proliferation, differentiation, and the development of neoplastic diseases. Mutations in Myc genes are frequently associated with various cancers, leading to the constitutive expression of Myc proteins. This abnormal expression results in the deregulation of numerous genes involved in cell proliferation, ultimately contributing to cancer formation. Specifically, c-Myc functions as a transcription factor and proto-oncogene, acting as a key regulator in processes such as cell cycle regulation, metabolism, apoptosis, differentiation, cell adhesion, and tumorigenesis.
The c-Myc protein is a 62 kDa transcription factor encoded by the MYC gene on chromosome 8q24. It plays a central role in regulating cell proliferation, differentiation, apoptosis, and cell cycle progression, and is frequently overexpressed in a wide range of human malignancies. Phosphorylation at Thr58 and Ser62 by kinases such as GSK-3, CDKs, ERK2, and JNK modulates c-Myc activity and stability. c-Myc is essential for tumor vasculogenesis and angiogenesis, facilitating tumor growth by supporting vascular development. The deregulated expression of c-Myc can induce apoptosis depending on cellular context. Antibodies against c-Myc epitopes detect proteins with Myc tags at either terminus. Members of the MYC gene family c-Myc, N-Myc, and L-Myc are involved in oncogenesis. C-Myc amplification is seen in lung, breast, and colon cancers, while N-Myc is amplified in neuroblastoma. Chromosomal translocations involving c-Myc and immunoglobulin loci are characteristic of Burkitt lymphoma and other B-cell lymphoproliferative disorders.
This MAb is specific to Complement 4d (C4d) and reacts with the secreted as well as cell-bound C4d.C4d is a degradation product of the activated complement factor C4b. Complement 4b is typically activated by binding of Abs to specific target molecules. Following activation and degradation of the C4 molecule, thio-ester groups are exposed, which allow transient, covalent binding of the degradation product Complement 4d to endothelial cell surfaces and extracellular matrix components of vascular basement membranes near the sites of C4 activation.?
Carbonic Anhydrase IX (CA IX) belongs to a family of zinc containing metalloproteins that catalyze the reversible hydration of carbon dioxide (CO?). Among the various carbonic anhydrases, CA IX is unique as it is anchored to the cell membrane and is predominantly expressed in the human gastrointestinal tract, especially in the stomach.
Studies have shown that CA IX exhibits consistent immunoreactivity in clear cell renal cell carcinoma (RCC), making it a valuable marker for identifying this type of tumor.
Carbonic anhydrases (CAs) are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide to carbonic acid, which subsequently dissociates into protons (H?) and bicarbonate ions (HCO??). These enzymes are ubiquitously expressed across mammalian tissues and play essential roles in maintaining acid-base homeostasis by modulating pH through the regulation of proton flux.
Among the carbonic anhydrase isoforms, carbonic anhydrase IX (CA IX) is highly inducible under hypoxic conditions, primarily through transcriptional activation by hypoxia-inducible factor 1-alpha (HIF-1?). CA IX is characterized by its membrane localization and relative stability under hypoxic stress, contributing to its functional significance in the tumor microenvironment.
In hypoxic tissues, CA IX contributes to extracellular acidification and intracellular pH regulation, processes critical for cell survival. Inhibition of CA IX activity disrupts this balance, leading to enhanced cell death under hypoxic conditions. Due to its selective expression and stability in hypoxia, CA IX is widely recognized as a robust histochemical marker of hypoxic regions in both neoplastic and non-neoplastic tissues
The mucins are a family of highly glycosylated, secreted proteins characterized by a basic structure of variable numbers of tandem repeats (VNTRs). These high molecular weight glycoproteins are components of the glycocalyx, a polysaccharide biofilm that shields mucosal epithelial surfaces from particulate matter and microorganisms. Epithelial mucins, found on cell surfaces and secreted by cells, play critical roles in adhesion modulation, cell signaling, and the protection of epithelial cells. The number of tandem repeats varies significantly among different alleles, highlighting the polymorphic nature of these proteins.
The mucin family includes Mucins 1-4, Mucin 5 (isoforms AC and B), Mucins 6-8, Mucins 11-13, and Mucins 15-17. Mucin 16, also known as CA125 and encoded by the MUC16 gene, is a high molecular weight tumor-associated antigen. It contains three main domains: a carboxy-terminal domain, an extracellular domain, and an amino-terminal domain. Mucin 16, an ovarian cancer-associated antigen, is commonly used as a biomarker to monitor the progression of epithelial ovarian cancer. This hydrophilic, membrane-associated protein may also play a role in vitamin A functions.
Carcinoma antigen 125 (CA125) is a high?molecular-weight tumor-associated antigen, characterized as a heavily glycosylated mucin encoded by the MUC16 gene. It is expressed in ovarian carcinoma as well as in various epithelial malignancies, including endometrial carcinoma, cervical carcinoma, and clear cell carcinoma of the urinary bladder. Additionally, CA125 demonstrates affinity for mesothelin, a cell-surface glycoprotein expressed in mesothelioma. The CA125 mesothelin interaction is postulated to facilitate peritoneal dissemination of ovarian carcinoma cells, thereby contributing to metastatic progression.
A notable human chromosomal translocation involving the Myc gene is t(8;14), which is critical for the pathogenesis of most cases of Burkitt's lymphoma. Aberrations in Myc expression have also been implicated in the development of several other malignancies, including carcinomas of the cervix, colon, breast, lung, and stomach.
Calcitonin is a 32-amino acid polypeptide hormone that is produced in humans primarily by C-cells located in the thyroid, and in many other animals in the ultimobranchial gland. It acts to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH). It has been found in fish, reptiles, birds, and mammals. Its importance in humans has not been as well established as in other animals.
Immunohistochemical staining with Calcitonin antibody has proven to be an effective way of demonstrating the existence of Calcitonin-producing cells in the thyroid. C-cell Hyperplasia and Medullary Thyroid Carcinomas stain positive for Calcitonin. Studies of Calcitonin have resulted in the identification of a wide spectrum of C-cell proliferative abnormalities.
Calcitonin is a 32-amino acid polypeptide hormone that is produced in humans primarily by C-cells located in the thyroid, and in many other animals in the ultimobranchial gland. It acts to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH). It has been found in fish, reptiles, birds, and mammals. Its importance in humans has not been as well established as in other animals.
Immunohistochemical staining with Calcitonin antibody has proven to be an effective way of demonstrating the existence of Calcitonin-producing cells in the thyroid. C-cell Hyperplasia and Medullary Thyroid Carcinomas stain positive for Calcitonin. Studies of Calcitonin have resulted in the identification of a wide spectrum of C-cell proliferative abnormalities
Calcitonin is a 32-residue polypeptide hormone predominantly synthesized and secreted by the parafollicular (C) cells of the thyroid gland. It plays a critical role in calcium homeostasis by exerting hypocalcemic and hypophosphatemic effects, primarily through the inhibition of osteoclastic bone resorption and enhancement of calcium and phosphate deposition in the skeletal matrix. Immunohistochemical detection of calcitonin via specific antibodies serves as a valuable diagnostic tool in the evaluation of C cell hyperplasia and the identification of medullary thyroid carcinoma
Caldesmon is a smooth muscle?associated regulatory protein that binds to actin, myosin, tropomyosin, and calmodulin. It demonstrates greater specificity for smooth muscle differentiation compared to desmin and muscle-specific actin. Immunohistochemically, caldesmon is valuable for distinguishing smooth muscle neoplasms from myofibroblastic tumors, as well as for differentiating uterine leiomyomas from endometrial stromal tumors. Additionally, it serves as a useful marker in the identification of epithelioid mesothelioma
Caldesmon is a developmentally regulated actin-binding protein implicated in the regulation of contractile activity in both smooth muscle and non-muscle cells. Two closely related isoforms of human caldesmon have been characterized, distinguished by their electrophoretic mobility and tissue-specific expression profiles. The high molecular weight isoform (h-caldesmon; 120?150 kDa) is predominantly expressed in smooth muscle tissue, whereas the low molecular weight isoform (l-caldesmon; 70?80 kDa) is primarily localized in non-muscle cells. Notably, neither isoform has been detected in skeletal muscle tissue
Multiple isoelectric variants of calponin have been identified, but only two molecular weight isoforms are known: a 34 kDa form and a 29 kDa form. The 29 kDa isoform, also known as I-calponin, is predominantly found in the smooth muscle of the urogenital tract, whereas the 34 kDa isoform is primarily present in vascular and visceral smooth muscle.
In Western blot analysis, this monoclonal antibody (MAb) specifically reacts with the 34 kDa isoform of calponin in human aortic medial smooth muscle extracts but shows no reactivity with fibroblast extracts from cultured human foreskin. Calponin, a protein that binds to calmodulin, F-actin, and tropomyosin, is believed to play a role in regulating smooth muscle contraction. Its expression is restricted to smooth muscle cells and serves as a marker of the differentiated, contractile phenotype in developing smooth muscle tissue.
Calponin is a smooth muscle-specific protein that binds to actin, tropomyosin, and calmodulin. It is believed to play a role in the regulation of actomyosin activity and the modulation of muscle contraction. Calponin is expressed in smooth muscle cells and myoepithelial cells and has been utilized in identifying invasive breast lesions. Additionally, it is expressed in malignant fibrous histiocytoma of bone and adenoid cystic carcinoma of the salivary gland.
The consistent positive staining pattern of calponin in adenoid cystic carcinomas can help distinguish them from polymorphous low-grade adenocarcinomas, which consistently show negative staining.
This antibody specifically recognizes a 31.5 kDa protein identified as Calretinin. Calretinin is an intracellular calcium-binding protein that belongs to the troponin C superfamily, characterized by an EF-hand domain. During immunohistochemical analysis, calretinin expression in the developing cerebellum becomes evident in the later stages, starting with weak staining in Purkinje and basket cells, as well as in the neurons of the dentate nucleus from week 21 of gestation. The staining intensity increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and certain pulmonary adenocarcinomas. Additionally, calretinin occasionally shows positivity in other tumor types, including ameloblastomas and sex cord tumors of the ovary and testis.
Calretinin, encoded by gene calb2, also known as Calbindin 2, is a calcium-binding protein belonging to the troponin C superfamily and calbindin subfamily. It consists of 271 amino acids and has a molecular weight of 31.5 kD. Among the many calcium-binding proteins in the nervous system, calretinin, together with parvalbumin and calbindin-D28K, are particularly striking in their abundance and in the specificity of their distribution.
They can be found in different subsets of neurons in many brain regions and are considered valuable markers of neuronal subpopulations for anatomical and developmental studies. Calretinin is approved as a highly sensitive and specific marker for mesothelial cells and one of the best positive markers for differentiating epithelial malignant mesotheliomas.
Calretinin, encoded by the CALB2 gene on chromosome 16, is a calcium-binding protein belonging to the troponin C superfamily. It contains six EF-hand motifs, which are helix-loop-helix structural domains responsible for coordinating calcium ion binding. Through these motifs, calretinin plays a critical role in calcium signaling, intracellular calcium buffering, and the regulation of neuronal excitability.
Calretinin is physiologically expressed in a variety of cell types, including mesothelial cells, mast cells, select populations of neurons, as well as in hair follicles and adipocytes
In formalin-fixed, paraffin-embedded tissue sections, AMACR (P504S) serves as a valuable positive diagnostic marker for prostate carcinoma. When used in conjunction with basal cell markers such as high-molecular-weight cytokeratin (34?E12) or p63?which act as negative markers?it enhances diagnostic accuracy, particularly in identifying small foci of carcinoma in prostate needle biopsies.
This gene encodes a member of the cysteine-aspartate protease (caspase) family, enzymes that play a pivotal role in the execution phase of apoptosis. Caspases are synthesized as inactive zymogens that undergo proteolytic cleavage at conserved aspartate residues, generating large and small subunits that assemble into the catalytically active heterodimer. The encoded protein functions by cleaving and activating caspases-6, -7, and -9, while itself being processed by caspases-8, -9, and -10. It represents the principal caspase responsible for the proteolytic cleavage of amyloid precursor protein (APP) at the amyloid-beta 4A site, a process implicated in neuronal degeneration associated with Alzheimer?s disease. Alternative splicing of this gene gives rise to two transcript variants encoding an identical protein product.
Cathepsin D is a gene located on chromosome 11p15.5 that encodes a lysosomal aspartic endopeptidase involved in the proteolytic degradation of intracellular and endocytosed proteins. This enzyme exhibits ubiquitous tissue expression, with particularly high levels observed in the liver, kidney, and central nervous system. Cathepsin D is initially synthesized as an inactive zymogen, procathepsin D, which undergoes proteolytic maturation under acidic lysosomal conditions to yield the catalytically active form. In addition to its canonical role in lysosomal protein catabolism and homeostasis, Cathepsin D is functionally implicated in diverse physiological and pathological processes, including programmed cell death (apoptosis), peptide hormone processing, and MHC class II antigen presentation. Aberrant expression or dysregulated enzymatic activity of Cathepsin D has been associated with the pathogenesis of numerous disorders, notably neurodegenerative diseases, malignancies, and cardiovascular conditions. In oncogenesis, Cathepsin D overexpression correlates with enhanced tumor invasiveness and metastatic potential, thereby representing a candidate biomarker and putative therapeutic target. Ongoing investigations continue to elucidate its multifaceted roles in cellular physiology and disease.
