Cancer Diagnostics Solutions
This antibody specifically targets Synacthen, which corresponds to amino acids 1-24 of ACTH, and does not cross-react with CLIP, the region encompassing amino acids 17-39 of ACTH. Pro-opiomelanocortin (POMC), also known as corticotropin-lipotropin, is a 267-amino-acid precursor hormone that undergoes extensive post-translational modifications in a tissue-specific manner, mediated by convertase enzymes.
This antibody stains corticotroph cells in the adenohypophysis and is valuable for the classification of pituitary adenomas.
Actin is a globular-structural, 345 kDa protein that polymerizes in a helical fashion to form an actin filament (or microfilament). Actin filaments provide mechanical support for the cell, determine the cell shape, enable cell movements (through lamellipodia, filopodia, or pseudopodia); and participate in certain cell junctions, in cytoplasmic streaming and in contraction of the cell during cytokinesis. In muscle cells they play an essential role, along with myosin, in muscle contraction. In the cytosol, actin is predominantly bound to ATP, but can also bind to ADP. Actin, Muscle Specific antibody recognizes actin of skeletal, cardiac, and smooth-muscle cells. It is not reactive with other mesenchymal cells except for myoepithelium. Muscle-Specific Actin recognizes alpha and gamma isotypes of all muscle groups. Non-muscle cells such as vascular endothelial cells and connective tissues are nonreactive. Neoplastic cells of non-muscle-derived tissue such as Carcinomas, Melanomas and Lymphomas are negative. This antibody is useful in the identification of rhabdoid cellular elements.
Actin is one of two major cytoskeletal proteins. The antibody can be used to identify smooth muscle tumors. It stains leiomyomas, leiomyosarcomas and pleomorphic adenomas but does not stain carcinomas, melanomas, lymphomas or non- smooth muscle sarcomas.
It stains the muscularis and muscularis mucosa of the gastrointestinal tract, the uterine myometrium, medial layer of blood vessels, the mesenchymal components of the prostate, and myoepithelial cells of salivary glands and other organs.
The antibody does not stain striated muscle such as skeletal and cardiac muscle, endothelium, connective tissue, epithelium or nerve.
Adipocyte differentiation-related protein (ADFP), also known as adipophilin, is a lipid droplet-associated protein detected on the surface of milk lipid globules from humans, bovines, and rodents. It localizes to the globule membrane surface and is a major component of a detergent-insoluble protein complex that includes butyrophilin and xanthine oxidase. Although initially characterized as adipocyte-specific, ADFP is widely expressed across various cultured cell lines, such as fibroblasts, endothelial cells, and epithelial cells. However, in vivo expression is restricted to select cell populations, including lactating mammary epithelial cells, cells of the adrenal cortex, Sertoli and Leydig cells in the testis, and hepatocytes exhibiting steatosis in the context of alcoholic liver cirrhosis. ADFP serves as a potential biomarker for terminally differentiated, lipid droplet-rich cells and may be indicative of pathological conditions characterized by abnormal lipid accumulation.
Albumins constitute a family of globular proteins, with serum albumin being the predominant form present in blood plasma. Unlike other plasma proteins, albumins are non-glycosylated and are primarily synthesized in the liver. Functionally, albumin acts as a transport protein for various endogenous ligands, including steroid hormones, fatty acids, and thyroid hormones, and contributes to the maintenance of oncotic pressure and extracellular fluid homeostasis. The gene encoding albumin is located on chromosome 4, and mutations within this gene may give rise to structurally or functionally aberrant albumin variants.
Hypoalbuminemia, or reduced serum albumin concentration, can result from a range of pathological and physiological conditions such as hepatic insufficiency, nephrotic syndrome, extensive burns, protein-losing enteropathy, malabsorption syndromes, nutritional deficiencies, advanced pregnancy, analytical artifacts, genetic polymorphisms, and neoplastic disorders. Conversely, hyperalbuminemia is typically associated with hemoconcentration secondary to dehydration, though elevated high-normal albumin levels may occasionally be observed in vitamin A (retinol) deficiency.
