You Searched For: gastroin

Supplier: Biotium

Description: Beta-catenin associates with the cytoplasmic portion of E-cadherin, which is necessary for the function of E-cadherin as an adhesion molecule. In normal tissues, beta-catenin is localized to the membrane of epithelial cells, consistent with its role in the cell adhesion complex. In breast ductal neoplasia, beta-catenin is usually localized in cellular membranes. However, in lobular neoplasia, a marked redistribution of beta-catenin throughout the cytoplasm results in a diffuse cytoplasmic pattern. Immuno-staining of beta-catenin and E-cadherin is helps in the accurate identification of ductal and lobular neoplasms, including a distinction between low-grade ductal carcinoma in situ (DCIS) and lobular carcinoma. Additionally, some rectal and gastric adenocarcinomas demonstrate diffuse cytoplasmic beta-catenin staining and a lack of membranous staining, mimicking the staining pattern observed with lobular breast carcinomas.

Supplier: Biotium

Description: This antibody recognizes a glycoprotein of ~200 kDa, identified as carbonic anhydrase IX (CAIX/gp200). Carbonic Anhydrases (CAs) are members of a large family of zinc metallo-enzymes that catalyze the reversible hydration of carbon dioxide. CAs are involved in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption and the formation of aqueous humor, cerebrospinal fluid, saliva and gastric juice. They show extensive diversity in distribution and in their subcellular localization. CA IX is specifically expressed in clear-cell renal carcinomas.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.

Supplier: Biotium

Description: This antibody recognizes a glycoprotein of ~200 kDa, identified as carbonic anhydrase IX (CAIX/gp200). Carbonic Anhydrases (CAs) are members of a large family of zinc metallo-enzymes that catalyze the reversible hydration of carbon dioxide. CAs are involved in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption and the formation of aqueous humor, cerebrospinal fluid, saliva and gastric juice. They show extensive diversity in distribution and in their subcellular localization. CA IX is specifically expressed in clear-cell renal carcinomas.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®647 is a far-red fluorescent dye (Ex/Em 650/665 nm) with excellent brightness. It also is compatible with super-resolution imaging by STORM.

Catalog Number: (10750-616)

Supplier: Prosci

Description: FAM120A Antibody: FAM120A (C9orf10) is a member of the constitutive coactivator of PPAR gamma family and the gene was mapped to chromosome 9q22.31. FAM120A was recently detected within the Pur-alpha-containing mRNA-protein complex in the brain. As a novel RNA-binding protein, FAM120A is a critical component of the oxidative stress-induced survival signaling. It may participate in mRNA transport in the cytoplasm. FAM120A activates src family kinases and acts as a scaffolding protein enabling src family kinases to phosphorylate and activate PI3-kinase. FAM120A protects cells from apoptosis through activation of SRKs in response to oxidative stress. Blocking of the survival signaling mediated by FAM120A, which sensitizes the cancer cells to stress-induced apoptosis, may be a novel therapeutic approach for gastric scirrhous carcinoma cells.

Catalog Number: (10663-406)

Supplier: Bioss

Description: The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.

Catalog Number: (10663-418)

Supplier: Bioss

Description: The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.

Catalog Number: (10663-420)

Supplier: Bioss

Description: The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.

Catalog Number: (10399-766)

Supplier: Bioss

Description: The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.

Catalog Number: (10399-764)

Supplier: Bioss

Description: The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.

Catalog Number: (10405-202)

Supplier: Bioss

Description: The finding that mutations in DNA mismatch repair genes are associated with hereditary nonpolyposis colorectal cancer (HNPCC) has resulted in considerable interest in the understanding of the mechanism of DNA mismatch repair. Initially, inherited mutations in the MSH2 and MLH1 homologs of the bacterial DNA mismatch repair genes MutS and MutL were demonstrated at high frequency in HNPCC and were shown to be associated with microsatellite instability. The demonstration that 10 to 45% of pancreatic, gastric, breast, ovarian and small cell lung cancers also display microsatellite instability has been interpreted to suggest that DNA mismatch repair is not restricted to HNPCC tumors but is a common feature in tumor initiation or progression. Two additional homologs of the prokaryotic MutL gene, designated PMS1 and PMS2, have been identified and shown to be mutated in the germline of HNPCC patients.

Catalog Number: (76107-844)

Supplier: Bioss

Description: Leucine-rich repeats (LRRs) are 20-29 amino acid motifs that mediate protein-protein interactions. The primary function of these motifs is to provide a versatile structural framework for the formation of these protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutation in the genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 3B (LRRC3B), also designated LRP15, is a 259 amino acid protein that contains 3 LRR repeats. The gene encoding LRRC3B is a tumor suppressor gene that is regulated by DNA methylation. Decreased expression of LRRC3B has been shown in colorectal cancer and gastric cancer, making LRRC3B a candidate marker for those cancers.

Catalog Number: (10486-328)

Supplier: Bioss

Description: Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.

Catalog Number: (10486-334)

Supplier: Bioss

Description: Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.

Catalog Number: (10486-332)

Supplier: Bioss

Description: Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.

Catalog Number: (10486-336)

Supplier: Bioss

Description: Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.

Catalog Number: (10254-018)

Supplier: Bioss

Description: Carbonic anhydrases (CAs), also designated carbonate dehydratases or carbonate hydrolyases, form a large family of genes that encode zinc metalloenzymes of great physiologic importance. As catalysts of the reversible hydration of carbon dioxide, these enzymes participate in a variety of biologic processes, including respiration, acid-base balance, bone resorption and calcification as well as the formation of aqueous humor, cerebrospinal fluid, saliva and gastric acid. Genes in the ?carbonic anhydrase family encode either active carbonic anhydrase isozymes or 揳catalytic?(devoid of CO2 hydration activity) carbonic anhydrase-related proteins. Human CA I (CA1) is encoded by the CA1 gene, which maps to a region on chromosome 8 that harbors a cluster of CA genes. CA I localizes to the cytoplasm and research indicates that a severe deficiency of CA I does not result in any obvious hematological or renal consequences.