The gene encodes a lysosomal cysteine protease belonging to the peptidase C1 family, primarily involved in the degradation of bone matrix proteins during bone remodeling and resorption. It is predominantly expressed in osteoclasts, where it plays a critical role in osteolytic activity. In addition to its physiological function in skeletal homeostasis, aberrant expression of the encoded protease has been observed in a substantial subset of human breast carcinomas, suggesting a potential role in facilitating tumor invasion and metastasis through extracellular matrix degradation. Pathogenic variants in this gene are causative of pycnodysostosis, a rare autosomal recessive osteosclerotic skeletal dysplasia characterized by increased bone density, short stature, and skeletal fragility. Moreover, the gene may undergo RNA editing, which could contribute to post-transcriptional regulation and functional diversity of the encoded enzyme.
CD10, a 100 KD glycoprotein, also known as Common Acute Lymphocytic Leukemia Antigen (CALLA), is a cell surface enzyme with neutral metalloendopeptidase activity which inactivates a variety of biologically active peptides. CD10 is expressed on the cells of lymphoblastic, Burkitt?s, and follicular germinal center lymphomas, and chronic myelogenous leukemia (CML). It is also expressed on the surface of normal early lymphoid progenitor cells, immature B cells within bone marrow and germinal center B cells within lymphoid tissue. CD10 is also present on breast myoepithelial cells, with especially high expression on the brush border of kidney and gut epithelial cells.
The common acute lymphoblastic leukemia antigen (CALLA/CD10) is a type II single-pass transmembrane metalloendopeptidase that functions by cleaving and inactivating a range of peptide substrates involved in signal transduction, including enkephalins, bombesin, and substance P. Through its enzymatic activity, CD10 regulates peptide-mediated signaling pathways.
CD10 is expressed in various hematopoietic cell populations, including immature T and B lymphocytes, B cells within the germinal centers of lymphoid follicles, and granulocytes. In addition to hematopoietic tissues, CD10 is also detected in several non-hematopoietic cell types, such as epithelial cells of the gastrointestinal tract and renal tubular epithelium. In the liver, moderate to strong immunoreactivity is typically observed in bile canaliculi.
Clinically, CD10 serves as a valuable immunophenotypic marker in the diagnosis and classification of hematologic malignancies, including acute lymphoblastic leukemia (ALL), follicular lymphoma, Burkitt lymphoma, certain myeloid and lymphoid neoplasms, and chronic myelogenous leukemia (CML) in lymphoid blast crisis.
Furthermore, CD10 is recognized as a marker of endometrial stromal cells and is diagnostically useful in distinguishing endometrial stromal sarcoma (ESS) from other uterine mesenchymal tumors, such as uterine cellular leiomyoma (UCL) and uterine leiomyosarcoma (ULS).
CD10, a 100 KD glycoprotein, also known as Common Acute Lymphocytic Leukemia Antigen (CALLA), is a cell surface enzyme with neutral metalloendopeptidase activity which inactivates a variety of biologically active peptides.
CD10 is expressed on the cells of lymphoblastic, Burkitt?s, and follicular germinal center lymphomas, and chronic myelogenous leukemia (CML). It is also expressed on the surface of normal early lymphoid progenitor cells, immature B cells within bone marrow and germinal center B cells within lymphoid tissue.
CD10 is also present on breast myoepithelial cells, with especially high expression on the brush border of kidney and gut epithelial cells.
CD103, also known as integrin ?E, is encoded by the ITGAE gene located on chromosome 17. This integrin subunit is characteristically expressed in nearly all cases of hairy cell leukemia (HCL), while its expression is largely absent in most other B-cell lymphoproliferative disorders, with the exception of occasional cases of splenic marginal zone lymphoma. Immunohistochemical studies have demonstrated CD103 expression in mononuclear cells localized within the interfollicular zones of lymph nodes and in intraepithelial lymphocytes primarily situated near the basal layer of the tonsillar mucosa. Due to its high sensitivity and specificity for HCL, CD103 serves as a valuable immunophenotypic marker for differentiating HCL from other B-cell neoplasms
CD105 (Endoglin) is a type I transmembrane glycoprotein that serves as a co-receptor in the TGF-? receptor complex. It is expressed on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells, and is essential for cardiovascular development and vascular remodeling. Mutations in ENG are linked to hereditary hemorrhagic telangiectasia type 1. CD105 expression is markedly upregulated in proliferating endothelial cells during tumor angiogenesis and inflammation, while largely absent in normal vasculature. Tumor angiogenesis is driven by factors such as VEGF, which promotes endothelial proliferation and vascular permeability. Unlike pan-endothelial markers CD31 and CD34, Endoglin is more specific for neovascularization, making it a sensitive biomarker for angiogenesis. Its expression correlates with poor prognosis in several malignancies, including prostate, lung, gastric, breast, and brain cancers. Owing to its restricted expression in angiogenic vessels, CD105 is also a promising therapeutic target for anti-angiogenesis strategies.
Endoglin, also known as CD105, is a Type I membrane glycoprotein found on cell surfaces and is an integral part of the TGF-beta receptor complex. This protein is present on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. It plays a critical role in the development of the cardiovascular system and in vascular remodeling, with its expression being tightly regulated during heart development. CD105 is notably highly expressed in endothelial cells during tumor angiogenesis and inflammation, while showing weak or negative expression in the vascular endothelium of normal tissues. This selective expression makes it a promising prognostic marker in various tumors. Unlike CD31 or CD34, which are other markers for angiogenesis, endoglin is more specific and sensitive as it labels only newly-formed blood vessels. Therefore, it may serve as a prognostic marker for prostate adenocarcinoma, as well as cancers of the lung, stomach, breast, and brain.
KIT (also known as c-KIT or CD117) is a proto-oncogene encoding a type III transmembrane receptor tyrosine kinase that serves as the cellular receptor for mast cell growth factor (MGF), also referred to as stem cell factor (SCF). Initially identified as the cellular homolog of the feline sarcoma viral oncogene v-kit, KIT plays a pivotal role in the regulation of proliferation, survival, and functional activation of both hematopoietic and non-hematopoietic cell lineages.
Activating mutations in KIT have been implicated in the pathogenesis of several malignancies and disorders, including gastrointestinal stromal tumors (GISTs), systemic mastocytosis, acute myeloid leukemia (AML), and the pigmentation disorder piebaldism. Among these, the D816V mutation in the activation loop of the KIT tyrosine kinase domain is of particular clinical relevance due to its constitutive signaling and resistance to certain tyrosine kinase inhibitors (TKIs), thereby serving as a critical molecular target in therapeutic interventions for neoplastic mast cell proliferation.
KIT is expressed in various cell types, notably hematopoietic stem cells, germ cells, interstitial cells of Cajal in the gastrointestinal tract, and mast cells. Ligand binding by SCF induces KIT dimerization, leading to auto phosphorylation of specific intracellular tyrosine residues, including Tyr703, which facilitates the recruitment of adaptor proteins such as Grb2 and the subsequent activation of the Ras-MAPK (ERK) signaling cascade. In addition to the MAPK pathway, activated KIT transduces signals through multiple downstream effectors, including PI3K-AKT, PLC?, and the JAK/STAT pathways. These signaling networks collectively contribute to critical biological processes such as haematopoiesis, stem cell niche maintenance, and gametogenesis.
CD117 is a tyrosine-kinase receptor for stem cell factor (SCF), also known as ?steel factor? or ?c-kit ligand?. C-kit is a polypeptide that activates bone marrow precursors of a number of blood cells, but its receptor is also present in other cells. C-kit mutations in the interstitial cells of Cajal in the digestive tract are probably the key to Gastrointestinal Stromal Tumors (GISTs). CD117 antibody reacts with interstitial cells of Cajal, germ cells, bone marrow stem cells, melanocytes, breast epithelium and mast cells. This receptor is found on a wide variety of tumor cells (Follicular and Papillary Carcinoma of the Thyroid, Adenocarcinomas from endometrium, lung, ovary, pancreas, breast; Malignant Melanoma, Endodermal Sinus Tumor, Small-cell Carcinoma) but has been particularly useful in differentiating Gastrointestinal Stromal Tumors (GIST) from Kaposi?s Sarcoma and tumors of smooth-muscle origin
Interleukin-3 receptor alpha subunit (IL-3R?), a member of the type I cytokine receptor superfamily, forms a heterodimeric complex with the common beta subunit (?c, also known as CDw131) to mediate signaling in response to Interleukin-3 (IL-3). The IL-3R? chain confers ligand specificity, while dimerization with the ?c subunit?induced upon IL-3 binding?is essential for downstream signaling activation, though not required for high-affinity ligand binding. Notably, IL-3R? is overexpressed on blasts in acute myeloid leukemia (AML) relative to normal hematopoietic progenitor cells, highlighting its relevance as a candidate target for the development of AML-directed therapeutic strategies
CD13, also referred to as aminopeptidase-N, is a type II transmembrane metalloprotease widely expressed in endothelial cells, epithelial cells, fibroblasts, and leukocytes. It is a clinically relevant myeloid-associated antigen and is frequently incorporated into immunophenotypic panels for the diagnosis of acute myeloid leukemia (AML), particularly in combination with markers such as CD34, CD117, CD16, and CD33. CD13 expression is also a consistent feature of myeloid sarcoma, where its detection by anti-CD13 antibody supports accurate lineage determination when used with complementary markers. In addition, CD13 is expressed in both normal and neoplastic hepatocytes, showing a characteristic canalicular staining pattern similar to that observed with polyclonal carcinoembryonic antigen (CEA) and CD10. This pattern makes anti-CD13 a useful ancillary marker for differentiating hepatocellular carcinoma from non-hepatocellular neoplasms.
CD138, also known as syndecan-1, is a transmembrane heparan sulfate proteoglycan that interacts with a broad spectrum of cytokines and extracellular matrix (ECM) components, thereby modulating signaling pathways and influencing various developmental and cellular processes. Its expression is predominantly observed in differentiating keratinocytes and is transiently upregulated across all epidermal layers in response to tissue injury. CD138 is also constitutively expressed on plasma cells and has been detected on fibroblasts, vascular smooth muscle cells, and endothelial cells. Alterations in CD138 surface expression either upregulation or downregulation are frequently associated with the acquisition of oncogenic properties. The soluble, shed form of CD138 (sCD138) in serum serves as a prognostic biomarker for tumor progression and malignancy
CD14 is a 55-kDa molecule predominantly expressed as a glycosylphosphatidylinositol (GPI)-anchored membrane protein on the surface of monocytes, macrophages, and polymorphonuclear leukocytes, and is also present in a soluble form in the circulation. It primarily functions as a pattern recognition receptor (PRR) for lipopolysaccharide (LPS), facilitating innate immune responses to Gram-negative bacteria. In addition to its established role in endotoxin-mediated signaling, CD14 has been implicated in lipid transport, intercellular communication during immunological processes, and the recognition and clearance of apoptotic cells. CD14 expression is markedly elevated on monocytes and macrophages and is significantly upregulated during the differentiation of monocytic precursors into mature monocytes, making it a widely used phenotypic marker for monocyte/macrophage lineage differentiation. CD14-specific monoclonal antibodies also recognize Langerhans cells and subsets of dendritic cells, reflecting its broader expression within the myeloid lineage
3-fucosyl-N-acetyllactosamine (3-FAL) or CD15 or X-hapten plays a role in mediating phagocytosis, bactericidal activity, and chemotaxis. It is present on >95% of granulocytes including neutrophils and eosinophils and to a lesser degree on monocytes. CD15 is also expressed in Reed-Sternberg cells and some epithelial cells. CD15 antibody is very useful in the identification of Hodgkin?s disease. CD15 is occasionally expressed in large cell lymphomas of both B and T phenotypes which otherwise have a quite distinct histological appearance.
CD15, also referred to as Lewis X or stage-specific embryonic antigen-1 (SSEA-1), is a trisaccharide epitope composed of 3-fucosyl-N-acetyllactosamine. It is expressed on various glycoconjugates, including glycolipids, glycoproteins, and proteoglycans, across multiple cell types such as granulocytes, mast cells, monocytes, macrophages, gastric epithelial cells, neural cells, and a range of neoplastic cells. Several structural variants of Lewis X exist, including sialyl-Lewis X and sulphated Lewis X. Cells exhibiting high surface levels of Lewis x demonstrate pronounced calcium-dependent homotypic aggregation via Lewis x Lewis x interactions, a mechanism that plays a role in biological processes such as embryonic compaction and the autoaggregation of teratocarcinoma cells. The sialylated forms of Lewis X (sialyl-Lewis x) and its isomer sialyl-Lewis A (sialyl-Lewis a) serve as ligands for selectins, contributing to selectin-mediated cell adhesion. Immunohistochemical detection of CD15 is commonly utilized as a diagnostic marker, particularly in the confirmation of classical Hodgkin lymphoma.
CD15 is a complex cluster of cell surface glycoproteins and glycolipids with a common trisaccharide structure, 3-fucosyl-N-acetyllactosamine (3-FL), also referred to as Lewis X (LeX) antigen. This antigen is involved in neutrophil functions such as, cell-cell interactions, phagocytosis, stimulation of degranulation and respiratory burst.
The CD15 is expressed in Reed-Sternberg cells, myeloid cells as well as epithelial cells. CD15 antibody has been used as an immunohistochemical marker to identify Reed-Sternberg cells (RSC) in classical Hodgkin lymphoma (CHL).
