28226 Results for: "Biotium"

Supplier: Biotium

CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.

Supplier: Biotium

CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.

Supplier: Biotium

CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.

Supplier: Biotium

CD11c, also known as Integrin, alpha X (complement component 3 receptor 4 subunit) (ITGAX), is a type I transmembrane protein found at high levels on most human dendritic cells, but also on monocytes, macrophages, neutrophils, and some B cells that induces cellular activation and helps trigger neutrophil respiratory burst; expressed in hairy cell leukemias, acute non-lymphocytic leukemias, and some B-cell chronic lymphocytic leukemias.

Supplier: Biotium

Recognizes a polypeptide which is identified as insulin, a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. Deficiency of insulin results in diabetes mellitus. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as beta-cell and insulinoma marker.

Supplier: Biotium

This antibody recognizes a protein doublet of 20-22 kDa, identified as MART-1 (Melanoma Antigen Recognized by T cells 1) or Melan-A. MART-1 is a newly identified melanocyte differentiation antigen recognized by autologous cytotoxic T lymphocytes. Seven other melanoma associated antigens recognized by autologous cytotoxic T cells include MAGE-1, MAGE-3, tyrosinase, gp100, gp75, BAGE-1, and GAGE-1. Subcellular fractionation shows that MART-1 is present in melanosomes and endoplasmic reticulum. This MAb cocktail labels melanomas and other tumors showing melanocytic differentiation. It is also a useful positive-marker for angiomyolipomas. It does not stain tumor cells of epithelial, lymphoid, glial, or mesenchymal origin.

Supplier: Biotium

This MAb is specific to lambda light chain of immunoglobulin and shows no cross-reaction with lambda light chain or any of the five heavy chains. In mammals, the two light chains in an antibody are always identical, with only one type of light chain, kappa or lambda. The ratio of Kappa to Lambda is 70:30. However, with the occurrence of multiple myeloma or other B-cell malignancies this ratio is disturbed. Antibody to the lambda light chain is reportedly useful in the identification of leukemias, plasmacytomas, and certain non-Hodgkin's lymphomas. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is malignant.

Supplier: Biotium

At least five CD1 genes (CD1a, b, c, d, and e) are identified. CD1 proteins have been demonstrated to restrict T cell response to non-peptide lipid and glycolipid antigens and play a role in non-classical antigen presentation. CD1a is a non-polymorphic MHC Class 1 related cell surface glycoprotein, expressed in association with Beta-2 microglobulin. Anti-CD1a labels Langerhans cell histiocytosis (Histiocytosis X), extranodal histiocytic sarcoma, a subset of T-lymphoblastic lymphoma/leukemia, and interdigitating dendritic cell sarcoma of the lymph node. When combined with antibodies against TTF-1 and CD5, anti-CD1a is useful in distinguishing between pulmonary and thymic neoplasms since CD1a is consistently expressed in thymic lymphocytes in both typical and atypical thymomas, but only focally in 1/6 of thymic carcinomas and not in lymphocytes in pulmonary neoplasms. Anti-CD1a is reported to be a new marker for perivascular epithelial cell tumor (PEComa).

Supplier: Biotium

Pax genes contain paired domains with strong homology to genes in Drosophila, which are involved in programming early development. Lesions in the Pax-6 gene account for most cases of aniridia, a congenital malformation of the eye, chiefly characterized by iris hypoplasia, which can cause blindness. Pax-6 is involved in other anterior segment malformations besides aniridia, such as Peters anomaly, a major error in the embryonic development of the eye with corneal clouding with variable iridolenticulocorneal adhesions. The Pax-6 gene encodes a transcriptional regulator that recognizes target genes through its paired-type DNA-binding domain. The paired domain is composed of two distinct DNA-binding subdomains, the amino-terminal subdomain and the carboxy-terminal subdomain, which bind respective consensus DNA sequences. The human Pax-6 gene produces two alternatively spliced isoforms that have the distinct structure of the paired domain.

Supplier: Biotium

Recognizes a protein of 55 kDa, which is identified as fascin-1. Its actin binding ability is regulated by phosphorylation. Antibody to fascin-1 is a very sensitive marker for Reed-Sternberg cells and variants in nodular sclerosis, mixed cellularity, and lymphocyte depletion Hodgkin's disease. It is uniformly negative in lymphoid cells, plasma cells, and myeloid cells. Fascin-1 is also expressed in dendritic cells. This marker may be helpful to distinguish between Hodgkin lymphoma and non-Hodgkin lymphoma in difficult cases. Also, the lack of expression of fascin-1 in the neoplastic follicles in follicular lymphoma may be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased. Antibody to fascin-1 has been suggested as a prognostic marker in neuroendocrine neoplasms of the lung as well as in ovarian cancer. Fascin-1 expression may be induced by Epstein-Barr virus (EBV) infection of B cells with the possibility that viral induction of fascin in lymphoid or other cell types must also be considered in EBV-positive cases.