In patients with systemic lupus erythematosus (SLE), elevated titers of IgG-class autoantibodies directed against human serum albumin (anti-HSA IgG) have been documented and are positively correlated with disease activity, suggesting a potential role in the immunopathogenesis or as a biomarker for disease monitoring
Anaplastic lymphoma kinase (ALK) is a receptor tyrosine kinase belonging to the insulin receptor superfamily. Typically, ALK is expressed at low levels in regions of the developing central and peripheral nervous systems. In cancer, ALK can be activated through various mechanisms. The most common mechanism is the formation of a fusion protein resulting from chromosomal translocations, as seen in anaplastic large cell lymphoma (ALCL) and inflammatory myofibroblastic tumors. Additionally, ALK can be amplified through mutations, as observed in neuroblastomas. Aberrant ALK expression has also been found in various solid tumors, including non-small cell lung carcinoma (NSCLC) and brain cancers. ALK staining is present in both the nucleus and cytoplasm and is positive in about 60% of ALCL cases. ALK protein expression intumor cells serves as an independent prognostic factor predicting a favorable outcome.
Anaplastic Lymphoma Kinase (ALK) was initially identified as part of the NPM-ALK fusion protein. The ALK gene, located on chromosome 2, undergoes a chromosomal translocation with chromosome 5 [t(2;5)(p23;q35)], resulting in fusion with the Nucleophosmin (NPM) gene. This translocation produces a chimeric oncoprotein, NPM-ALK, an 80 kDa protein composed of the N-terminal region of NPM fused to the complete intracellular domain of ALK. The ALK-1 antibody specifically recognizes the p80 fusion protein generated by the NPM-ALK translocation. This aberrant protein is expressed in approximately one-third of large-cell lymphomas and is detected in around 60% of anaplastic large-cell lymphomas (ALCL). Immunohistochemical detection of ALK-1 has clinical relevance, as ALK-positive ALCL cases are generally associated with a more favorable prognosis compared to ALK-negative counterparts
Alpha-1-Antichymotrypsin (ACT) is an acute-phase glycoprotein that acts as a serine protease inhibitor, targeting proteolytic enzymes released by neutrophils and mast cells during inflammatory responses. Its primary site of synthesis is hepatocytes, although it is also locally expressed by histiocytes, including macrophages and Kupffer cells within the liver. Immunohistochemically, Alpha-1-Antichymotrypsin serves as a valuable diagnostic marker for malignant fibrous histiocytomas, facilitating distinction from other soft tissue neoplasms such as liposarcomas and Ewing?s sarcoma
Alpha-1-antitrypsin (A1AT) is a serine protease inhibitor (serpin superfamily) that modulates the activity of various proteolytic enzymes released by inflammatory cells. It functions as an acute-phase glycoprotein, synthesized primarily by hepatocytes, with additional expression in enterocytes and select mononuclear leukocyte populations. Immunohistochemical detection of A1AT is employed to demonstrate intracellular accumulation within hepatocellular lesions and certain histiocytic neoplasms
This monoclonal antibody (MAb) recognizes an oncofetal glycoprotein, alpha-fetoprotein (AFP), which consists of a single 70kDa chain, as identified in the ISOBM TD-2 workshop. It exhibits high specificity for AFP, with no cross-reactivity to other oncofetal antigens or serum albumin.
AFP is typically produced in the liver, intestinal tract, and yolk sac during fetal development. Anti-AFP antibodies have proven valuable in detecting hepatocellular carcinomas (HCC) and germ cell tumors, particularly yolk sac tumors
Alpha-fetoprotein (AFP) is a major plasma glycoprotein predominantly expressed during fetal development and is considered the fetal analogue of serum albumin. AFP exhibits high-affinity binding to various ligands, including copper, nickel, fatty acids, and bilirubin, and exists in multiple oligomeric forms, such as monomers, dimers, and trimers.