CD16 (Fc?RIII) is a low-affinity Fc receptor for IgG, existing in two isoforms: CD16A (Fc?RIIIa) and CD16B (Fc?RIIIb). These isoforms are expressed on various immune effector cells, including natural killer (NK) cells, neutrophils, monocytes, and activated macrophages. Engagement of CD16 with IgG-opsonized targets can trigger antibody-dependent cellular cytotoxicity (ADCC), proinflammatory cytokine release, and microbial clearance.
In a recent study by Sconocchia et al., elevated intratumoral infiltration of CD16-positive cells in colorectal carcinoma was significantly correlated with improved overall survival. This prognostic association remained independent of established clinical variables, including CD8+ T-cell infiltration and the presence of metastatic disease.
CD163 is a protein encoded by the CD163 gene in humans. It acts as a high-affinity scavenger receptor for the hemoglobin-haptoglobin complex and, with lower affinity, for hemoglobin alone in the absence of haptoglobin. CD163 is exclusively expressed on the surface of human monocytes and macrophages, primarily during the late phase of inflammation, making it valuable for macrophage phenotyping. There is also a soluble form in plasma, sCD163, which is elevated in various inflammatory diseases such as liver cirrhosis, type 2 diabetes, atherosclerosis, and several others.
CD19, a 95 kDa transmembrane glycoprotein of the immunoglobulin superfamily, contains two extracellular Ig-like C2-set domains and is expressed throughout B cell ontogeny, except in terminally differentiated plasma cells. It is also present on follicular dendritic cells and certain monocytic lineage-derived myeloid leukemias. Recognized as the earliest and most broadly expressed B cell-specific marker, CD19 is universally present in B cell precursor leukemias. Functionally, CD19 forms a signaling complex with CD21, CD81, Leu13, MHC class II, and the B cell receptor (BCR), serving as a potent coreceptor that amplifies BCR-mediated signaling. CD19 engagement induces tyrosine phosphorylation, intracellular calcium mobilization, and clonal proliferation. Notably, it can initiate signaling independently of BCR co-ligation, acting as a critical hub for multiple pathways that regulate both physiological and malignant B cell responses. CD19 mutations can cause hypogammaglobulinemia, while overexpression contributes to B cell hyperactivity. It is consistently expressed on all peripheral B cells, marked by kappa or lambda light chains
CD19 is present in both normal and malignant B-cells and has long been considered to be the most reliable surface marker of this lineage over a wide range of maturational stages. In normal lymphoid tissue, CD19 is observed in germinal centers, mantle zone cells, and scattered cells in the interfollicular areas.
Anti-CD19 exhibits an overall immunoreactivity pattern similar to those of the antibodies against CD20 and CD22. However, in contrast to CD20, CD19 is also expressed in immature B-cells; although recent studies have described CD19 loss in a few B-cell neoplasms
CD19 is a transmembrane glycoprotein of the immunoglobulin superfamily, characterized by two Ig-like domains. It is expressed throughout B cell development, from early precursors to mature B cells, but is absent in terminally differentiated plasma cells. CD19 is also found on follicular dendritic cells and, in some cases, on myeloid leukemia cells of monocytic lineage. It is considered the earliest and most broadly expressed B cell-specific antigen and is present in all B cell precursor leukemias. Functionally, CD19 forms a multimolecular complex with CD21, CD81, Leu13, MHC class II, and the B cell receptor (BCR), acting as a critical signal-amplifying coreceptor. It enhances BCR signaling by lowering the threshold for activation, enabling B cells to respond sensitively to low-affinity antigens. CD19 signaling induces tyrosine phosphorylation, calcium mobilization, and cellular proliferation. Importantly, CD19 can also mediate B cell activation independently of BCR co-ligation, serving as a central regulatory hub for various signaling pathways. CD19 is essential for normal B cell homeostasis, and its dysregulation has pathological consequences?loss-of-function mutations cause hypogammaglobulinemia, while overexpression leads to hyperactive B cell responses. CD19 is expressed on all peripheral B cells, as defined by ? or ? light chain
At least five CD1 genes (CD1a, CD1b, CD1c, CD1d, and CD1e) have been identified. CD1 proteins restrict T cell responses to non-peptide lipid and glycolipid antigens, playing a crucial role in non-classical antigen presentation. CD1a is a non-polymorphic, MHC Class I-related cell surface glycoprotein that associates with beta-2 microglobulin. Anti-CD1a antibodies can label Langerhans cell histiocytosis (Histiocytosis X), extranodal histiocytic sarcoma, certain T-lymphoblastic lymphoma/leukemias, and interdigitating dendritic cell sarcoma of the lymph node. When used alongside TTF-1 and CD5 antibodies, anti-CD1a helps differentiate pulmonary neoplasms from thymic neoplasms.
CD1a is consistently expressed in thymic lymphocytes in both typical and atypical thymomas but is only focally expressed in 1 out of 6 cases of thymic carcinoma and absent in pulmonary neoplasm lymphocytes. Additionally, anti-CD1a is reported as a new marker for perivascular epithelial cell tumor (PEComa)
CD2 is a cell-adhesion molecule located on the surfaces of T-cells and natural killer (NK) cells. Also known as T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, erythrocyte receptor, and rosette receptor, CD2 belongs to the immunoglobulin superfamily due to its structural features. It contains two immunoglobulin-like domains in its extracellular region and interacts with other adhesion molecules, including lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans and CD48 in rodents, which are found on the surfaces of other cells. Besides its adhesive role, CD2 serves as a co-stimulatory molecule for T and NK cells.
CD20 is a non-Ig differentiation antigen of B cells and the expression of CD20 is restricted to normal and neoplastic B cells, being absent from all other leukocytes and tissues. CD20 is the most specific B-cell marker used in paraffin immunohistochemistry. It acts as calcium channel involved in B cell activation and cell cycle progression
OX2 (also known as CD200 or MOX2) is a 248-amino acid cell surface glycoprotein belonging to the immunoglobulin superfamily (IgSF). It is expressed on lymphoid cells, neurons, and vascular endothelium. Its cognate receptor, OX2R, is a heavily glycosylated membrane protein, with N-linked oligosaccharides accounting for approximately 70% of its molecular mass. OX2R expression is predominantly restricted to lymphoid and neuronal tissues. Phylogenetic analyses indicate that OX2 and OX2R are evolutionarily related to other leukocyte IgSF glycoproteins, suggesting divergence from a common ancestral protein. The cytoplasmic tail of OX2R contains NPXY motifs, which serve as docking sites for proteins harboring PTB/PID interaction domains. Engagement of OX2 with OX2R is implicated in immunomodulatory signaling pathways that attenuate macrophage-mediated inflammatory responses and limit tissue injury.
CD21, also known as complement receptor 2 (CR2), C3d receptor, or Epstein-Barr virus (EBV) receptor, is a membrane-bound glycoprotein that binds to cleavage fragments of complement component C3?particularly C3d, C3dg, and iC3b?which remain covalently linked to complement-activated surfaces or antigenic structures. CD21 plays a pivotal role in the immune system by mediating the capture and retention of immune complexes, supporting the long-term survival of memory B cells, and contributing to the initiation and maintenance of T cell?dependent humoral immune responses. Functionally, CD21 serves as a primary receptor for EBV, facilitating viral entry into B lymphocytes. It also plays a role in the pathogenesis of prion diseases by directing prion proteins to follicular dendritic cells and promoting neuroinvasion following peripheral exposure. A soluble form of CD21 (sCD21), produced via proteolytic shedding from the lymphocyte surface, retains ligand-binding capacity and may modulate immune signaling in the extracellular environment. CD21 also interacts with interferon-alpha (IFN?), CD23, and forms a multimeric signal transduction complex with CD19, CD81 (TAPA-1), and Leu13, which lowers the threshold for B cell receptor (BCR) activation and enhances B cell signaling. Genetic polymorphisms in the CR2 gene have been associated with increased susceptibility to systemic lupus erythematosus type 9 (SLEB9), suggesting a role in autoimmunity. Additionally, alternative splicing of CR2 transcripts generates multiple CD21 isoforms, which may contribute to functional diversity
CD21 is a type 2 transmembrane protein that functions as the complement receptor for C3d and the Epstein-Barr virus. This protein is notably expressed on follicular dendritic cells and mature B cells, especially in the marginal and mantle zones of lymphoid tissues. CD21 serves as a valuable marker for identifying neoplasms originating from follicular dendritic cells.
CD22 (BL-CAM) is a type I transmembrane glycoprotein expressed on mature B cells and most B-cell lymphomas, including hairy cell leukemia and diffuse large B-cell lymphoma, but absent in classical Hodgkin lymphoma. It exists as two isoforms (130 and 140 kDa) produced via alternative splicing. Its extracellular region contains seven Ig-like domains that bind ?2, 6-linked sialic acids on various cell types, though this binding may be masked by cis interactions on the same cell surface. CD22 expression is restricted to late-stage B-cell differentiation, making it a valuable marker for identifying mature B-cell malignancies. Intracellularly, CD22 contains six tyrosine residues within ITIM and activation-like motifs. Upon B-cell receptor (BCR) engagement, these sites are phosphorylated, allowing CD22 to modulate BCR signaling. It exerts inhibitory effects via SH2 domain-containing phosphatases (e.g., SHP-1) and promotes signaling through Src family kinases. Its regulatory function and lineage-specific expression make CD22 a key diagnostic and therapeutic target in B-cell biology.
CD23 is a type II membrane glycoprotein which functions as a receptor for IgE and for lymphocyte growth factor. CD23 plays an important role in B cell activation and growth.
CD23 can be positive in B lymphocytes, monocytes, macrophages, follicular dendritic cells, and T cell subsets. CD23 staining is applied in the differentiation of small lymphocytic lymphomas (SLL) and mantle cell lymphoma.
CD23 expression can be detected in SLL, mediastinal large B cell lymphoma, and lymphoplasmacytic lymphoma
CD23, a type II transmembrane glycoprotein, is a key molecule for B-cell activation and growth and functions as a receptor for IgE.
CD23 antibody labels activated B cells expressing IgM/IgD and follicular dentritic cells. In tumors, CD23 antibody is helpful in identification of B-cell chronic lymphocytic leukemia (CLL), follicular dendritic cell tumors and mediastinal large B-cell lymphoma. In addition, anti-CD23 is useful to differentiate CLL from mantle cell lymphoma which is CD23 negative
CD23 (FCE2) is a type II integral membrane glycoprotein that is expressed on mature B cells, monocytes, eosinophils, platelets and dendritic cells. CD23 is a low affinity IgE receptor that mediates IgE-dependent cytotoxicity and phagocytosis by macrophages and eosinophils. CD23 associates as an oligomer where cooperative binding of at least two lectin domains is required for high affinity IgE binding to CD23. It may play a role in antigen presentation by B cells by interacting with CD40. CD23 has been shown to be associated with the Fyn tyrosine kinase. The truncated molecule can be secreted, then function as a potent mitogenic growth factor.
CD25, also known as the interleukin-2 receptor alpha chain (IL2RA), is a component of the heterotrimeric interleukin-2 (IL-2) receptor complex, which plays a critical role in the proliferation, differentiation, and survival of T and B lymphocytes. The high-affinity IL-2 receptor is composed of IL2RA, IL2RB (beta chain), and IL2RG (common gamma chain), the latter of which is shared with other cytokine receptors, including IL-4 and IL-7. IL2RA homodimers form low-affinity receptors, while IL2RB homodimers generate intermediate-affinity complexes.
IL2 is primarily synthesized by activated, mature T lymphocytes, and its expression in thymocytes is monoallelic?an uncommon regulatory mechanism that ensures precise gene dosage. IL-2 functions as a pleiotropic cytokine, promoting lymphocyte proliferation, enhancing natural killer (NK) cell cytotoxicity, and suppressing granulocyte-macrophage colony formation. Disruption of the Il2ra gene in murine models results in an inflammatory phenotype resembling ulcerative colitis, implicating its role in immune tolerance and regulation. Pathogenic variants in IL2RA are linked to interleukin-2 receptor alpha deficiency, a condition characterized by immune dysregulation
CD276, also referred to as B7-H3, is a type I transmembrane glycoprotein and a member of the B7 family of immune co-stimulatory molecules. It functions to promote the activation and proliferation of CD4? and CD8? T lymphocytes, augments cytotoxic T cell responses, and preferentially enhances interferon-gamma (IFN-?) secretion. CD276 expression is inducible on antigen-presenting cells such as dendritic cells and monocytes upon stimulation with pro-inflammatory cytokines. Additionally, it exhibits constitutive expression in various peripheral tissues, including the heart, kidney, testis, and colon. In humans, CD276 is expressed as two distinct isoforms generated through gene duplication and alternative splicing mechanisms. Emerging evidence highlights its potential as an immunotherapeutic target, particularly in modulating cell-mediated immune responses in oncological settings, where it may synergize with anti-angiogenic strategies
The CD3 antigen is present on early thymocytes and mature T cells and is generally regarded as a pan-T cell marker. This antibody will help detect CD3 expression in normal and neoplastic tissues.
This antibody reacts with the intracytoplasmic portion of the CD3 antigen expressed by T cells. It stains human T cellsin both the cortex and medulla of the thymus and in peripheral lymphoid tissues. This antibody issuitable for staining normal and neoplastic T cells in formalin-fixed, paraffin-embedded tissues
CD3 (Cluster of Differentiation 3) represents a sophisticated protein complex that directly interacts with the T-cell antigen receptor (TCR). Comprising five invariant polypeptide chains, CD3 forms three dimers essential for its function. These chains, denoted gamma, delta, epsilon, zeta, and eta, collectively orchestrate T-cell development and viability.
