Cancer Diagnostics Solutions
The BAP1 gene is part of the ubiquitin C-terminal hydrolase subfamily of deubiquitination enzymes, which play a key role in removing ubiquitin from proteins. The enzyme encoded by this gene interacts with the breast cancer type 1 susceptibility protein (BRCA1) through its RING finger domain and functions as a tumor suppressor. Additionally, it is implicated in regulating transcription, cell cycle and growth, DNA damage response, and chromatin dynamics.
Germline mutations in BAP1 are linked to tumor predisposition syndrome (TPDS), a condition that increases the risk of cancers such as malignant mesothelioma, uveal melanoma, and cutaneous melanoma.
BCL10, with an N-terminal caspase recruitment domain (CARD), is found in a number of apoptotic regulatory molecules. It was identified through its direct involvement in t(1;14) of mucosa-associated lymphoid tissue (MALT) lymphoma. Expression of BCL10 was shown to induce NF B activation in a NIK-dependent pathway.
This MAb labels subpopulations of normal B and T cells and is a useful tool for the sub-classification of lymphomas. In MALT lymphomas with the t(1;14) translocation, while 55% of MALT lymphomas lacking this translocation exhibited the same labeling pattern, although at a much lower level.
The Bcl-2 family of proteins regulates apoptosis by controlling mitochondrial permeability and release of cytochrome c. Bcl-2 is an anti-apoptotic protein that resides in the outer mitochondrial wall and inhibits release of cytochrome c. Over-expression of Bcl-2 has been shown to promote cell survival by suppressing apoptosis. It has been documented that Bcl-2 becomes deregulated in tumor cells as a result of translocation into the immunoglobulin heavy-chain locus and is therefore activated in B-cell malignancies.?
This antibody recognizes a protein of 25-26kDa, identified as bcl-2 alpha oncoprotein. It shows no cross-reaction with Bcl-x or Bax protein. Expression of bcl-2 alpha oncoprotein inhibits the programmed cell death (apoptosis). In most follicular lymphomas, neoplastic germinal centers express high levels of bcl-2 alpha protein, whereas the normal or hyperplastic germinal centers are negative. This antibody is valuable when distinguishing between reactive and neoplastic follicular proliferation in lymph node biopsies. It may also be used in distinguishing between those follicular lymphomas that express bcl-2 protein and small number in which neoplastic cells are bcl-2 negative.
The bcl-6 gene is a transcriptional regulator that encodes a 706-amino-acid nuclear zinc finger protein. Antibodies targeting this protein specifically stain germinal center cells within lymphoid follicles, as well as follicular and interfollicular cells in cases of Follicular Lymphoma, Diffuse Large B-Cell Lymphomas, Burkitt?s Lymphoma, and a majority of Reed-Sternberg cells in Nodular Lymphocyte-Predominant Hodgkin?s Disease.
The bcl-6 antibody is also valuable for identifying neoplastic cells in Nodular Lymphocyte-Predominant Hodgkin?s Disease. In contrast, bcl-6 staining is infrequent in Mantle-Cell Lymphoma and MALT Lymphoma. Expression of bcl-6 is observed in approximately 45% of CD30+ Anaplastic Large-Cell Lymphomas, but it is consistently absent in other types of peripheral T-cell Lymphomas
BCL6 is a transcriptional regulator gene that encodes a 706-amino-acid nuclear zinc finger protein. In normal tissues, these antibodies exhibit strong nuclear staining in a subset of B-lymphocytes, primarily located in germinal centers (GC).
BCL6 antibodies also stain malignant cells in follicular lymphoma, diffuse large B-cell lymphoma, Burkitt lymphoma, classical Hodgkin lymphoma, and the majority of tumor cells in nodular lymphocyte-predominant Hodgkin lymphoma. Additionally, BCL6 expression has been observed in anaplastic large cell lymphomas (ALCL).
Bcl-6, a transcriptional repressor, can promote or inhibit apoptosis depending on the cell type and also plays an important role in normal immune responses. Bcl-6 negatively regulates NFkB expression, thereby inhibiting NFkB-mediated cellular functions and is frequently found to be deregulated in non-Hodgkin?s lymphoma.
BCoR (Bcl-6 corepressor) is a 1,755 amino acid protein that associates with histone deacetylases (HDACs) to transcriptionally repress Bcl-6. With ubiquitous expression, BCoR is localized to the nucleus where it interacts with other proteins through its three ANK repeat domains. Mutations in the gene encoding BCoR result in microphthalmia with associated anomalies 2, also known as anophthalmia, which is characterized by variable features, such as renal aplasia, mental retardation, hyospadias, microencephaly and cryptorchidism. There are four isoforms of BCoR which are produced as a result of alternative splicing events
Beta-catenin interacts with the cytoplasmic region of E-cadherin, a connection essential for E-cadherin?s role as an adhesion molecule. In healthy tissues, beta-catenin localizes to the membrane of epithelial cells, reflecting its function in the cell adhesion complex. In breast ductal neoplasia, beta-catenin primarily remains at the cellular membranes. In contrast, in lobular neoplasia, beta-catenin is notably redistributed throughout the cytoplasm, creating a diffuse cytoplasmic pattern.