The most frequently observed aberration is a chromosomal translocation that generates a fusion gene composed of the 3' region of the ALK gene from chromosome 2 and the 5' region of the nucleophosmin (NPM) gene from chromosome 5. This rearrangement results in the expression of a chimeric oncogenic protein, NPM-ALK, which possesses constitutive tyrosine kinase activity. Sequence analysis of ALK reveals it encodes a novel receptor tyrosine kinase characterized by an extracellular ligand-binding domain, a single-pass transmembrane domain, and an intracellular tyrosine kinase domain. Notably, the extracellular and transmembrane domains are absent in the NPM-ALK fusion product, which contributes to its aberrant cytoplasmic localization and oncogenic potential. Phylogenetic comparisons indicate that ALK shares the highest sequence homology with Leukocyte Tyrosine Kinase (LTK).
Alpha-Methylacyl-CoA Racemase (AMACR, P504S) is an enzyme that catalyzes the racemization of ?-methyl-branched chain fatty acyl-CoA esters, playing a key role in the ?-oxidation of branched-chain fatty acids and bile acid intermediates. AMACR has been identified as a prostate cancer?associated gene, with its overexpression strongly correlated with prostatic adenocarcinoma.
?-Methylacyl-CoA racemase (AMACR) is a key mitochondrial and peroxisomal enzyme involved in the ?-oxidation of branched-chain fatty acids. Immunohistochemical analysis of formalin-fixed, paraffin-embedded tissue demonstrates marked overexpression of AMACR in prostatic adenocarcinoma, whereas benign prostatic glands typically lack detectable expression. Importantly, AMACR expression is also observed in prostatic intraepithelial neoplasia (PIN), a recognized precursor lesion of carcinoma.
p63, a member of the p53 tumor suppressor gene family, is consistently expressed in the basal (progenitor) cell layer of stratified epithelia. In the prostate, nuclear p63 immunoreactivity is restricted to basal cells in benign prostatic glands and PIN, but is absent in prostatic adenocarcinoma. Consequently, p63 serves as a negative marker for adenocarcinoma and a reliable indicator of basal cell integrity.
The combined application of AMACR (cytoplasmic staining in adenocarcinoma and PIN) and p63 (nuclear staining of basal cells in benign glands and PIN) provides a highly effective immunohistochemical panel for distinguishing benign prostatic glands, premalignant PIN lesions, and invasive adenocarcinoma, particularly in diagnostically challenging or limited tissue samples
This monoclonal antibody (MAb) recognizes a 110 kDa protein identified as the androgen receptor (AR). It specifically binds to both the full-length receptor and the newly characterized A form, without cross-reacting with estrogen, progesterone, or glucocorticoid receptors. The expression of AR has been reported to be inversely correlated with histologic grade in prostate tumors, with higher levels observed in well-differentiated tumors compared to poorly differentiated ones. In the context of prostate cancer, AR is proposed as a marker for hormone responsiveness, making it potentially valuable for identifying patients who may benefit from anti-androgen therapy. Clinically, this MAb has been effective in distinguishing morpheaform basal cell carcinoma (mBCC) from desmoplastic trichoepithelioma (DTE) in skin tissue samples. Additionally, it excels in staining tissues preserved in formalin and embedded in paraffin.
The ANXA1 gene, part of the annexin family, contains four annexin repeats, with each pair potentially forming a binding site for calcium and phospholipids. ANXA1 plays a role in membrane fusion and exocytosis. Its gene expression is upregulated in hairy cell leukemia (HCL), and the protein serves as a highly sensitive and specific biomarker for diagnosing this condition. Additionally, Annexin A1 has been shown to protect breast cancer cells from heat-induced DNA damage, indicating its involvement in tumor-suppressive and protective mechanisms. It is also linked to treatment resistance in certain cancers.
Recognizes a protein of 35-38kDa, which is identified as Arginase 1 (ARG1). Arginase is a manganese metallo-enzyme that catalyzes the hydrolysis of arginine to generate ornithine and urea. Arginase I and II are isoenzymes which differ in subcellular localization, regulation, and possibly function.
Arginase I is a cytosolic enzyme, which is expressed mainly in the liver as part of the urea cycle, whereas arginase II is a mitochondrial protein found in a variety of tissues. Antibody to ARG-1 labels hepatocytes in normal tissues and granulocytes in peripheral blood. ARG-1 is a sensitive and specific marker for identification of hepatocellular carcinoma.