CD3 expression extends across various T-cell populations, spanning from the thymus to peripheral lymphoid tissues, blood, and bone marrow. Leveraging CD3 as a hallmark allows for precise identification of T-cells and T-cell derived malignancies. The credibility of CD3 as a marker is endorsed by its validation through the 9th International Conference on Human Leukocyte Differentiation Antigens (HLDA9).
CD30, a single chain glycoprotein, is synthesized as a 90kDa precursor which is processed in the Golgi complex into a membrane-bound phosphorylated mature 105/120kDa glycoprotein. The CD30/Ki-1 antigen is expressed by mononuclear Hodgkin and multinucleated Reed-Sternberg cells in Hodgkin?s disease, by the tumor cells of a majority of anaplastic large cell lymphomas, and by a varying proportion of activated T and B cells. Ber-H2 distinguishes large cell lymphomas derived from activated lymphoid cells from histiocytic malignancies and lymphomas derived from resting and precursor lymphoid cells or from anaplastic carcinomas
CD31 (PECAM-1) is a transmembrane glycoprotein member of the immunoglobulin supergene family of adhesion molecules. CD31 is expressed by stem cells of the hematopoietic system and is primarily used to identify and concentrate these cells for experimental studies as well as for bone marrow transplantation. Anti-CD31 has shown to be highly specific and sensitive for vascular endothelial cells. Staining of nonvascular tumors (excluding hematopoietic neoplasms) is rare. CD31 MAb reacts with normal, benign, and malignant endothelial cells which make up blood vessel lining. The level of CD31 expression can help to determine the degree of tumor angiogenesis, and a high level of CD31 expression may imply a rapidly growing tumor and potentially a predictor of tumor recurrence.
CD31, also known as platelet endothelial cell adhesion molecule-1 (PECAM-1), is an immunoglobulin superfamily member functioning as an inhibitory coreceptor in both T and B lymphocytes. It contains dual immunoreceptor tyrosine-based inhibitory motifs (ITIMs) within its cytoplasmic domain, which, upon phosphorylation by associated kinases, serve as docking sites for protein tyrosine phosphatases, thereby modulating immune signaling. CD31 is widely expressed throughout the vascular endothelium and is predominantly localized at intercellular junctions. Its N-terminal Ig-like domain mediates homophilic binding, facilitating endothelial cell-cell adhesion. CD31 is a multifunctional molecule involved in diverse physiological processes, including regulation of integrin-mediated adhesion, leukocyte transendothelial migration, angiogenesis, apoptosis, inhibition of immunoreceptor signaling, and control of macrophage phagocytosis. Additionally, it plays roles in autoimmune regulation, IgE-mediated hypersensitivity, and thrombosis. Given its broad functionality and expression profile, CD31 is considered a critical regulatory molecule within the vascular and immune systems, contributing to both vascular integrity and immune homeostasis.
CD33 is a transmembrane receptor belonging to the sialic acid-binding immunoglobulin-like lectin (Siglec) family and functions as an immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing molecule. It mediates inhibitory signaling through the recruitment of Src homology region 2 domain-containing phosphatases SHP-1 and SHP-2 to its cytoplasmic ITIM motifs. These motifs also facilitate receptor internalization via ubiquitin-dependent endocytosis. CD33 is predominantly expressed on cells of the myelomonocytic lineage, including granulocyte and macrophage progenitors in the bone marrow, but is absent on pluripotent hematopoietic stem cells. The receptor binds ?2,3- and ?2,6-linked sialic acid residues present on N- and O-linked glycans on cell surfaces. CD33 serves as a critical immunophenotypic marker for peripheral blood monocytes and is employed diagnostically to differentiate myeloid leukemias from lymphoid and erythroid malignancies. It is also a clinically validated therapeutic target in acute myeloid leukemia (AML). Aberrant CD33 function or expression has been implicated in pathologies such as gallbladder lymphoma and extracutaneous mastocytoma.
CD34, a single chain transmembrane glycoprotein, is selectively expressed on human lymphoid and myeloid hematopoietic progenitor cells. Staining for CD34 has been used to measure angiogenesis, which reportedly predictstumor recurrence. CD34 functions as a cell-cell adhesion factor and cell-surface glycoprotein. It may also mediate the attachment of stem cells to bone marrow extracellular matrixes or directly to stromal cells. Cells expressing CD34 are normally found in the umbilical cord and bone marrow as hematopoietic cells, and in vascular endothelium.
CD34 (Cluster of Differentiation 34) is a single-pass, type I transmembrane glycoprotein that primarily functions as a cell?cell adhesion molecule. It is characteristically expressed during the stem/progenitor stages of lymphohematopoietic development, where it is thought to facilitate the attachment of hematopoietic stem cells to the bone marrow extracellular matrix and/or to stromal cells. CD34 expression is observed on hematopoietic stem and progenitor cells, vascular endothelial cells, fibroblasts, and various stromal elements. It serves as a critical marker for the quantification and isolation of hematopoietic progenitor and stem cell populations. Additionally, CD34 is valuable in the histopathological identification of neoplasms exhibiting endothelial or lymphoid differentiation and is an established immunohistochemical marker in the diagnosis of gastrointestinal stromal tumors.
CD35 (Complement Receptor 1; CR1) is a membrane-bound, monomeric glycoprotein that functions as a receptor for the complement components C3b and C4b, which are central to the complement cascade and critical for the clearance of immune complexes and opsonized pathogens. CD35 facilitates cellular adhesion to complement-activated particles and immune complexes, thereby enhancing their phagocytosis and subsequent removal. It exists as four allotypic variants?C (160 kDa), A (190 kDa), B (220 kDa), and D (250 kDa)?resulting from gene polymorphism and alternative splicing. Functionally, CD35 contributes to immune complex processing, enhances C3b-mediated binding and phagocytic uptake, and down regulates further complement activation. CD35 is expressed on neutrophils, eosinophil?s, monocytes, B lymphocytes, a subset of natural killer (NK) cells, erythrocytes, myeloid leukaemia?s, and follicular dendritic cells, but is absent from basophils. Reduced expression or mutations in the CR1 gene have been implicated in several pathologies, including gallbladder carcinoma, membranoproliferative glomerulonephritis (mesangiocapillary GN), systemic lupus erythematosus (SLE), and sarcoidosis. Additionally, genetic variants of CR1 associated with reduced rosetting of Plasmodium falciparum?infected erythrocytes confer protection against severe malaria. Multiple allele-specific splice variants encoding distinct isoforms have been identified, and a soluble isoform of CD35 has been reported, though it remains incompletely characterized.
CD38 is a multifunctional type II transmembrane glycoprotein and ectoenzyme involved in NAD? metabolism, generating second messengers like cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP) that regulate intracellular calcium signaling. It is expressed on various immune cells including B cells, T cells, NK cells, and monocytes, with dynamic expression during B cell development. CD38 also localizes to the nucleus, where it may influence calcium homeostasis. Functionally, it acts as an ADP-ribosyl cyclase, cADPR hydrolase, NAD? glycohydrolase, and signaling receptor, contributing to lymphocyte activation, proliferation, differentiation, adhesion, and apoptosis. The CD34?CD38? population defines primitive hematopoietic stem cells. Clinically, CD38 is used as a diagnostic and prognostic marker in hematologic malignancies such as multiple myeloma and chronic lymphocytic leukemia, and for monitoring HIV-1 progression. High CD38 expression is observed in tissues like the pancreas, liver, and kidney, as well as in malignant lymphoma and neuroblastoma.
CD38 is a glycoprotein present on the surface of various immune cells, including CD4+ and CD8+ T cells, B cells, and natural killer (NK) cells, serving as a marker of cell activation. This protein is associated with conditions such as HIV infection, leukemia, multiple myeloma, solid tumors, type II diabetes mellitus, and bone metabolism disorders, as well as some genetically-determined diseases. CD38 has particular significance as a prognostic marker in leukemia.
This protein is highly expressed in thymocytes and is also found in early-stage B and T lineage cells, NK cells, plasma cells, monocytes, and macrophages. CD38 expression can be detected in cells related to multiple myeloma, acute lymphoblastic leukemia (ALL, both B and T cell types), and some forms of acute myeloid leukemia (AML).
The expression of CD38 antibodies is valuable in differentiating subtypes of lymphomas and leukemias, inhibiting B-cell development, detecting plasma cells, protecting B cells from apoptosis, and identifying activated B and T-cell proliferation.
The epsilon-chain of CD3 is part of the CD3 complex, which consists of five distinct polypeptide chains gamma, delta, epsilon, zeta, and eta ranging in molecular weight from 16 to 28 kDa. This complex is tightly associated with the T cell antigen receptor (TCR) on the surface of lymphocytes. It plays a key role in transmitting signals into the T cell following antigen recognition. The CD3 antigen first appears in early thymocytes and is likely one of the earliest indicators of T cell lineage commitment. In cortical thymocytes, CD3 is mainly located within the cytoplasm, while in medullary thymocytes, it is expressed on the cell surface. CD3 is a highly specific T cell marker and is present in the majority of T cell neoplasms.
CD4 is a glycoprotein present on the surface of various immune cells, including T helper cells, monocytes, macrophages, and dendritic cells. It acts as a co-receptor, supporting the T-cell receptor (TCR) in its recognition of antigens presented by antigen-presenting cells.
CD4 also interacts with MHC class II molecules on these cells via its extracellular domain. Within lymphatic tissues, CD4+ T cells are predominantly found in the parafollicular zone, with fewer cells located in the germinal centres and mantle zone. Additionally, CD4 is expressed in hepatic sinusoidal cells and monocyte-derived cells, but not in B cells or immature thymocytes.
The expression of CD4 in precursor T-lymphoblastic lymphomas can vary. Most mature T-cell lymphomas are CD4 positive, except for aggressive NK-cell leukaemia and extra nodal NK/T-cell lymphoma. CD4 is an essential marker for identifying and classifying lymphocytes in both inflammatory conditions and malignant lymphomas.
CD4 is a cell-surface glycoprotein that serves as a co-receptor for the recognition of major histocompatibility complex (MHC) class II molecules and acts as an entry receptor for human immunodeficiency virus (HIV). Its expression is predominantly restricted to a subset of T lymphocytes known as T helper cells, but it is also present on other immune cell populations, including monocytes, macrophages, and dendritic cells. At the tissue level, CD4 is detectable in lymphoid organs such as the thymus, lymph nodes, tonsils, and spleen, as well as in discrete regions of the central nervous system, gastrointestinal tract, and other non-lymphoid sites. Functionally, CD4 contributes to the initiation and amplification of early T-cell activation by associating with the T-cell receptor (TCR) complex and the Src family protein tyrosine kinase Lck. Beyond its immunological role, CD4 has been implicated as a mediator of direct neuronal injury in certain infectious and immune-mediated disorders of the central nervous system. Multiple alternatively spliced transcript variants have been identified for the CD4 gene
CD4 is a glycoprotein present on the surface of various immune cells, including T helper cells, monocytes, macrophages, and dendritic cells. It acts as a co-receptor, supporting the T-cell receptor (TCR) in its recognition of antigens presented by antigen-presenting cells. CD4 also interacts with MHC class II molecules on these cells via its extracellular domain. Within lymphatic tissues, CD4+ T cells are predominantly found in the parafollicular zone, with fewer cells located in the germinal centers and mantle zone. Additionally, CD4 is expressed in hepatic sinusoidal cells and monocyte-derived cells, but not in B cells or immature thymocytes. The expression of CD4 in precursor T-lymphoblastic lymphomas can vary. Most mature T-cell lymphomas are CD4 positive, except for aggressive NK-cell leukemia and extranodal NK/T-cell lymphoma. CD4 is an essential marker for identifying and classifying lymphocytes in both inflammatory conditions and malignant lymphomas.
ITGA2B encodes CD41, or integrin alpha IIb. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain IIb undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibrinogen receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. In addition to adhesion, integrins are known to participate in cell-surface medicated signalling.
CD41 antibody expression has been found on platelets, megakaryocyes, and immature hematopoietic progenitors
CD43, also referred to as leukosialin or sialophorin, is a heavily glycosylated, mucin-like transmembrane protein distinguished by its highly anionic extracellular domain. It is broadly expressed across hematopoietic lineages, with the exception of quiescent B lymphocytes. CD43 exhibits both pro-adhesive and anti-adhesive properties, forming a steric and electrostatic barrier that can inhibit cell-cell interactions while also facilitating leukocyte aggregation under specific physiological conditions. It plays a role in the activation and functional regulation of T cells, B cells, natural killer (NK) cells, and monocytes. Upon cellular activation, CD43 expression is downregulated through proteolytic cleavage.
CD43 Antibody (DF-T1) is an IgG1 ? mouse monoclonal antibody that specifically targets the CD43 protein of human origin. This antibody can be utilized in various applications, including Western Blot (WB), Immunoprecipitation (IP), Immunofluorescence (IF), Immunohistochemistry on paraffin-embedded sections (IHC-P), and Flow Cytometry (FCM). The CD43 Antibody (DF-T1) is available in both non-conjugated and multiple conjugated forms, such as agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and several Alexa Fluor conjugates.