Supplier: Biotium

This MAb recognizes basic (Type II or HMW) cytokeratins, which include 67 kDa (CK1); 64 kDa (CK3); 59 kDa (CK4); 58 kDa (CK5); 56 kDa (CK6); 52 kDa (CK8). Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50 , 48, 46, 45, and 40 kDa. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis.

Supplier: Biotium

This MAb recognizes basic (Type II or HMW) cytokeratins, which include 67 kDa (CK1); 64 kDa (CK3); 59 kDa (CK4); 58 kDa (CK5); 56 kDa (CK6); 52 kDa (CK8). Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50 , 48, 46, 45, and 40 kDa. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis.

Supplier: Biotium

Recognizes a protein of 30-33 kDa, which is identified as CD20 (Workshop V; Code CD20.4). It is a non-Ig differentiation antigen of B-cells and its expression is restricted to normal and neoplastic B-cells, being absent from all other leukocytes and tissues. CD20 is expressed by pre B-cells and persists during all stages of B-cell maturation but is lost upon terminal differentiation into plasma cells. The protein passes through the membrane 4 times with both ends in cytoplasm and exposes one short and one longer loop to the external environment. CD20 is not glycosylated in resting B-cells and its cytoplasmic domains are differentially phosphorylated upon activation. It acts as calcium channel involved in B cell activation and cell cycle progression.

Supplier: Biotium

Recognizes a protein of 180 kDa, identified as CD11a (Leucocyte Workshop IV; Code 1524). CD11a complex with the 2 subunit of the integrin family, CD18, to form the cell surface heterodimer, LFA-1 or CD11a /C18 (aLbL). LFA-1 is expressed on all leukocytes including lymphocytes, monocytes, and granulocytes. It is involved in leukocyte adhesion to its ligands including intercellular adhesion molecule-1 (ICAM-1 or CD54), ICAM-2 (CD102), ICAM-3 (CD50) and Telencephalin (TLN) and play a role in most immune/inflammatory responses. This MAb potently blocks LFA-1 dependent homotypic cell aggregation.

Supplier: Biotium

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). CK8 is primarily found in the non-squamous epithelia and is present in 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. CK8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Anti-CK8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against CK8, CK18 and CK19). Reportedly, anti-CK8 is useful for the differentiation of lobular (ring-like, perinuclear) from ductal (peripheral-predominant) carcinoma of the breast.

Supplier: Biotium

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). CK8 is primarily found in the non-squamous epithelia and is present in 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. CK8 exists on several types of normal and neoplastic epithelia, including many ductal and glandular epithelia such as colon, stomach, small intestine, trachea, and esophagus as well as in transitional epithelium. Anti-CK8 does not react with skeletal muscle or nerve cells. Epithelioid sarcoma, chordoma, and adamantinoma show strong positivity corresponding to that of simple epithelia (with antibodies against CK8, CK18 and CK19). Reportedly, anti-CK8 is useful for the differentiation of lobular (ring-like, perinuclear) from ductal (peripheral-predominant) carcinoma of the breast.

Supplier: Biotium

This is a cocktail of four highly specific monoclonal antibodies (EGP40/826, EGP40/837, EGP40/1110, EGP40/1120) that recognize extracellular as well as intracellular domains of the epithelial cellular adhesion molecule (Ep-CAM). It is a 40-43 kDa transmembrane epithelial glycoprotein, identified as epithelial specific antigen (ESA), or Ep-CAM. Ep-CAM is expressed on baso-lateral cell surface in most simple epithelia and a vast majority of carcinomas. This epithelial antigen plays an important role as a tumor-cell marker in lymph nodes from patients with esophageal carcinoma otherwise classified as node-negative. Epithelial antigen has also been suggested as a discriminator between basal cell and baso-squamous carcinomas, and squamous cell carcinoma of the skin.

Supplier: Biotium

This MAb recognizes the 56.5 kDa (CK10); 50 kDa (CK14); 50 kDa (CK15); 48 kDa (CK16); 40 kDa (CK19) keratins of the acidic (Type I or LMW) subfamily. Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50', 48, 46, 45, and 40 kDa. MAb AE3 recognizes the 65-67, 64, 59, 58, 56, and 52 kDa keratins of basic subfamily. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. AE1/AE3 is a broad spectrum anti pan-keratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer.

