| Description | Hepases, derived from microorganisms, are polysaccharide lyases that cleave the a-1,4 glycosidic bond between N-acetylglucosamine (GlcNAc) and hexuronic acid (GlcUA/IdoUA) through a typical b-elimination mechanism. They generate an unsaturated double bond with specific absorption at 232 nm at the C4Hepases, derived from microorganisms, are polysaccharide lyases that cleave the a-1,4 glycosidic bond between N-acetylglucosamine (GlcNAc) and hexuronic acid (GlcUA/IdoUA) through a typical b-elimination mechanism. They generate an unsaturated double bond with specific absorption at 232 nm at the C4 and C5 positions of hexuronic acid, which facilitates the analysis and detection of enzymatic hydrolysis products. HEPases have been identified in Hep/HS degrading bacteria, such as Flavobacterium heparinum, Bacteroides thetaiotaomicron，Bacteroides stercoris，Sphingomonas, Bacillus, Pseudomonas aeruginosa[ Wait. HEPases can be divided into three categories based on substrate selectivity: HEPase I selectively degrades the high sulfation zone in Hep and HS; HEPase III selectively degrades the low sulfur acidification zone in HS and Hep; HEPase II can degrade both Hep and HS simultaneously. The above three types of HEPases belong to endonucleases, and recently a heparin exonuclease family (exoHEPases) has been discovered for the first time. HEPases, as an important tool enzyme, are widely used in the structural and functional research of Hep/HS, the production of low molecular weight heparin, quality testing and consistency evaluation of heparin drugs, etc. We can provide customers with various known types of HEPase enzyme preparations according to their needs, meeting their various requirements from analysis and detection to large-scale production.ApplicationHeparinase I and III Blend from Flavobacterium heparinum has been used in:the digestion of heparan sulfate from ovine vitreous；human embryonic kidney cells；glycosaminoglycans from arterial tissues；P0 retinae digestion... Read More | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.ApplicationUseful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondriaDetermination of enzyme localization on membranesTreatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone | 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 |