Over 100 cell surface markers have been identified using monoclonal antibodies. These markers are invaluable in distinguishing specific subpopulations of cells within mixed colonies. They have been systematically classified under the "cluster of differentiation" (CD) nomenclature. CD43 is a predominant O-glycosylated cell-surface sialoglycoprotein present on the membranes of leukocytes. As a member of the surface mucin family, it plays a pivotal role in cellular adhesion and tumor progression. Commonly referred to as leukosialin, CD43 is widely recognized as a marker for identifying normal and neoplastic T cells, as well as a subset of neoplastic B cells in tissues. Functionally, CD43 is believed to act as a negative regulator of cellular adhesion
CD44 is a 100 kDa type I transmembrane glycoprotein broadly expressed on leukocytes, central nervous system white matter, and epithelial cells of the intestine and breast. It serves as a primary receptor for hyaluronic acid (HA) and mediates cell adhesion, migration, and intercellular interactions. CD44 plays key roles in lymphocyte activation, trafficking, and homing. Its expression is up regulated in activated T and B lymphocytes, memory T cells, and bone marrow-derived myeloid cells. In epithelial cells, CD44 localizes to filopodia, suggesting involvement in cytoskeletal dynamics. The CD44 gene undergoes complex alternative splicing, generating numerous isoforms with distinct structural and functional characteristics; CD44H is the most prevalent in normal tissues. Certain splice variants are associated with tumor progression and metastasis, although the full-length nature of many variants remains undefined. CD44 dysregulation is implicated in diseases such as superficial keratitis and lichen sclerosus and is increasingly studied for its potential role in cancer metastasis.
CD45, also referred to as leukocyte common antigen (LCA), is a transmembrane protein tyrosine phosphatase (PTPase) expressed on the surface of nearly all hematopoietic lineage cells, including lymphocytes, granulocytes, monocytes, and macrophages, but absent in terminally differentiated erythrocytes and megakaryocytes. Immunohistochemical detection of CD45 serves as a frontline marker in establishing the hematopoietic origin of neoplastic proliferations. Although highly specific, rare instances of undifferentiated and neuroendocrine carcinomas exhibiting CD45 immunoreactivity have been documented.
CD45 leukocyte common antigen (LCA) belongs to the family of at least four isoforms of membrane glycoproteins (220, 205, 190, 180kDa) expressed on hematopoietic cell lines but absent on non-hematopoietic cell lines, normal, and malignant non-hematopoietic tissues. The intracellular portion of these molecules have protein phosphatase activity and are involved in regulation of transmembrane signals. Antibody to CD45 is useful in differential identification of lymphoid tumors from non-hematopoietic undifferentiated neoplasms.
The CD45 family comprises multiple isoforms derived from a single, complex gene. Among these, three principal isoforms are recognized: the B-lymphocyte-associated form, designated B220 (molecular mass: 220 kDa); the na?ve T-lymphocyte isoform, CD45RA; and the activated/memory T-lymphocyte isoform, CD45RO. CD45RO is a single-chain transmembrane glycoprotein representing the low?molecular weight variant of the Leukocyte Common Antigen (LCA). It is expressed on the majority of thymocytes, approximately 45% of peripheral blood T-lymphocytes, nearly all T-cells within cutaneous reactive infiltrates, and the predominant subset of T-cell neoplasms. Expression is also observed on a minor subset of B-lymphocytes and, infrequently, on certain B-cell lymphomas.
The CD45RO monoclonal antibody (T-cell, pan-specific) exhibits reactivity with thymocytes and activated T-lymphocytes, as well as with a defined subpopulation of resting T-cells. It demonstrates no reactivity toward B-lymphocytes, rendering it a reliable immunophenotypic marker for T-cell?derived malignancies. Additionally, this antibody labels granulocytes and monocytes.
CD5 is a transmembrane glycoprotein broadly expressed on the surface of nearly all mature human T lymphocytes, with the exception of approximately 10% of CD4-positive T cells that lack CD5 expression. In immature T-cell precursors (CD34-positive), CD5 is weakly expressed, with its expression increasing progressively during T-cell maturation. CD5 is also detected on a minor subset of normal human B lymphocytes, comprising roughly 20% of peripheral blood B cells and scattered cells within the mantle zones of lymph nodes.
Anti-CD5 is a pan T-cell marker that also binds to a variety of neoplastic B-cells. Its expression is valuable for distinguishing mature T-cell neoplasms and differentiating among mature small lymphoid cell malignancies. Anti-CD5 does not react with granulocytes or monocytes.
CD5 (Lymphocyte antigen T1/Leu-1) is a transmembrane glycoprotein involved in regulating T-cell proliferation. The CD5 antibody labels various T lymphocytes, mantle zone lymphocytes, and a small subset of B lymphocytes. In tumors, CD5 is expressed in T-cell malignancies, B-cell chronic lymphocytic leukemia (CLL)/small lymphocytic lymphoma (SLL), and mantle-cell lymphoma, making it a valuable diagnostic tool for these cancers. Additionally, anti-CD5 is useful in diagnosing thymic carcinoma, as it is CD5 positive.
CD56 or Neural-Cell Adhesion Molecule (NCAM) is a homophilic binding glycoprotein expressed on the surface of neurons, glia and skeletal muscle. CD56 has been implicated in cell-cell adhesion, neurite outgrowth, synaptic plasticity, and learning and memory. Normal cells that stain positively for CD56 include NK cells, activated T-cells, brain and cerebellum, and neuroendocrine tissues.
Tumors that are CD56-positive are Myeloma, Myeloid Leukemia, Neuroendocrine tumors, Wilm?s Tumor, Adult Neuroblastoma, NK/T cell Lymphomas, Pancreatic Acinar-cell Carcinoma, Pheochromocytoma, and Small-cell Lung Carcinoma. It is also expressed on some mesodermally-derived tumors (Rhabdomyosarcoma). Ewing?s Sarcoma/PNET is CD56-negative.
Anti-CD57 selectively identifies a subset of lymphocytes characterized as natural killer (NK) cells. Follicular centre cell lymphomas frequently demonstrate a notable infiltration of NK cells within the neoplastic follicular architecture. In addition to hematolymphoid applications, anti-CD57 also exhibits immunoreactivity with neuroendocrine cells and their associated neoplasms, such as carcinoid tumors and medulloblastomas. Furthermore, when utilized in conjunction with a broader immunohistochemical panel including GLUT1, CD5, and carcinoembryonic antigen (CEA), anti-CD57 can aid in the differential diagnosis between type B3 thymoma and thymic carcinoma.
Anti-CD57 marks a subset of lymphocytes known as natural killer (NK) cells. Follicular center cell lymphomas often contain many NK cells within the neoplastic follicles. Anti-CD57 also stains neuroendocrine cells and their derived tumors, including carcinoid tumor and medulloblastoma. Anti-CD57 can also be useful in separating type B3 thymoma from thymic carcinoma when combined with a panel that includes antibodies against GLUT1, CD5, and CEA.
CD61, also known as glycoprotein IIIa (GPIIIa) or integrin ?3 (ITGB3), is a 105 kDa transmembrane glycoprotein expressed on activated T lymphocytes, granulocytes, megakaryocytes, platelets, and their precursors. It plays a central role in platelet aggregation and hemostasis by functioning as a receptor for extracellular matrix proteins, including fibrinogen, fibronectin, von Willebrand factor, vitronectin, and thrombospondin. CD61 forms non-covalent heterodimeric complexes with various integrin ? subunits: it associates with integrin ?IIb (CD41) to form the fibrinogen receptor gpIIb/IIIa on platelets and with integrin ?V (CD51) to generate the vitronectin receptor on other cell types. These integrin complexes mediate cell adhesion and intracellular signaling by binding to matrix ligands. CD61 is prominently expressed on megakaryocytes and platelets (with CD41) and on endothelial cells, monocytes, and osteoclasts (with CD51). Dysregulation or deficiency of CD61 is implicated in disorders such as Glanzmann thrombasthenia and Platelet-type 16 bleeding disorder, emphasizing its critical role in thrombosis and vascular integrity.
CD68 antigen is a 110-kD type 1 membrane glycoprotein that appears in endosomes or lysosomes (long variant) and to a lesser extent on the cell surface (short variant). It is highly expressed by blood monocytes and tissue macrophages. It is also reported to be expressed in immature myeloid cells, lymphoma, many tumor cell lines, and some epithelial tumors, although the labeling is usually less intense than in macrophages. Clone KP1 reacts strongly with a fixativeresistant epitope of CD68 protein that is expressed by virtually all macrophages of the human body. The CD68 antibody can be used as part of a panel in the evaluation of poorly differentiated neoplasms in cytological materials.
CD7 antigen is a 40-kDa cell surface glycoprotein that is a member of the immunoglobulin gene superfamily. While its precise function is not known, it is suggested that CD7 plays a role in T-cell interactions as it is one of the earliest T-cell lineage associated antigens expressed during T-cell ontogeny. CD7 is expressed in thymocytes, mature peripheral T-cells, natural killer cells, and lymphoid and myeloid progenitors.
The CD7 Antibody is validated for use in immunohistochemistry on paraffin-embedded tissues (IHC-P), and flow cytometry (FCM). The antibody is available in unconjugated form as well as conjugated to multiple labels such as agarose, horseradish peroxidase (HRP), phycoerythrin (PE) and fluorescein isothiocyanate (FITC).
CD7, a type I transmembrane glycoprotein, is predominantly expressed on pluripotent hematopoietic progenitor cells, the majority of thymocytes, and a subset of peripheral T lymphocytes. It plays a pivotal role in T cell activation, particularly in T cell subsets, and is considered essential in immune regulation.
CD7 is commonly used as a diagnostic marker in hematologic malignancies, including T-cell acute lymphoblastic leukemia and leukemias of pluripotent stem cell origin. Its expression is frequently down regulated in CD8+ T cells from individuals with chronic viral infections and is also diminished during acute immune responses, such as in infectious mononucleosis, reflecting its modulation under pathological immune conditions.
Transferrin receptor 1 (CD71) is expressed in placental syncytiotrophoblasts, myocytes, basal keratinocytes, hepatocytes, endocrine pancreatic cells, spermatocytes, and erythroid precursors. Its expression is most prominent in early erythroid precursors, persists through the intermediate normoblast stage, and gradually diminishes during reticulocyte maturation, becoming absent in mature erythrocytes. Anti-CD71 serves as a highly effective immunohistochemical marker for evaluating erythroid precursors within bone marrow biopsy specimens, characterized by a distinct membranous and cytoplasmic staining pattern, specificity for the erythroid lineage, and a maturation-dependent decline in expression, with maximal levels in early erythroid forms, reduced intensity in late normoblasts, and complete absence in fully mature erythrocytes.
CD74, also referred to as the MHC class II?associated invariant chain (Ii), is a type II transmembrane glycoprotein that associates with newly synthesized MHC class II ?/? heterodimers, occupying the peptide-binding groove and preventing premature loading with endogenous peptides. Its expression is predominantly restricted to professional antigen-presenting cells, including B lymphocytes (from the pre-B stage through to pre?plasma cell differentiation), monocytes, macrophages, and subsets of epithelial cells.
Immunohistochemically, anti-CD74 demonstrates strong labeling of germinal center B lymphocytes and B-cell lymphomas, with infrequent staining of T-cell lymphomas. The antibody shows both membranous reactivity and characteristic paranuclear globular staining, corresponding to the Golgi region. Diagnostic applications of CD74 include distinguishing atypical fibroxanthoma from malignant fibrous histiocytoma, as well as discriminating small-cell lung carcinoma from non?small cell lung carcinoma.
D79a is a protein non-covalently associated with membrane- bound immunoglobulins on B-cells, forming part of the B-cell antigen receptor complex. CD79a expression begins at the pre-B- cell stage and continues through to the plasma cell stage, where it becomes an intracellular component. It is commonly found in the majority of precursor B-cell type acute leukemias, in B-cell lines, B-cell lymphomas, and certain cases of myelomas. The CD79a antibody is a B-cell marker often used in conjunction with CD20. While it stains many of the same lymphomas as CD20, CD79a has broader staining for B-precursor lymphoid leukemias and is more frequently positive in plasma cell myelomas. Additionally, CD79a occasionally stains certain endothelial cells. It can also stain many cases of acute promyelocytic leukemia (FAB- M3), though it rarely stains other types of myeloid leukemia.
CD79 is a heterodimeric complex composed of two transmembrane proteins: CD79a (also known as mb-1) and CD79b (also referred to as B29). CD79a is associated with the Ig-? chain, while CD79b associates with the Ig-? chain of the B-cell antigen receptor (BCR) complex. The expression of CD79 occurs prior to immunoglobulin (Ig) heavy-chain gene rearrangement and precedes the expression of CD20. In early B-cell development, specifically in precursor B cells, CD79a and CD79b are detectable within the cytoplasm (cytoplasmic CD79, or CyCD79). Membranous expression of CD79 initiates at the pro-B cell stage and is maintained throughout all subsequent stages of B-cell maturation, including terminal differentiation into plasma cells. CD79a serves as a highly reliable immunophenotypic marker for the detection of both normal and neoplastic B-cell populations. The specificity and utility of the CD79a antibody have been validated by the 9th International Workshop on Human Leukocyte Differentiation Antigens (HLDA9).
CD8 (Cluster of Differentiation 8) is a transmembrane glycoprotein that serves as a co-receptor for the T-cell receptor (TCR), enhancing antigen recognition in conjunction with major histocompatibility complex (MHC) class I molecules. The CD8 complex is typically composed of ? and ? chains that form a disulfide-linked heterodimer and is predominantly expressed on the surface of cytotoxic T lymphocytes (CTLs). In addition, CD8 expression is also observed on subsets of natural killer (NK) cells, cortical thymocytes, and dendritic cells.
