Cancer Diagnostics Solutions
Galectin-3 is a member of the beta-galactosidase-binding lectin family. It is associated with cell growth, adhesion, inflammation, mRNA processing, and apoptosis. Aberrant expression of Galectin-3 is related to malignant transformation and metastasis in carcinomas of the breast, colon and thyroid.Galectin-3 reactivity can be seen in the nucleus of neutrophils, vascular endothelium, carcinomas of the colon, breast, and thyroid. Galectin-3 may be useful in the differentiationof benign and malignant thyroid neoplasms.Galectin-3 may also be useful in the identification of certain liver disorders
Galectin-3 is a 30-kDa protein belonging to the ?-galactoside-binding lectin family. It is involved in various cellular processes, including proliferation, adhesion, inflammation, mRNA splicing, and apoptosis. Aberrant expression of Galectin-3 has been linked to oncogenic transformation and metastatic progression in several carcinomas, particularly of the breast, colon, and thyroid. Immunoreactivity for Galectin-3 is commonly observed in the nuclei of neutrophils, vascular endothelial cells, and tumor cells in colon, breast, and thyroid cancers. It serves as a useful biomarker in differentiating benign from malignant thyroid neoplasms and may also aid in the identification of specific liver disorders.
Trans-acting T-cell-specific transcription factor, GATA-3 is a protein that in humans is encoded by the GATA3 gene. GATA-3 b regulates luminal epithelial cell differentiation in the mammary gland, is an important regulator of T cell development and plays an important role in endothelial cell biology.
GATA-3 is one of the three genes mutated in >10% of breast cancers. Nuclear expression of GATA-3 in breast cancer is considered a marker of luminal cancer in ER+ cancer and luminal androgen responsive cancer in ER-/AR+ tumors. It is highly coexpressed with FOXA1 and serves as a negative predictor of basal subtype and HER-2 and is also considered a strong predictor of taxane and platinum salts insensitivity.
GATA3 expression is found in urothelial carcinoma, especially in invasive and high grade tumors. Therefore, anti-GATA3 can be used in a panel of antibodies for diagnosis of unknown primary carcinoma, when carcinomas of the breast or bladder are a possibility. Studies have also shown the utility of GATA-3 in differentiating urothelial carcinoma from prostate adenocarcinoma and squamous cell carcinomas of the uterine, cervix, anus and lung
It recognizes a protein of 15kDa, identified as Gross cystic disease fluid protein 15 (GCDFP-15). It is a major protein component of benign breast gross cysts.
It is a known marker of breast cancer, as it is found in approximately 50% of all breast cancer specimens. GCDFP-15, also known as PIP, for prolactin inducible protein, is a prolactin and androgen controlled protein. This antibody is useful in the identification of metastatic breast carcinoma, or fluid analysis
Glial fibrillary acidic protein or GFAP is a Type III protein of the intermediate filaments principally found in astrocytes in the central nervous system, but can also be found in neurons, hepatic stellate cells, kidney mesangial cells, pancreatic stellate cells, and Leydig cells. It has a role in the cytoskeleton of the astrocyte and possibly many other stellate-shaped cells. Antibodies to GFAP are very useful as markers of astrocytic cells. In addition, many types of brain tumors, presumably derived from astrocytic cells, heavily express GFAP. This marker is mainly used to distinguish neoplasms of astrocytic origin from other neoplasms in the central nervous system.
Glial Fibrillary Acidic Protein (GFAP) is a class III intermediate filament protein predominantly specific to astrocytes in the brain. Additionally, it is expressed in certain ependymal cells within the central nervous system, as well as in Schwann cells, enteric glial cells, and satellite cells of the peripheral nervous system.
GFAP serves as a key marker for distinguishing astrocytomas from nonglial cell tumors
Glial fibrillary acidic protein (GFAP) is a type III intermediate filament protein predominantly expressed in astrocytes and certain astroglial subtypes within the central nervous system (CNS). It is also expressed in satellite glial cells of peripheral ganglia and in non-myelinating Schwann cells of the peripheral nervous system. Furthermore, GFAP is robustly expressed in neural stem cells. Due to its cell-type specificity, GFAP serves as a reliable immunohistochemical marker for identifying astrocytic lineage cells. GFAP expression is also markedly elevated in numerous astrocytoma and glioma subtypes, indicating its diagnostic utility in CNS tumor classification. Beyond the CNS, GFAP expression has been detected in lens epithelial cells, hepatic Kupffer cells, certain salivary gland neoplasms, and sporadically in erythrocytes. GFAP plays a critical role in distinguishing astrocytes from other glial cell populations during neurodevelopment. Pathogenic mutations in the GFAP gene are causative of Alexander disease, a leukodystrophy characterized by astrocyte dysfunction. The GFAP gene undergoes alternative splicing, giving rise to multiple transcript variants encoding distinct protein isoforms with potentially diverse functional roles.
