| Description | Hyaluronidase is widely present in nature.In humans, it is present in a number of organs and body fluids. Hyaluronidase is found in the secretions of virus, bacteriophage, fungi and bacteria. It is also present in nematode and leeches secretions. Snakes and scorpions produce hyaluronidase in their Hyaluronidase is widely present in nature.In humans, it is present in a number of organs and body fluids. Hyaluronidase is found in the secretions of virus, bacteriophage, fungi and bacteria. It is also present in nematode and leeches secretions. Snakes and scorpions produce hyaluronidase in their venom. Hyaluronidase is also secreted by bees, spiders, wasps, hornets, caterpillars, fishes and lizards. ApplicationHyaluronidase from Streptomyces hyalurolyticus has been used:in the preparation of DMEM/F-12 (Dulbecco′s modified eagle medium/nutrient mixture F-12) media for the isolation and purification of single cells from dissociated tumour tissue；as a component of digestion solution for the derivation of germline stem cells from testicular tissue... Read More | Inquire | Purity>95% SDS-PAGE.FunctionB Cell Activating Factor Receptor (BAFF-R), also named tumor necrosis factor receptor superfamily member 13C, is a member of the TNFR superfamily. It is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ Purity>95% SDS-PAGE.FunctionB Cell Activating Factor Receptor (BAFF-R), also named tumor necrosis factor receptor superfamily member 13C, is a member of the TNFR superfamily. It is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFF receptor is a type III transmembrane protein containing a single extracellular phenylalanine-rich domain and binds with high specificity to BAFF (TNFSF13B). It enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. BAFF receptor/BAFF signaling plays a critical role in B cell survival and maturation... Read More | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis... Read More | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionSerine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect Purity> 95% by SDS-PAGE and HPLC analyses.FunctionSerine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. May be involved in the formation or reorganization of synaptic connections as well as for synaptic plasticity in the adult nervous system. May protect neurons from cell damage by tissue-type plasminogen activator... Read More |