CD8+ cytotoxic T lymphocytes are key effectors of the adaptive immune response and play a critical role in immunosurveillance, particularly in the recognition and elimination of malignant or virally infected cells. Engagement of the CD8 co-receptor with MHC class I molecules enhances TCR sensitivity by approximately 100-fold, thereby promoting effective antigen-specific responses.
CD8 is frequently expressed in T-cell large granular lymphocytic (T-LGL) leukemia and may be co-expressed with CD4 in certain cases of T-lymphoblastic lymphoma.
Clinically, the presence of intratumoral CD8+ T cells termed tumor-infiltrating lymphocytes (TILs) has been associated with favorable prognosis and improved overall survival across multiple malignancies, including colorectal, ovarian, esophageal, renal, pulmonary, and pancreatic carcinomas. Moreover, an elevated CD8+/CD4+ T-cell ratio has been correlated with enhanced survival outcomes, particularly in colorectal and ovarian cancer patients
CD8 is a cell surface receptor that exists either as a heterodimer with the CD8 beta chain (CD8 alpha/beta) or as a homodimer (CD8 alpha/alpha). It is expressed on the surface of most thymocytes and a subset of mature T cells and NK cells. CD8 binds to MHC class I molecules and, through its association with the protein tyrosine kinase p56lck, plays a crucial role in T cell development and in the activation of mature T cells. In mature T cells, CD4 and CD8 expression are generally mutually exclusive, so anti-CD8 is often used alongside anti-CD4 to distinguish between different T cell populations.
CD8 is a valuable marker for differentiating helper/inducer T-lymphocytes, with most peripheral T-cell lymphomas presenting as CD4+/CD8-. Anaplastic large cell lymphoma typically shows CD4+ and CD8- expression, whereas T-lymphoblastic lymphoma/leukemia often co-expresses both CD4 and CD8. CD8 can also be found in the littoral cell angioma of the spleen.
CD8 is a cell surface receptor that exists either as a heterodimer with the CD8 beta chain (CD8 alpha/beta) or as a homodimer (CD8 alpha/alpha). It is expressed on the surface of most thymocytes and a subset of mature T cells and NK cells. CD8 binds to MHC class I molecules and, through its association with the protein tyrosine kinase p56lck, plays a crucial role in T cell development and in the activation of mature T cells. In mature T cells, CD4 and CD8 expression are generally mutually exclusive, so anti-CD8 is often used alongside anti-CD4 to distinguish between different T cell populations.
CD8 is a valuable marker for differentiating helper/inducer T-lymphocytes, with most peripheral T-cell lymphomas presenting as CD4+/CD8-. Anaplastic large cell lymphoma typically shows CD4+ and CD8- expression, whereas T-lymphoblastic lymphoma/leukemia often co-expresses both CD4 and CD8. CD8 can also be found in the littoral cell angioma of the spleen
Thy-1, also designated CD90 (Cluster of Differentiation 90), is a conserved 25?37 kDa cell surface glycoprotein that is heavily N-glycosylated and anchored via a glycosylphosphatidylinositol (GPI) linkage. It contains a single V-like immunoglobulin domain and was originally identified as a thymocyte antigen. CD90 is expressed across multiple cell types, including thymocytes, neurons, glial cells, endothelial cells, fibroblasts, fetal liver cells, and hematopoietic stem cells within normal bone marrow and umbilical cord blood. Functionally, Thy-1 has been widely employed as a marker for diverse stem cell populations as well as for axonal projections in differentiated neurons. Clinically, CD90 expression is associated with adverse prognostic and biological features in acute myeloid leukemia. In prostate cancer, CD90 is significantly upregulated in cancer-associated fibroblasts and is recognized as a marker of tumor-associated stroma.
CD95 (Fas) is a cell surface receptor of the tumor necrosis factor (TNF) receptor superfamily that mediates apoptotic signaling upon engagement with its cognate ligand, Fas ligand (CD95L). CD95L exists either as a membrane-bound trimeric form or as a soluble isoform generated by proteolytic cleavage via a putative metalloproteinase. CD95 is broadly expressed across diverse cell types. Activation of the CD95 signaling pathway induces programmed cell death, a process critical for the preservation of tissue homeostasis. Dysregulation of this apoptotic mechanism has been implicated in the pathogenesis of autoimmune disorders, lymph proliferative syndromes, and various malignancies. Moreover, the CD95 death pathway contributes to apoptosis induced by ionizing radiation, chemotherapeutic agents, and viral infections. Expression levels of CD95 have prognostic relevance, serving as a biomarker for disease progression and therapeutic response in multiple tumor types.
The CD99 antigen is a 32 kD T-cell surface glycoprotein, also referred to as MIC2, E2, 12E7, HuLy-m6, or FMC29. Research indicates that CD99 is present on the cell membranes of certain lymphocytes, cortical thymocytes, and granulosa cells in the ovary. It is also expressed in most pancreatic islet cells, Sertoli cells of the testis, and certain endothelial cells. In contrast, mature granulocytes show minimal or no expression of CD99. Notably, engagement of specific epitopes on CD99 can quickly induce T-cell death through a unique caspase-independent pathway.
CD99 is a highly specific surface marker for Ewing?s sarcoma and primitive peripheral neuroectodermal tumors, making it valuable in identifying these malignancies and distinguishing them from other small blue cell tumors.
Recognizes a sialoglycoprotein of 27-32 kDa, identified as CD99, the MIC2 gene product, or E2 antigen. The MIC2 gene is located in the pseudo-autosomal region of the human X and Y chromosomes. It encodes two distinct proteins produced by alternative splicing of the CD99 gene transcript, identified as bands of 30 and 32 kDa (p30/32). Although its function is not fully understood, CD99 is implicated in various cellular processes, including homotypic aggregation of T cells, upregulation of T cell receptor and MHC molecules, apoptosis of immature thymocytes, and leukocyte diapedesis. CD99 is expressed on the cell membrane of some lymphocytes, cortical thymocytes, and granulosa cells of the ovary. It is also expressed in most pancreatic islet cells, Sertoli cells of the testis, and some endothelial cells, whereas mature granulocytes express very little or no CD99. MIC2 is strongly expressed on Ewing's sarcoma cells and primitive peripheral neuroectodermal tumors. This monoclonal antibody shows very similar reactivity to other CD99 MAbs (e.g., O13, 12E7, or HBA-71) and is excellent for immunohistochemical staining of formalin-fixed, paraffin-embedded tissues.
The CDH17 gene encodes a member of the cadherin superfamily, a group of calcium-dependent, membrane-associated glycoproteins involved in cell?cell adhesion. The CDH17 protein is cadherin-like in structure, characterized by an extracellular domain comprising seven tandem cadherin repeats and a single transmembrane domain, but notably lacks the conserved cytoplasmic domain typical of classical cadherins. CDH17 is predominantly expressed in the gastrointestinal tract and pancreatic ducts, where it functions as a proton-dependent oligopeptide transporter, facilitating the initial uptake of peptide-based therapeutics during oral absorption. In addition to its transport function, CDH17 is implicated in maintaining epithelial architecture and contributing to the morphological organization of the liver and intestine. Multiple transcript variants resulting from alternative splicing have been identified, encoding distinct isoforms with potential functional variability.
Cyclin-dependent kinase 4 (CDK4) is a member of the serine/threonine protein kinase family and serves as the catalytic subunit of a kinase complex that plays a pivotal role in regulating the G1 phase of the cell cycle. Its enzymatic activity is confined to the G1-S phase transition and is modulated by association with D-type cyclins and negatively regulated by the cyclin-dependent kinase inhibitor p16^INK4a^. Immunohistochemical overexpression of CDK4 has been documented across a broad spectrum of malignancies, including oral squamous cell carcinoma and neoplasms of the pancreas (particularly pancreatic endocrine tumors), lung, breast, and colon. CDK4 expression has been positively correlated with tumor progression and increased proliferative capacity. Binh et al. reported high CDK4 expression (92%) in atypical lipomatous tumors/well-differentiated liposarcomas (ALT-WDLPS) and dedifferentiated liposarcomas (DDLPS). CDK4 immunoreactivity is diagnostically valuable in distinguishing ALT-WDLPS from benign lipomatous neoplasms and in differentiating DDLPS from other poorly differentiated sarcomas.
Cyclin-dependent kinase-4 (CDK4) is a protein-serine kinase involved in the cell cycle. It is essential for the G1- to S-phase transition during the cell cycle and its expression is primarily controlled at the transcriptional level .
CCND1- CDK4 axis is not only critical in glial tumor cells but also in stromal-derived cells in the surrounding tumor microenvironment that are vital to sustain tumor outgrowth CDK4 is highly expressed in highly differentiated and dedifferentiated liposarcomas, but rarely expressed in other benign liposarcomas and other sarcomas. CDK4 and MDM2 combined to differentiate between highly differentiated liposarcoma (+), dedifferentiated liposarcoma (+) and myxoid liposarcoma, pleomorphic liposarcoma, spindle lipoma, pleomorphic lipoma and other high-grade sarcomas
CDX2 is a caudal-type homeobox gene that encodes an intestine-specific transcription factor expressed early in intestinal development and that may be involved in the regulation of proliferation and differentiation of intestinal epithelial cells. It is expressed in the nuclei of epithelial cells throughout the intestine, from duodenum to rectum. The CDX2 protein is expressed in Primary and Metastatic Colorectal Carcinomas and has also been demonstrated in the intestinal metaplasia of the stomach and intestinal-type gastric cancer.
It is not expressed in the normal gastric mucosa. Loss of CDX2 protein expression has been correlated with loss of differentiation in colorectal cancers. Anti-CDX2 antibody has been useful in distinguishing the gastrointestinal origin of Metastatic Adenocarcinomas and carcinoids. Studies have shown that CDX2 is a superior marker compared to CK20. A high percentage of Mucinous Carcinomas of the Ovary also stain positively with this antibody, as well as Carcinomas from the upper gastrointestinal tract.
CDX2 is an intestine-specific transcription factor belonging to the caudal-related home box gene family, critically involved in regulating proliferation, differentiation, and maintenance of intestinal epithelial cell identity. It plays a key role in promoting the differentiation of precursor cells into mature villus enterocytes. The monoclonal antibody clone CDX2-88 targets a conserved epitope of the 40 kDa CDX2 protein, which is localized to the cell nucleus. This antibody exhibits nuclear immunoreactivity specific to colonic epithelial cells and colorectal adenocarcinomas in formalin-fixed, paraffin-embedded tissue specimens, making it a reliable marker for gastrointestinal origin in diagnostic pathology.
Carcinoembryonic Antigen (CEA) is found in several adenocarcinomas, such as colon, lung, breast, stomach and pancreas. Malignant mesothelioma is usually negative for CEA.
The antibody is a useful tool for the identification of colon carcinomas, and for the distinction of mesothelioma from adenocarcinoma when used with a panel of antibodies
Carcinoembryonic antigen (CEA) is a glycoprotein involved in cell adhesion. It is normally produced during fetal development, but the production of CEA stops before birth. Therefore, it is not usually present in the blood of healthy adults, although levels are raised in heavy smokers. CEA is synthesized during development in the fetal gut, and is re-expressed in increased amounts in Intestinal Carcinomas and several other tumors. CEA is employed essentially as a tool to assist in the distinction between Adenocarcinoma and Malignant Mesotheliomas of the epithelial type, along with other markers for mucosubstances such as Leu M1 and Ber-EP4. Another suggested use of CEA is the immunophenotyping of various Metastatic Adenocarcinomas as a means of identifying their origin.
Chromogranin A is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. Examples of cells producing chromogranin A are the adrenal medulla, enterochromaffin-like cells and beta cells of the pancreas. The function of chromogranin A is unknown but it is a precursor to 3 functional peptides: vasostatin, pancreastatin and parastatin. These peptides negatively modulate the neuroendocrine function of the releasing cell (autocrine) or nearby cells (paracrine). Chromogranin A is an excellent marker for Carcinoid Tumors, Pheochromocytomas, Paragangliomas, and other Neuroendocrine Tumors. Coexpression of chromogranin A and neuron-specific enolase (NSE) is common in neuroendocrine neoplasms. It has been identified in a wide variety of endocrine tissues including the pituitary, pancreas, hypothalamus, thymus, thyroid, intestine and parathyroid. It is generally accepted that the coexpression of certain keratins and chromogranin means neuroendocrine lineage. The presence of strong chromogranin staining and absence of keratin staining should raise the possibility of paraganglioma. Most pituitary adenomas and prolactinomas readily express chromogranin.
Claudin-4 is a member of the tight-junction-associated protein family, primarily expressed in most epithelial cells but not in mesothelial cells.
Immunohistochemical (IHC) detection of Claudin-4 is a valuable diagnostic tool for distinguishing lung adenocarcinoma from malignant mesothelioma in tissue samples. In malignant effusions, Claudin-4 detection demonstrates high sensitivity and specificity in identifying adenocarcinoma as opposed to malignant mesothelioma. Additionally, studies have indicated that Claudin-4 serves as an independent positive prognostic factor in gastric carcinoma. Its expression restricts gastric cancer cell migration, and its overexpression?linked to epigenetic derepression?suppresses cancer progression, contributing to improved patient prognosis.