Recognizes a protein of 55kDa, which is identified as GLUT-1. Glucose transporters are integral membrane glycoproteins involved in transporting glucose into most cells. There are many types of glucose transport carrier proteins, designated as Glut-1 to Glut-12. Glut-1 is a major glucose transporter in the mammalian blood-brain barrier. It is expressed in high density on the membranes of human erythrocytes and the brain capillaries that comprise the blood-brain barrier.
Glucose plays a critical role in mammalian cellular metabolism. Multiple isoforms of glucose transporter (GLUT) proteins have been characterized, with several demonstrating regulatory responses to insulin and insulin-like growth factor-1 (IGF-1) signalling pathways. GLUT-1 is broadly expressed across various human tissues, including the colon, lung, stomach, oesophagus, and breast. In certain malignancies, such as transitional cell carcinoma of the urinary bladder, elevated GLUT-1 expression has been correlated with increased tumor aggressiveness and poor prognostic outcomes
Recognizes a protein of 55kDa, which is identified as GLUT-1. Glucose transporters are integral membrane glycoproteins involved in transporting glucose into most cells. There are many types of glucose transport carrier proteins, designated as Glut-1 to Glut-12. Glut-1 is a major glucose transporter in the mammalian blood-brain barrier. It is expressed in high density on the membranes of human erythrocytes and the brain capillaries that comprise the blood-brain barrier.
Glut-1 is expressed at variable levels in many human tissues. Overexpression of Glut-1 has been linked to tumor progression or poor survival of patients with carcinomas of the colon, breast, cervical, lung, bladder and mesothelioma. Glut-1 is a sensitive and specific marker for the differentiation of malignant mesothelioma (positive) from reactive mesothelium (negative).
Glycophorin A (CD235a) is a 151-amino acid sialoglycoprotein predominantly localized on the plasma membrane of mature erythrocytes and erythroid precursor cells, with an estimated expression of ~500,000 copies per cell. The GYPA gene encoding glycophorin A is situated on chromosome 4 and exists in two major allelic variants, M and N, which differ by amino acid substitutions at positions 1 (Ser?Leu) and 5 (Gly?Glu). These polymorphisms define the M/N blood group system. Functionally, glycophorin A contributes to erythrocyte membrane integrity by forming a mucin-like structure that reduces intercellular adhesion, thereby maintaining red cell dispersion and preventing spontaneous agglutination or fusion. It also serves as a receptor for a range of pathogens, including Sandei virus, parvovirus B19, and the Streptococcus adhesin Hsa. Environmental genotoxic stressors may induce mutations or allelic loss in GYPA, potentially altering cell surface phenotype. Emerging evidence links such genetic alterations to increased susceptibility to malignancies and cardiovascular diseases, underscoring glycophorin A's diagnostic and pathophysiological relevance in hematologic and systemic disorders.
Glycophorin A (GPA) and B (GPB) are single-pass membrane sialoglycoproteins. GPA is responsible for the blood group M and N antigens, while GPB is associated with the S and U antigens. Both GPA and GPB contribute to a large mucin-like surface on the cell, which is thought to act as a barrier to cell fusion and thereby reduce the likelihood of red blood cell aggregation in the bloodstream.
Antibodies against Glycophorin A have been utilized to study erythroid cell development and to diagnose erythroid leukemias
Glypican-3 (GPC3) is a glycosylphospatidyl inositol-anchored membrane protein, which may also be found in a secreted form. Anti-GPC3 has been identified as a useful tumor marker for the diagnosis of hepatocellular carcinoma (HCC), hepatoblastoma, melanoma, testicular germ cell tumors, and Wilm's tumor. In patients with HCC, GPC3 is overexpressed in neoplastic liver tissue and elevated in serum, but is undetectable in normal liver, benign liver, and the serum of healthy donors.