Supplier: Biotium

Recognizes a cell surface glycoprotein of 80-95 kDa (CD44) on lymphocytes, monocytes, and granulocytes. The CD44 family of glycoproteins exists in a number of variant isoforms, the most common being the standard 85-95 kDa or hematopoietic variant (CD44s). Higher molecular weight isoforms are described in epithelial cells (CD44v), which are believed to function in intercellular adhesion and stromal binding. CD44 immunostaining is commonly used for the discrimination of urothelial transitional cell carcinoma in-situ from non-neoplastic changes in the urothelium.

Supplier: Biotium

This is a cocktail of four highly specific monoclonal antibodies (EGP40/826, EGP40/837, EGP40/1110, EGP40/1120) that recognize extracellular as well as intracellular domains of the epithelial cellular adhesion molecule (Ep-CAM). It is a 40-43 kDa transmembrane epithelial glycoprotein, identified as epithelial specific antigen (ESA), or Ep-CAM. Ep-CAM is expressed on baso-lateral cell surface in most simple epithelia and a vast majority of carcinomas. This epithelial antigen plays an important role as a tumor-cell marker in lymph nodes from patients with esophageal carcinoma otherwise classified as node-negative. Epithelial antigen has also been suggested as a discriminator between basal cell and baso-squamous carcinomas, and squamous cell carcinoma of the skin.

Supplier: Biotium

Reacts with the N-terminal extracellular domain of CD195. The CC chemokine receptor 5 (CCR5) is a member of the CC-chemokine receptor family, and has the characteristic structure of a 7 transmembrane G protein-coupled receptor (GPCR). CCR5 regulates trafficking and effector functions of memory/effector Th1 cells, macrophages, NK cells, and immature dendritic cells. CCR5 and its ligands play an important role in viral pathogenesis. CCR5 represents the co-receptor for macrophage (M) and dual (T cell and M)-tropic immunodeficiency viruses. Together with the CD4 binding receptor, CCR5 plays a critical role in HIV entry into the target cells. Moreover, the CCR5 ligands macrophage inflammatory protein (MIP)-1 alpha, MIP-1 beta and RANTES act as endogenous inhibitors of HIV infection, making both CCR5 and its chemokine ligands attractive therapeutic targets for HIV infection. Recent studies have also highlighted the role of CCR5 in a variety of other human diseases, ranging from infectious and inflammatory diseases to cancer.

Supplier: Biotium

This MAb recognizes human 17-26 kDa protein, which is identified as cytokine TNF-alpha (Tumor Necrosis Factor-alpha). TNF-alpha can be expressed as a 17 kDa free molecule, or as a 26 kDa membrane protein. TNF-alpha is a protein secreted by lipopolysaccharide-stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF alpha is believed to mediate pathogenic shock and tissue injury associated with endotoxemia. TNF alpha exists as a multimer of two, three, or five non-covalently linked units, but shows a single 17 kDa band following SDS PAGE under non-reducing conditions. TNF alpha is closely related to the 25 kDa protein Tumor Necrosis Factor beta (lymphotoxin), sharing the same receptors and cellular actions. TNF alpha causes cytolysis of certain transformed cells, being synergistic with interferon gamma in its cytotoxicity. Although it has little effect on many cultured normal human cells, TNF alpha appears to be directly toxic to vascular endothelial cells. Other actions of TNF alpha include stimulating growth of human fibroblasts and other cell lines, activating polymorphonuclear neutrophils and osteoclasts, and induction of interleukin 1, prostaglandin E2 and collagenase production. TNF alpha is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Supplier: Biotium

This antibody reacts with the C-terminus of TGF alpha and shows no cross-reaction with EGF and the neuropeptide synenkephalin. TGF alpha (aa50) is a growth factor with 33% homology to EGF, binds to EGFR, activates tyrosine phosphorylation of the receptor, and stimulates cell proliferation. It plays a role in tumor initiation by inducing the reversible transformed phenotype.

Supplier: Biotium

This antibody reacts with the C-terminus of TGF alpha and shows no cross-reaction with EGF and the neuropeptide synenkephalin. TGF alpha (aa50) is a growth factor with 33% homology to EGF, binds to EGFR, activates tyrosine phosphorylation of the receptor, and stimulates cell proliferation. It plays a role in tumor initiation by inducing the reversible transformed phenotype.