Conversely, Claudin-4 expression is downregulated in certain epithelial malignancies and precancerous lesions. It also plays a significant role in tumor cell invasion and metastasis. Importantly, Claudin-4 is a highly specific and sensitive marker for differentiating epithelioid mesotheliomas from metastatic carcinomas
This gene encodes a member of the claudin family, a group of integral membrane proteins that constitute essential components of tight junction strands. Tight junctions function as selective barriers, restricting the unregulated passage of solutes and water across the paracellular space between epithelial and endothelial cell layers, while also contributing to the maintenance of cell polarity and the regulation of intracellular signaling pathways. Expression of this gene is upregulated in individuals with ulcerative colitis and markedly overexpressed in infiltrating ductal adenocarcinomas. In gastric epithelial cells, its transcriptional regulation occurs through the PKC/MAPK/AP-1 (protein kinase C/mitogen-activated protein kinase/activator protein-1) signaling cascade. Additionally, alternative splicing generates multiple transcript variants that encode distinct isoforms.
Clusterin (apolipoprotein J) is a 75?80 kDa disulfide-linked heterodimeric glycoprotein implicated in apoptotic regulation and the clearance of cellular debris. It functions as a stress-inducible, cytoprotective molecular chaperone under the transcriptional control of heat shock factor 1 (HSF1), exhibiting functional parallels to small heat-shock proteins. Clusterin demonstrates broad tissue and fluid distribution, being detectable in epithelial cells, plasma, cerebrospinal fluid, breast milk, semen, and urine. Aberrant expression has been reported across a spectrum of hematopoietic and non-hematopoietic neoplasms, with particularly high prevalence (80?100%) in systemic anaplastic large cell lymphomas. Immunohistochemical inclusion of clusterin in diagnostic panels enhances differentiation between systemic anaplastic large cell lymphoma and classical Hodgkin lymphoma. Furthermore, Grogg et al., in a cohort of 202 spindle cell tumors, demonstrated that clusterin exhibits high sensitivity and specificity for follicular dendritic cell tumors. Clinically, clusterin overexpression correlates with adverse outcomes, including poor prognosis and recurrence in breast carcinoma, while in cervical carcinoma its expression is associated with chemosensitivity yet predictive of unfavourable survival.
Collagen type IV is a structural protein that constitutes a fundamental component of basement membranes across multiple tissues, including kidney, lung, and skin. Unlike fibrillar collagens, collagen IV assembles into a sheet-like network that provides mechanical stability, tensile strength, and structural support to the overlying cellular layers. It is composed of heterotrimers formed by three ?-chains encoded primarily by the COL4A1, COL4A2, and COL4A3 genes. Pathogenic variants in collagen IV genes are associated with inherited basement membrane disorders, notably Alport syndrome, characterized by progressive renal dysfunction and sensorineural hearing loss, and Goodpasture syndrome, an autoimmune disease targeting basement membranes of renal glomeruli and pulmonary alveoli.
Prostaglandins are a diverse group of autocrine and paracrine hormones that mediate many cellular and physiologic processes. Prostaglandin H2 (PGH2) is an intermediate molecule in formation of the prostaglandins.
Cyclooxygenase-1 (Cox-1) and cyclooxygenase-2 (Cox-2) are prostaglandin synthases that catalyze the formation of PGH2 from arachidonic acid (AA). Cox-1 and Cox-2 are isozymes of prostaglandin-endoperoxidase synthase (PTGS). Cox-1 is constitutively expressed in most tissues and is thought to serve in general housekeeping functions.
Cox-2 is efficiently induced in migratory cells responding to pro-inflammatory stimuli and is considered to be an important mediator of inflammation. Both enzymes are targets for the nonsteroidal therapeutic anti-inflammatory drugs, NSAIDs. COX2 expression is significantly increased in 85-90% of human colorectal adenocarcinomas whereas levels of COX-1 are not changed.
Cyclin D1, a key regulator of the cell cycle, is a putative proto-oncogene that is overexpressed in numerous human neoplasms. Cyclins are essential proteins that control the progression through specific phases of the cell cycle by modulating the activity of cyclin-dependent kinases (CDKs).
During the mid-to-late G1 phase, cyclin D1 expression peaks in response to growth factor stimulation. Anti-cyclin D1 antibodies have proven effective in research and hold promise as tools for advancing studies in cell cycle biology and cancer-related abnormalities. These antibodies are particularly valuable for distinguishing mantle cell lymphomas (cyclin D1-positive) from other lymphoproliferative disorders, such as chronic lymphocytic leukemia/small lymphocytic lymphoma and follicular lymphomas (both cyclin D1-negative). Additionally, cyclin D1 may show weak expression in hairy cell leukemia and plasma cell myeloma.
The antibody recognizes a 36 kDa protein identified as cyclin D1, which is a crucial regulator of the cell cycle and a putative protooncogene often overexpressed in various human cancers. It neutralizes cyclin D1 activity in vivo. Approximately 60% of mantle cell lymphomas (MCL) exhibit a t(11;14)(q13;q32) translocation, leading to cyclin D1 overexpression. This antibody is useful for distinguishing mantle cell lymphomas (cyclin D1 positive) from chronic lymphocytic leukemia/small lymphocytic lymphoma (CLL/SLL) and follicular lymphomas (both cyclin D1 negative). Occasionally, cyclin D1 is weakly expressed in hairy cell leukemia and plasma cell myeloma
Cyclin E is a member of the highly conserved cyclin family, defined by oscillatory protein expression patterns that regulate cell-cycle progression. Cyclins function as essential activators of cyclin-dependent kinases (CDKs), with each subtype displaying distinct expression and degradation dynamics that ensure temporal coordination of mitotic events. Cyclin E associates with CDK2 to form an active kinase complex required for the G1/S transition. Its expression peaks at the G1/S boundary and undergoes proteolytic degradation during S phase. Aberrant overexpression of Cyclin E has been documented in multiple malignancies, where it contributes to chromosomal instability and oncogenesis. Cyclin E also interacts with and phosphorylates NPAT (nuclear protein at the ATM locus), a key regulator of histone gene transcription, and thereby promoting cell-cycle progression independent of retinoblastoma protein (pRB) control. The CCNE1 gene gives rise to at least two well-characterized alternatively spliced isoforms, with additional putative splice variants reported but not fully characterized at the nucleotide level.
Cytokeratin 34?E12 is a High Molecular Weight cytokeratin that reacts with all squamous and ductal epithelium and stains carcinomas. This antibody recognizes cytokeratins 1, 5, 10, and 14 that are found in complex epithelia. Cytokeratin 34?E12 shows no reactivity with hepatocytes, pancreatic acinar cells, proximal renal tubules or endometrial glands; there has been no reactivity with cells derived from simple epithelia. Nerve cells, glial cells and mesenchymal tissue such as blood vessels containing only non-keratin types of intermediate filaments are not labeled; however, reactivity with smooth-muscle cells has been occasionally observed. Mesenchymal Tumors, Lymphomas, Melanomas, Neural Tumors and Neuroendocrine Tumors are unreactive with this antibody. Cytokeratin 34?E12 has been shown to be useful in distinguishing Prostatic Adenocarcinoma from Hyperplasia of the Prostate.
Cytokeratin 10 (CK10) is a type I intermediate filament protein that typically forms heterodimers with cytokeratin 1 (CK1). Its expression is predominantly localized to the suprabasal layers of stratified epithelia, particularly within the epidermis. CK10 serves as a marker of epidermal differentiation and is widely utilized in diagnostic pathology. Immunodetection of CK10 is especially valuable for distinguishing well-differentiated squamous cell carcinomas, where its presence reflects the degree of epithelial maturation.
Keratin proteins constitute a highly conserved family of structural proteins that form intermediate filaments within epithelial cells, existing as obligate pairs of acidic and basic isoforms. Cytokeratin 13 (CK13), a major acidic keratin, heterodimerizes with its basic counterpart CK4 and is predominantly expressed in the suprabasal layers of non-keratinized stratified epithelia, including the mucosa of the tongue, esophagus, anal canal, trachea, uterine cervix, and urothelium. CK13 serves as a reliable marker for non-keratinized squamous epithelium. Its expression is retained in squamous metaplasia but is significantly downregulated in squamous dysplasia and squamous cell carcinoma
Cytokeratins (CKs) are intermediate filament proteins characteristic of epithelial cells, found in both keratinizing epithelia (e.g., epidermis) and non-keratinizing epithelia (e.g., mesothelial linings). More than 20 distinct cytokeratin isoforms have been identified, classified into two major biochemical groups: type I (acidic) and type II (basic to neutral) polypeptides. Keratin 14, a type I low molecular weight cytokeratin, co-expressed with keratin 5 (a type II keratin), is a specific marker of stratified epithelial cells and serves to distinguish them from simple epithelial phenotypes. Keratin 14 is particularly valuable in the histopathological identification of squamous cell carcinomas and is also considered a prognostic biomarker in breast carcinoma. All epithelial cells express at least one acidic (type I) and one basic (type II) cytokeratin, which together form heterodimeric filaments essential for cytoskeletal integrity and epithelial differentiation
Keratins constitute a large family of intermediate filament proteins that polymerize into filaments by heterodimerization of type I (keratins 9?23) and type II (keratins 1?8) subunits. Their expression is tightly regulated in a tissue- and differentiation-specific manner. Keratin 15 (K15) is a type I keratin uniquely expressed in basal keratinocytes of stratified epithelia and, unlike other type I keratins, lacks a defined type II partner. Its expression is down regulated upon keratinocyte activation. Cytokeratin 15 is recognized as a specific marker of hair follicle bulge stem cells and has diagnostic utility in distinguishing basal cell carcinoma (BCC) from trichoepithelioma. Trichoblastomas, benign neoplasms demonstrating follicular differentiation and frequently arising within nevus sebaceous, often display overlapping morphologic features with nodular BCC, complicating histopathological differentiation. Variable expression of cytokeratin 15 and cytokeratin 19, along with the absence of hair keratins, provides an immunohistochemical adjunct in resolving this diagnostic challenge.
Cytokeratins constitute a family of intermediate filament proteins that assemble into filaments through heterodimerization of one type I cytokeratin (CK9?CK23) with one type II cytokeratin (CK1?CK8). These proteins are essential for epithelial cell differentiation, tissue specialization, and the preservation of structural integrity. In diagnostic pathology, cytokeratins serve as valuable markers for determining the cellular origin of metastatic neoplasms. Cytokeratin 16 (CK16) demonstrates expression in benign stratified squamous epithelium, squamous cell carcinomas of the head and neck, as well as in luminal cells of the mammary gland and sweat ducts. Notably, CK16 is absent in normal breast tissue and non-invasive breast carcinomas
Cytokeratin 17 (CK17) is a 46 kDa intermediate filament protein expressed in simple epithelial tissues and serves as a biomarker for cervical reserve (stem) cells. CK17 is valuable in the histopathological evaluation of uterine cervical squamous epithelial lesions, including atypical immature squamous metaplasia, cervical intraepithelial neoplasia (CIN), and invasive cervical squamous cell carcinoma. Additionally, CK17 expression aids in the differential diagnosis of oral squamous cell carcinoma.
Cytokeratin 17 (CK17) is typically found in the basal cells of complex epithelia, but not in stratified or simple epithelia. The CK17 antibody is an excellent tool for distinguishing myoepithelial cells from luminal epithelial cells in various glands, such as mammary, sweat, and salivary glands. CK17 is expressed in epithelial cells of various origins, including bronchial epithelial cells and skin appendages, and it may be considered an epithelial stem cell marker because CK17 antibodies highlight basal cell differentiation. CK17 expression is significantly higher in small cell lung carcinoma (SCLC) compared to lung adenocarcinoma (LADC). Furthermore, 85% of triple-negative breast carcinomas exhibit immunoreactivity to basal cytokeratins, including anti-CK17. Notably, cases of triple-negative breast carcinoma expressing CK17 tend to have an aggressive clinical course. Additionally, CK17 and MUC1 immunoreactivity is indicative of the pancreatobiliary subtype, while MUC2 and CDX-2 positivity characterizes the intestinal subtype
Cytokeratin 18 (CK18; also referred to as Keratin 18, KRT18, or type I cytoskeletal keratin 18) is a member of the type I (acidic) subfamily of low-molecular-weight keratins and typically forms heterodimers with cytokeratin 8. CK18 is expressed in epithelial cells of the gastrointestinal, respiratory, and urogenital tracts, as well as in endocrine and exocrine tissues and mesothelial cells. Its distribution is largely restricted to non-squamous epithelia, where it is consistently detected in the majority of adenocarcinomas and ductal carcinomas, but is characteristically absent in squamous cell carcinomas. Hepatocellular carcinomas demonstrate expression restricted to cytokeratins 8 and 18. Pathogenic variants in the KRT18 gene have been associated with cryptogenic cirrhosis. Two transcript isoforms encoding an identical CK18 protein have been identified. Cytokeratin expression profiling serves as an increasingly valuable tool for distinguishing subtypes of epithelial malignancies. Antibodies against CK18, applied in immunohistochemistry, cytopathology, and flow cytometric analyses, are widely utilized in the differential diagnosis of tumors and in the characterization of epithelial lineage.
Cytokeratin 18 (CK18), a member of the type A (acidic) subfamily of low molecular weight keratins, typically pairs with CK8. Tissues from the gastrointestinal tract express both CK8 and CK18, but lack CK14. CK18 is present in tissues from the gastrointestinal, respiratory, and urogenital tracts, as well as in endocrine and exocrine tissues, and in mesothelial cells. The antibody DC10 specifically recognizes various simple epithelial tissues, including glandular epithelium, but does not react with stratified squamous epithelia.
