| Description | Clostridium histolyticum collagenases (CCH) are classified into two types ; I and II. Both are a single polypeptide with molecular weight of 114kDa - 113kDa, respectively. CCH I contains tandem domains and CCH II contain single domain for collagen binding.Application:Collagenase from Clostridium Clostridium histolyticum collagenases (CCH) are classified into two types ; I and II. Both are a single polypeptide with molecular weight of 114kDa - 113kDa, respectively. CCH I contains tandem domains and CCH II contain single domain for collagen binding.Application:Collagenase from Clostridium histolyticum has been used in a study to investigate the degradation of collagen by the cariogenic bacteria, Streptococcus mutans. Collagenase from Clostridium histolyticum has also been used in a study to investigate the survivability of collagen micronetworks in the presence of collagenase.Collagenase has been used in the preparation of arterial tissue for the study of Advanced Glycosylation End Products (AGE). The enzyme has also been used along with other proteases for the disaggregation of human tumor, mouse kidney, human brain, and lung epithelial tissues among several others. It is also effective in liver and kidney perfusion studies, digestion of pancreas, and isolation of nonparenchymal hepatocytes. The product has been used to digest forearm skin biopsies from Parkinson disease patients to grow human skin fibroblast primary cultures. The enzyme from Sigma has been used for rodent islet isolation in a study that assayed glucokinase functions... Read More | Inquire | Inquire | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Mesothelin (MSLN), also known as CAK1 and ERC, is a glycosylated cell-surface antigen present on normal mesothelial cells and over-expressed in several human tumors. The mesothelin gene encodes a ~70 kDa precursor protein that is cleaved at a dibasic proteolytic site into a 40 kDa membrane-bound protein termed MSLN and a 31 kDa shed fragment called megakaryocyte-potentiating factor (MPF) that is released from the cell. Cleaved, human MSLN remains attached to the cell surface via a GPI linkage and shares 58% amino acid sequence identity with mouse and rat MSLN. In human, alternate splicing generates additional MSLN isoforms that have either an eight amino acid insertion following Ser408 or a substituted C‑terminal region with no GPI anchor. Mesothelin is normally expressed on mesothelial cells in the pleura, pericardium, and peritoneum as well as in the developing and postnatal pancreas. It is up‑regulated in mesotheliomas and a range of carcinomas and adenomas. Mesothelin promotes tumor cell proliferation, migration, anchorage-independent growth, and tumor progression. It is co‑expressed with the tumor antigen CA125/MUC16 on advanced ovarian adenocarcinomas and interacts with this molecule to support cell adhesion. A soluble form of Mesothelin is released from tumor cells into the serum or tissue effusions... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hingePurity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： 100B, previously called S100 beta, belongs to the S100 family within the EF-hand superfamily of Ca2+ binding proteins. S100 proteins contain two EF-hand motifs that differ in affinity, separated by a hinge region with a hydrophobic cleft that is exposed upon Ca2+ binding. S100B is a 91 amino acid (aa) protein, after removal of the initial methionine, and is found as homodimers of 10.4 kDa monomers. Human S100B shares 99%, 98%, 100%, 99% and 97% aa sequence identity with mouse, rat, rabbit, equine and bovine S100B, respectively. Within the S100 family, human S100B shows the highest aa identity (59%) with S100A1. S100B is expressed primarily by astrocytes and oligodendrocytes in the central nervous system, and by Schwann cells in the peripheral nervous system. Ca2+-bound S100B interacts in vitro with at least 20 cytoplasmic proteins, including several structural molecules such as tubulin and GFAP. It can inhibit the phosphorylation of these kinase substrates and others such as tau and neuromodulin. Astrocytes can secrete S100B, which then acts in a cytokine-like manner. Nanomolar concentrations of S100B are secreted constitutively, promote proliferation, and are neurotrophic and anti-apoptotic. Blood levels of S100B reflect extracellular concentrations within the nervous system, and are elevated in Down’s syndrome, Alzheimer’s disease and Tourette’s syndrome, metabolic stress, acute brain injury and brain tumors. Micromolar concentrations of S100B can be destructive and pro-apoptotic; they induce the expression of iNOS, COX-2, IL-1, IL‑6 and TNF-alpha by microglia, astrocytes or neurons. Most extracellular actions of S100B can be mediated by RAGE (receptor for advanced glycation end products), which is also a receptor for other S100 proteins... Read More |