Arginase-1 is a cytosolic enzyme that catalyzes the final step of the urea cycle, converting L-arginine into L-ornithine and urea, thereby facilitating the detoxification of ammonia. It functions as a homotrimer and requires a binuclear manganese (Mn??) cluster for enzymatic activity. These Mn?? ions coordinate with a water molecule, activating it to act as a nucleophile that hydrolyzes L-arginine. Arginase-1 is predominantly expressed in hepatocytes and serves as a highly sensitive and specific immunohistochemical marker for hepatic differentiation. In normal liver tissue, arginase-1 demonstrates strong, diffuse cytoplasmic staining throughout all hepatocytes, with occasional patchy nuclear reactivity. Hepatocellular carcinoma (HCC) frequently shows elevated expression of ARG1 compared to normal liver, making it a useful diagnostic marker for identifying hepatocellular origin in neoplastic tissues. Due to its restricted expression and high sensitivity, arginase-1 is commonly used in distinguishing HCC from metastatic tumors and other hepatic or non-hepatic malignancies.
Aspergillus fumigatus and Aspergillus flavus are common filamentous fungi responsible for allergic responses and Invasive Aspergillosis (IA), particularly in immunocompromised individuals. Infection begins when airborne conidia are inhaled into the lungs or sinuses, where they germinate into hyphae in cases of Invasive Pulmonary Aspergillosis (IPA). These hyphae exhibit angioinvasion, facilitating dissemination to distant organs such as the brain, liver, spleen, and skin. In the lungs, Aspergillus induces bronchiolytic damage, pneumonia, edema, and necrotizing granulomas containing fungal fragments, often within macrophages. Thrombosis and platelet activation may restrict hyphal spread, but compromised immunity limits this response. IA has a high mortality rate (~85%) and is frequently diagnosed postmortem, as Aspergillus is rarely isolated from blood cultures. Diagnosis relies on histopathology and immunohistochemistry (IHC) using formalin-fixed tissue. Morphological similarities with fungi such as Fusarium, Scedosporium, and Pseudallescheria boydii make IHC essential for accurate species identification and appropriate antifungal treatment
Ataxia-telangiectasia mutated (ATM) is a serine/threonine kinase belonging to the phosphatidylinositol 3-kinase-related kinase (PIKK) family. It plays a central role in the DNA damage response, particularly in the repair of double-strand DNA breaks caused by ionizing radiation and other genotoxic stresses. Mutations in the ATM gene result in ataxia-telangiectasia, a rare autosomal recessive disorder characterized by neurodegeneration, immunodeficiency, and increased risk of lymphoid malignancies. Unlike classical PI3 kinases, ATM phosphorylates protein substrates such as p53, MDM2, BRCA1, and SMC1, regulating cell cycle checkpoints, DNA repair, and apoptosis. Upon DNA damage, ATM undergoes autophosphorylation and becomes activated, triggering downstream signalling pathways. ATM-deficient cells exhibit hypersensitivity to ionizing radiation, impaired p53 activation, and defective cell cycle arrest. Additionally, ATM is involved in the E2F1-regulated apoptotic pathway via activation of Nbs1 and Chk2. The C-terminal region of ATM shares homology with PI3 kinase catalytic domains, reflecting its kinase activity.
ATRX is a member of the Snf2 family of helicase/ATPases, which contribute to the remodeling of the nucelosome structure in an ATP-dependent manner, and facilitate the initiation of transcription and replication. Structurally, ATRX contains a PHD zinc finger motif. ATRX is regulated throughout the cell cycle where it is differentially distributed within the nucleus.
During interphase, ATRX predominately associates with the nuclear matrix, while during mitosis, ATRX localizes with condensed chromatin. At the onset of M phase, phosphorylation rapidly induces this redistribution of ATRX to the short arms of human acrocentric chromosomes, where it then specifically complexes with heterochromatin protein 1 a to mediate chromosomal segregation. Mutations in the ATRX gene correlate with a high incidence of severe X-linked form of syndromal mental retardation associated with a thalassaemia or ATR-X syndrome.