Immunostaining for beta-catenin and E-cadherin aids in accurately distinguishing between ductal and lobular neoplasms, particularly in differentiating low-grade ductal carcinoma in situ (DCIS) from lobular carcinoma. Similarly, some rectal and gastric adenocarcinomas exhibit diffuse cytoplasmic beta-catenin staining without membranous localization, mirroring the pattern observed in lobular breast carcinomas.
?-Catenin is a critical regulatory protein that mediates both cell?cell adhesion and intracellular signal transduction via the Wnt signaling pathway. It plays essential roles in embryonic development, cellular proliferation, and lineage differentiation. Activating mutations in the CTNNB1 gene, which encodes ?-catenin, result in impaired degradation of the protein, leading to its cytoplasmic accumulation and subsequent nuclear translocation. This aberrant nuclear localization contributes to the pathogenesis of several neoplasms, including familial adenomatous polyposis, desmoid-type fibromatosis, solitary fibrous tumors, and endometrial carcinoma. In desmoid-type fibromatosis, particularly when arising in anatomical sites such as the breast and mesentery, the detection of nuclear ?-catenin expression serves as a diagnostically valuable immunohistochemical marker, facilitating distinction from other histologically similar fibroblastic or myofibroblastic proliferations
Oct-binding factor 1 (OBF1), also referred to as BOB.1, is a B-cell-specific transcriptional coactivator encoded on chromosome 11q23.1. Its expression is largely confined to mature B lymphocytes, with strong immunoreactivity observed in germinal center B-cells. Studies of B-cell-derived cell lines across various developmental stages indicate a constitutive and lineage-restricted expression of BOB.1. In nodular lymphocyte predominant Hodgkin lymphoma (NLPHL), lymphocytic and histiocytic (LP) cells consistently demonstrate nuclear BOB.1 expression, reflecting their germinal center origin. In contrast, classical Hodgkin lymphoma (CHL) typically shows reduced or absent BOB.1 expression in Hodgkin and Reed-Sternberg cells, although occasional immunoreactivity may be seen. BOB.1 expression is also detected in other B-cell neoplasms, including follicular lymphoma, diffuse large B-cell lymphoma, and to a lesser extent, in some cases of acute myeloid leukemia. Weak to moderate staining may also be present in chronic lymphocytic leukemia, marginal zone lymphoma, and mantle cell lymphoma, aiding in their immunophenotypic characterization.
The expression of BOB.1 in various established B-cell lines, representative of different stages in B-cell development, suggests a constitutive and B-cell-specific pattern of expression. In nodular lymphocyte predominant Hodgkin lymphoma, the lymphocyte-predominant (LP) cells, which are derived from the germinal center, consistently exhibit immunopositivity for BOB.1. In contrast, BOB.1 immunoreactivity is observed in the Hodgkin and Reed-Sternberg cells in only some cases of classical Hodgkin lymphoma. Expression of BOB.1 has also been reported in follicular center cell lymphoma, diffuse large B-cell lymphoma, and certain cases of acute myeloid leukemia. Additionally, B-cell chronic lymphocytic leukemia (B-CLL), marginal zone lymphoma, and mantle cell lymphoma may exhibit weak to moderate immunoreactivity for BOB.1.Feel free to let me know if there are specific aspects you?d like further refined or any other modifications you have in mind!.
Brachyury is a rabbit monoclonal antibody for immunohistochemistry targeting the brachyury protein, encoded by the T gene on chromosome 6q27. Brachyury is a transcription factor within the T-box family, with a conserved role in midline specification and anterior?posterior axis development in bilaterian organisms, including chordates and mollusks. Mutations in this gene, such as vertebral and spinal dysplasia (VSD), are linked to abnormal cervical vertebral number in mammals. Expression of brachyury is a definitive diagnostic marker for chordoma, a malignant tumor derived from notochordal remnants, with gene duplication conferring increased susceptibility. Cytogenetic studies demonstrate brachyury locus gain in a subset of chordomas. Functionally, brachyury regulates epithelial?mesenchymal transition (EMT) by repressing E-cadherin, thereby facilitating invasion and metastasis. Overexpression is strongly associated with hepatocellular carcinoma, where it serves as a prognostic biomarker and potential therapeutic target. Furthermore, brachyury-driven EMT is implicated in benign fibrotic conditions such as renal fibrosis.