Cytokeratin 19 (CK19) is a type I intermediate filament protein predominantly expressed in both simple and non-keratinizing stratified epithelial tissues during embryogenesis and in adult epithelial structures. It represents the smallest member of the keratin family and is unique among keratins due to its lack of an obligate type II keratin pairing partner for filament formation, suggesting a distinct regulatory mechanism governing its expression. CK19 is a valuable immunohistochemical marker for epithelial-derived neoplasms. It is particularly useful in the differential diagnosis of hepatic tumors, aiding in the distinction between hepatocellular carcinoma (typically CK19-negative) and cholangiocarcinoma0 or metastatic adenocarcinomas to the liver (generally CK19-positive).
Anti-cytokeratin 19 (CK19) demonstrates immunoreactivity with both simple and stratified epithelia, encompassing glandular and ductal linings of organs such as the gastrointestinal tract and breast, as well as squamous epithelium. CK19 expression is frequently observed in a wide spectrum of carcinomas, including those originating from the colon, stomach, pancreas, biliary system, liver, and breast.? Immunohistochemical detection of CK19 has been applied in the diagnostic evaluation of hepatic neoplasms? and serves as a useful marker in the identification of papillary thyroid carcinoma
Cytokeratin 20 (CK20) is a 46 kDa type I intermediate filament protein with a restricted expression profile, predominantly localized to gastric and intestinal epithelium, urothelium, and Merkel cells. It represents a major structural protein of mature enterocytes and goblet cells within the gastric and intestinal mucosa.
Immunohistochemical detection of CK20 is characteristic of adenocarcinomas arising in the colon, stomach, pancreas, and biliary tract. CK20 expression is also observed in mucinous ovarian neoplasms, transitional cell carcinomas of the urinary tract, and Merkel cell carcinomas. By contrast, CK20 is essentially absent in squamous cell carcinomas, adenocarcinomas of the breast, lung, and endometrium, non-mucinous ovarian tumors, and small-cell carcinomas.
Owing to its distinct expression pattern, CK20 is widely utilized as a diagnostic marker for the characterization and differentiation of simple epithelial cell populations in the urinary tract as well as benign and malignant epithelial lesions. Furthermore, CK20 immunoreactivity is commonly assessed in combination with CK7 and additional markers to aid in distinguishing colorectal carcinomas (CK20-positive) from carcinomas of ovarian, pulmonary, and mammary origin.
Cytokeratin 20 (CK20) is a type-1 keratin which is primarily expressed in gastric and intestinal epithelium, urothelium, and Merkel-cells. CK20 is expressed in adenocarcinomas of the colon, stomach, pancreas and the bile system.
CK20 is also present in mucinous ovarian tumors, transitional-cell and Merkel-cell carcinomas. Notably, the squamous cell carcinomas and adenocarcinomas of the breast, lung, and endometrium, non-mucinous tumors of the ovary, and small cell carcinomas lack in CK20.
This monoclonal antibody recognizes a 58 kDa protein identified as Cytokeratin 5 (KRT5), a type II cytokeratin co-expressed with KRT14 in the basal layer of the epidermis. Antibodies against KRT5 selectively label basal cells of squamous and glandular epithelia, myoepithelial cells, and mesothelial cells. Immunohistochemically, anti-KRT5 has demonstrated utility in distinguishing metastatic carcinoma involving the pleura from epithelioid mesothelioma. KRT5 expression is observed in nearly all squamous cell carcinomas, approximately 50% of transitional cell carcinomas, and a subset of undifferentiated large cell carcinomas. When used in combination with anti-p63, anti-KRT5 provides high sensitivity and specificity for identifying squamous differentiation. Additionally, anti-KRT5 reliably marks myoepithelial cells in the breast, glandular epithelial cells, and basal cells of the prostate.
Keratins are cytoplasmic intermediate filament proteins expressed in epithelial cells. Among them, type II keratin CK5 and its partner, type I keratin CK14, are specifically co-expressed and play a critical role in the assembly of 8-nm intermediate filaments. CK5 serves as a marker for myoepithelial cells in the breast and basal cells of the prostate, while CK14 is particularly valuable in identifying breast carcinomas with a basal-like phenotype. Breast cancers co-expressing CK5/14 have been shown to represent a true basal phenotype, predominantly associated with BRCA1-related tumors. Expression of CK5/14 is regarded as a prognostic indicator in breast carcinoma.
Cytokeratin 5 (58 kDa) is a high-molecular weight, basic type of Cytokeratin is expressed in basal, intermediate and superficial-cell layers of stratified epithelia as well as transitional epithelia, complex epithelia, mesothelial cells and Mesothelioma. Cytokeratin 6 (56 kDa) is also a high-molecular weight, basic type cytokeratin expressed by proliferating squamous epithelium often paired with Cytokeratin 16.
CK 5 and 6 are positively seen in nearly 100% of Malignant Mesotheliomas and is rarely seen in Lung Adenocarcinomas. CK 5 and 6 can positively be seen in undifferentiated Large-cell Carcinoma as well as Squamous Carcinoma. Fewer than 10% of Carcinomas of the breast, colon, and prostate stain positively for this marker. CK 5 and 6 have also been used successfully as a myoepithelial cell marker in the prostate to determine.
Cytokeratin 5 (CK5, 58 kDa) and Cytokeratin 6 (CK6, 56 kDa) are high molecular weight, basic type II intermediate filament proteins. CK5 is expressed in basal, intermediate, and superficial layers of stratified squamous epithelia, as well as in transitional and complex epithelia, mesothelial cells, and mesotheliomas. CK6, commonly co-expressed with CK16, is typically observed in proliferating squamous epithelial cells.
Immunohistochemical detection of CK5/6 is strongly associated with Malignant Mesothelioma, showing near universal positivity, while Lung Adenocarcinomas demonstrate minimal to no reactivity. CK5/6 expression may also be observed in undifferentiated Large Cell Carcinomas and Squamous Cell Carcinomas. In contrast, fewer than 10% of carcinomas arising from the breast, colon, or prostate exhibit CK5/6 positivity. Additionally, CK5/6 immunostaining is employed as a marker of basal or myoepithelial cells in the prostate, aiding in the histopathological assessment of malignancy.
Cytokeratin 7 is a basic cytokeratin which is found in most glandular and transitional epithelia but not in the stratified squamous epithelia.
Keratin 7 is expressed in the epithelial cells of ovary, lung, and breast but not of colon, prostate, or gastrointestinal tract. Antibody to cytokeratin is useful in distinguishing ovarian carcinomas (keratin 7+) from colon carcinomas (keratin 7-).
Cytokeratin 7 is a basic cytokeratin which is found in most glandular and transitional epithelia but not in the stratified squamous epithelia.
Keratin 7 is expressed in the epithelial cells of ovary, lung, and breast but not of colon, prostate, or gastrointestinal tract. Antibody to cytokeratin is useful in distinguishing ovarian carcinomas (keratin 7+) from colon carcinomas (keratin 7-).
Cytokeratin 8 (CK8) is a member of the intermediate filament protein family that contributes to the cytoskeletal architecture of nearly all epithelial cells. It is classified as a basic type II cytokeratin with an approximate molecular weight of 52 kDa. CK8 is expressed in simple epithelia and in all adenocarcinomas. Also referred to as tissue polypeptide antigen (TPA), CK8 has been detected in the sera of patients with malignancies. Since this antibody does not cross-react with squamous epithelium, clone C51 is particularly useful in determining the epithelial origin of neoplasms. CK8 is expressed in various normal and neoplastic epithelial tissues, including ductal and glandular epithelia such as those of the colon, stomach, small intestine, trachea, esophagus, and transitional epithelium. Immunohistochemical detection of CK8 serves as an important diagnostic marker, particularly in distinguishing lobular carcinoma from ductal carcinoma of the breast. Additionally, recent evidence suggests that CK8 may represent a novel tumor marker in lung cancer.
Cytokeratin 8 (CK8) belongs to the type II (or B or basic) subfamily of high molecular weight cytokeratins and exists in combination with cytokeratin 18 (CK18). This MAb cocktail recognizes all simple epithelia including glandular epithelium, for example thyroid, female breast, gastrointestinal tract, respiratory tract, and urogenital tract including transitional epithelium. All adenocarcinomas and most squamous carcinomas are positive but keratinizing squamous carcinomas are usually negative. This antibody is useful in demonstrating the presence of Paget cells; there is very little keratin 18 in the normal epidermis so only Paget cells are stained.Immunohistochemical staining with this MAb is indistinguishable from that obtained with monoclonal antibody 5D3
Cytokeratin 8 (CK8) is a type II (basic or high molecular weight) intermediate filament protein that typically heterodimerizes with cytokeratin 18 (CK18). This monoclonal antibody (MAb) exhibits reactivity with all simple epithelial tissues, including glandular epithelia such as those of the thyroid, mammary gland, gastrointestinal tract, respiratory tract, and urogenital tract including transitional epithelium. CK8 immunoreactivity is observed in all adenocarcinomas and the majority of non-keratinizing squamous cell carcinomas; however, keratinizing squamous cell carcinomas generally lack expression. This antibody is particularly valuable for the identification of Paget cells, as normal epidermal tissue contains minimal CK18 expression, thereby allowing selective staining of Paget cells.
Cytokeratins are intermediate filament proteins essential for the structural integrity of epithelial cells. They are expressed in a tissue-specific and differentiation-dependent manner, making them highly valuable markers for epithelial cell identification and tumor classification. The Cytokeratin Cocktail Broad Spectrum combines three monoclonal antibodies: Clone AE1 ? reacts with acidic type I cytokeratins (CK10, 14, 15, 16, 19).Clone AE3 ? reacts with basic type II cytokeratins (CK1?8).Clone C51 ? specifically detects CK8 and CK18, enhancing sensitivity for simple epithelia and adenocarcinomas.This combination provides broad coverage across low- and high-molecular-weight cytokeratins, enabling reliable detection of most epithelial tissues and their neoplastic counterparts.
Cytokeratins are intermediate-filament keratins found in the intracytoplasmic cytoskeleton of epithelial tissue. There are two types of cytokeratins: the low-weight, acidic Type I cytokeratins and the high-weight, basic or neutral Type II cytokeratins. Cytokeratins are usually found in pairs comprising a Type I cytokeratin and a Type II cytokeratin. Expression of these cytokeratins is frequently organ or tissue-specific.
Cytokeratin HMW AE3 antibody is capable of recognizing all basic cytokeratins; therefore, it is a broadly reactive antibody staining most epithelia and their neoplasms. Cytokeratin HMW AE3 antibody stains normal and neoplastic cells of epithelial origin. CK HMW is primarily found in the non-squamous epithelia and is present in the majority of Adenocarcinomas and Ductal Carcinomas. It is absent in Squamous Cell Carcinomas. Hepatocellular Carcinomas are defined by the use of antibodies that recognize only cytokeratin 8 and 18.
The Cytokeratin CAM5.2 monoclonal antibody exhibits specific reactivity toward low molecular weight keratins, corresponding to Moll?s polypeptides #7 and #8, with molecular masses of approximately 48 kDa and 52 kDa, respectively?identified as cytokeratin 7 and 8. These intermediate filament proteins are predominantly expressed in the secretory epithelium of normal human tissues and are absent in stratified squamous epithelial cells. Immunohistochemical analysis using the CAM5.2 antibody demonstrates broad reactivity with epithelial-derived tissues, including hepatic parenchyma and renal tubular epithelium, and is diagnostically useful in the detection of hepatocellular carcinoma and renal cell carcinoma. Notably, the antibody may exhibit limited immunoreactivity with certain squamous cell carcinomas, reflecting its specificity for low molecular weight cytokeratin.
Cytokeratins are intermediate filament proteins that form a key component of the intracytoplasmic cytoskeleton of epithelial cells. They are classified into two major groups: low-molecular-weight, acidic type I cytokeratins and high-molecular-weight, basic/neutral type II cytokeratins. These proteins are typically expressed as complementary pairs consisting of one type I and one type II cytokeratin, with expression patterns that are often tissue- or organ-specific.
The Cytokeratin Low Molecular Weight (LMW) AE1 antibody exhibits broad reactivity by recognizing multiple acidic keratins, thereby staining a wide range of epithelial cells and their corresponding neoplasms. Because keratins are consistently expressed as type I/type II pairs, this antibody is effective in demonstrating the distribution of keratin-positive cells within epithelial tissues. Cytokeratin AE1 is particularly valuable in the differential diagnosis of poorly differentiated carcinomas versus non-epithelial neoplasms and serves as a robust marker for both normal and neoplastic epithelial cells
Human cytokeratins (40kD to 68kD) are a family of water-insoluble proteins that form a major part of the cytoskeleton of epithelial cells. Immunohistochemical analysis of a large variety of neoplasms has established keratin protein immunohistochemistry as an important aid for classification of epithelial neoplasms.
Between 10% and 40% of patients with acquired immunodeficiency syndrome (AIDS) develop cytomegalovirus (CMV) infections. In some cases, CMV can be detected in bronchoalveolar lavage fluid (BALF), urine, and other specimens, even in the absence of symptoms of CMV disease. To aid in the diagnosis of CMV disease in patients with AIDS or HIV infection, a reliable indicator of active CMV infection is needed. The CMV p65 antigen has been identified in the leukocytes of both peripheral blood and BALF during the early stages of CMV disease.