Glypican-3 (GPC3) is an integral membrane protein that is mutated in Simpson-Golabi-Behmel syndrome (SGBS), a recessive X-linked condition characterized by pre- and post-natal overgrowth. GPC3, also known as OCI-5 in rats, belongs to the glypican family of heparan sulfate proteoglycans, which are attached to the cell membrane through a glycosyl-phosphatidyl-inositol (GPI) anchor.
The expression of GPC3 is observed in embryonic mesodermal tissues of the lung, liver, and kidney. It is believed that GPC3 regulates the growth of tissues and organs by interacting with growth factors such as insulin-like growth factor II (IGF-II) and fibroblast growth factor 2 (FGF-2). The downregulation of GPC3 may occur through mechanisms such as promoter hypermethylation or the repression of specific transcription factors.
Glypican-3 (GPC3) is a glycosylphospatidyl inositol-anchored membrane protein, which may also be found in a secreted form. GPC3 belongs to a member of the glypican family of heparan sulfate proteoglycans. This protein may be involved in the suppression/modulation of growth in the predominantly mesodermal tissues and organs.
Glypican-3 is thought to regulate tissue and organ growth through interactions with growth factors such as Insulin-like growth factor II or fibroblast growth factor 2. GPC3 was identified to be useful tumor marker for the diagnosis of hepatocellular carcinoma (HCC), hepatoblastoma, melanoma, and testicular germ cell tumors. A high level of GPC3 expression has also been found in some types of embryonic tumors, such as Wilms tumor and hepatoblastoma.
Granzyme B is a neutral serine protease found in the cytolytic granules of activated cytotoxic T lymphocytes (CTLs) and natural killer (NK) cells. It is selectively expressed following activation of these cytotoxic cells and is absent in non-cytotoxic lymphoid populations. Also known as cathepsin G-like 1 (CGL1) and CTLA-1 (cytotoxic T lymphocyte-associated serine esterase-1), Granzyme B is essential for the induction of apoptosis in target cells during immune-mediated cytotoxic responses. It enters target cells primarily through the mannose-6-phosphate receptor, functioning as a death receptor. Once internalized, Granzyme B initiates apoptosis by cleaving caspase-3, activating the caspase cascade, and by cleaving Bid, a pro-apoptotic Bcl-2 family protein, to trigger the mitochondrial apoptotic pathway. Granzyme B thus plays a central role in immune surveillance and cytotoxicity. While multiple granzymes (A?G) have been identified in murine models, the number characterized in humans is more limited, with Granzyme B being one of the most functionally significant
Glutamate receptor 2 (GRIA2) is a ligand-gated ion channel that mediates excitatory synaptic transmission through L-glutamate and is predominantly expressed in the central nervous system. Transcriptomic profiling has demonstrated >100-fold upregulation of GRIA2 in solitary fibrous tumors (SFTs) compared with non-neoplastic control tissues. Immunohistochemical analyses further revealed GRIA2 expression in the majority of SFTs, with reported positivity ranging from 64?86%. In diagnostic evaluation, GRIA2 exhibited a sensitivity of 64% and a specificity of 92%, corresponding to positive and negative predictive values of 41% and 97%, respectively, for distinguishing SFTs from other mesenchymal soft tissue neoplasms. Collectively, these findings suggest that GRIA2 may serve as a useful ancillary biomarker for the identification of STAT6-negative SFTs.
Growth hormone (GH or hGH), also referred to as somatotropin or somatropin, is a peptide hormone synthesized and secreted by somatotroph cells of the anterior pituitary gland. GH mediates diverse physiological effects across multiple tissues and cell types, with its cellular actions broadly categorized into mitogenic, differentiative, and metabolic functions. Immunohistochemically, GH-specific antibodies selectively label somatotrophs in normal pituitary tissue. This marker is valuable in the histopathological classification and subtyping of pituitary adenomas, particularly in identifying somatotroph-derived neoplasms
Pituitary growth hormone (GH) plays a crucial role in stimulating and controlling the growth, metabolism and differentiation of many mammalian cell types by modulating the synthesis of multiple mRNA species. These effects are mediated by the binding of GH to its membrane-bound receptor, GHR, and involve a phosphorylation cascade that results in the modulation of numerous signaling pathways.
GH is synthesized by acidophilic or somatotropic cells of the anterior pituitary gland. Anti-GH is a useful marker in classification of pituitary tumors and the study of pituitary disease (acromegaly).