BRAF is a human gene that makes a protein called B-Raf, which is more formally known as serine/threonine-protein kinase B-Raf. The B-Raf protein is involved in sending signals inside cells, which are involved in directing cell growth. In 2002, it was shown to be mutated in some human cancers. Mutations in the BRAF gene can cause disease in two ways. First, mutations can be inherited and cause birth defects. Second, mutations can appear later in life and cause cancer, as an oncogene. Mutations in this gene have been found in cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, papillary thyroid carcinoma, non-small-cell lung carcinoma, and adenocarcinoma of the lung.
The frequency of BRAF mutations varies widely in human cancers, from more than 80% in melanomas and nevi, to as little as 0?18% in other tumors, such as 1?3% in lung cancers and 5% in colorectal cancer. In 90% of the cases, thymine is substituted with adenine at nucleotide 1799. This leads to valine (V) being substituted for by glutamate (E) at codon 600 (referred to as V600E) in the activation segment that has been found in human cancers. This mutation has been widely observed in papillary thyroid carcinoma, colorectal cancer, melanoma and non-small-cell lung cancer. BRAF-V600E mutation are present in 57% of Langerhans cell histiocytosis patients. The V600E mutation is a likely driver mutation in 100% of cases of hairy cell leukemia. High frequency of BRAF V600E mutations have been detected in ameloblastoma, a benign but locally infiltrative odontogenic neoplasm.
The BRAF gene encodes a protein that is part of the RAS-RAF-MEK-ERK signaling pathway, which regulates cell division and proliferation. The V600E mutation in the BRAF gene leads to the production of a constitutively active BRAF protein, resulting in uncontrolled cell growth and division. Identifying the presence of this mutation is crucial for diagnosing and guiding the treatment of certain cancers.
The BRAF (V600E) antibody is used in immunohistochemistry to detect the presence of a specific mutation in the BRAF gene known as V600E. This mutation is commonly associated with various cancers, including melanoma, colorectal cancer, and certain types of thyroid cancer, lung cancer, and Hairy cell leukemia. The BRAF (V600E) antibody specifically binds to the mutated BRAF protein, allowing pathologists to detect the mutation in cancer tissue. Immunohistochemistry using this antibody is often employed in the evaluation of tumor specimens to aid in the diagnosis and classification of cancers.
BRCA1 (breast and ovarian cancer susceptibility protein 1) is a nuclear phosphoprotein that functions as a key regulator of genomic integrity and serves as a tumor suppressor. In coordination with other tumor suppressors, DNA damage sensors, and signal transducers, it forms the BRCA1-associated genome surveillance complex (BASC), a large multiprotein assembly involved in genome monitoring and repair. BRCA1 associates with RNA polymerase II and, via its C-terminal domain, interacts with the histone deacetylase complex, thereby contributing to transcriptional regulation, DNA double-strand break repair, and homologous recombination.
Brg-1 (SMARCA4) is a key ATPase component of the SWI/SNF chromatin remodeling complex, which mediates transcriptional regulation through ATP-dependent modulation of nucleosome positioning and chromatin accessibility. Brg-1 functions in concert with other core subunits of the complex, including Brm (SNF2?), Ini1 (SNF5/SMARCB1), BAF155 (SMARCC1), and BAF170 (SMARCC2), forming a functional scaffold essential for chromatin remodeling activity. These interactions stabilize the SWI/SNF complex and influence its regulatory function in controlling gene expression programs associated with cellular proliferation, differentiation, and response to extracellular cues. Dysregulation of Brg-1 or SWI/SNF complex components is implicated in oncogenesis and other pathophysiological conditions. Underscoring the relevance of Brg-1 as a target for research in epigenetic regulation and cancer biology.
ABCB11 encodes the bile salt export pump (BSEP), an ATP-binding cassette (ABC) transporter responsible for the energy-dependent translocation of bile salts into the canalicular lumen of hepatocytes. Its expression is predominantly restricted to the liver, where it is localized specifically to the canalicular membrane microvilli and subcanalicular vesicular compartments. Structurally, ABCB11 is composed of two homologous halves, each comprising a hydrophobic transmembrane domain and a cytoplasmic nucleotide-binding domain, characteristic of ABC transporters. Pathogenic variants in ABCB11 are causative of progressive familial intrahepatic cholestasis type 2 (PFIC2), an autosomal recessive hepatobiliary disorder of early childhood marked by severe cholestasis and normal serum gamma-glutamyltransferase (GGT) levels. In addition to familial forms, mutations in ABCB11 have also been identified in sporadic cases of chronic intrahepatic cholestasis, indicating that defects in this gene may underlie both inherited and non-familial cholestatic liver disorders