Supplier: Biotium

Fibronectin is an extracellular matrix glycoprotein present on most cell surfaces, in extracellular fluids and in plasma. A high molecular weight heterodimeric protein, it was originally discovered as a protein missing from the surfaces of virus-transformed cells, and it has been shown to be involved in various functions including cell adhesion, cell motility and wound healing. Alternative splicing and glycosylation give rise to several different forms of Fibronectin, some of which exhibit restricted tissue distribution or association with malignancies. It has been shown that Myofibroblasts phenotype formation correlates with the occurrence of glycosylated Fibronectin and Fibronectin splice variants in Dupuytren's disease.

Supplier: Biotium

Fibronectin is a dimeric glycoprotein of 440 kDa, which is present in cells, extracellular matrix, and blood. It possesses at least four binding sites for collagen, glycosaminoglycans, transglutaminase, and a cell surface receptor. Fibronectin is involved in cell adhesion, tissue organization, and wound healing. This MAb is directed against the peptide core and reacts with both the plasma and cellular forms of fibronectin. It blocks the fibronectin-medicated cell attachment not by disrupting the collagen-fibronectin interaction, but by interfering with the attachment of fibronectin to its receptor on the cell surface.

Supplier: Biotium

Recognizes a 40-43 kDa transmembrane epithelial glycoprotein, identified as epithelial specific antigen (ESA), or epithelial cellular adhesion molecule (Ep-CAM). Ep-CAM is expressed on baso-lateral cell surface in most simple epithelia and a vast majority of carcinomas. This antibody has been used to distinguish adenocarcinoma from pleural mesothelioma and hepatocellular carcinoma. It is also useful in distinguishing serous carcinomas of the ovary from mesothelioma. This epithelial antigen plays an important role as a tumor-cell marker in lymph nodes from patients with esophageal carcinoma otherwise classified as node-negative. Epithelial antigen has also been suggested as a discriminator between basal cell and baso-squamous carcinomas, and squamous cell carcinoma of the skin.

Supplier: Biotium

Fibronectin is an extracellular matrix glycoprotein present on most cell surfaces, in extracellular fluids and in plasma. A high molecular weight heterodimeric protein, it was originally discovered as a protein missing from the surfaces of virus-transformed cells, and it has been shown to be involved in various functions including cell adhesion, cell motility and wound healing. Alternative splicing and glycosylation give rise to several different forms of Fibronectin, some of which exhibit restricted tissue distribution or association with malignancies. It has been shown that Myofibroblasts phenotype formation correlates with the occurrence of glycosylated Fibronectin and Fibronectin splice variants in Dupuytren's disease.

Supplier: Biotium

S100 belongs to the family of calcium binding proteins. S100A and S100B proteins are two members of the S100 family. S100A is composed of an alpha and beta chain whereas S100B is composed of two beta chains. S-100 protein has been found in normal melanocytes, Langerhans cells, histiocytes, chondrocytes, lipocytes, skeletal and cardiac muscle, Schwann cells, epithelial and myoepithelial cells of the breast, salivary and sweat glands, as well as in glial cells. Neoplasms derived from these cells also express S-100 protein, albeit non-uniformly. A large number of well-differentiated tumors of the salivary gland, adipose and cartilaginous tissue, and Schwann cell-derived tumors express S-100 protein. Almost all malignant melanomas and cases of histiocytosis X are positive for S-100 protein. Despite the fact that S-100 protein is an ubiquitous substance, its demonstration is of great value in the identification of several neoplasms, particularly melanomas and their metastases.

Supplier: Biotium

Reacts with the N-terminal extracellular domain of CD195. The CC chemokine receptor 5 (CCR5) is a member of the CC-chemokine receptor family, and has the characteristic structure of a 7 transmembrane G protein-coupled receptor (GPCR). CCR5 regulates trafficking and effector functions of memory/effector Th1 cells, macrophages, NK cells, and immature dendritic cells. CCR5 and its ligands play an important role in viral pathogenesis. CCR5 represents the co-receptor for macrophage (M) and dual (T cell and M)-tropic immunodeficiency viruses. Together with the CD4 binding receptor, CCR5 plays a critical role in HIV entry into the target cells. Moreover, the CCR5 ligands macrophage inflammatory protein (MIP)-1 alpha, MIP-1 beta and RANTES act as endogenous inhibitors of HIV infection, making both CCR5 and its chemokine ligands attractive therapeutic targets for HIV infection. Recent studies have also highlighted the role of CCR5 in a variety of other human diseases, ranging from infectious and inflammatory diseases to cancer.