| 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 | Inquire | Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionInhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, Purity> 97 % by SDS-PAGE and HPLC analyses.Additional sequence informationThis product is for the mature full length protein. The signal peptide is not included.FunctionInhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：KGF (keratinocyte growth factor), also known as FGF-7 (fibroblast growth factor-7), is one of 22 known members of the mouse FGF family of secreted proteins that plays a key role in development, morphogenesis, angiogenesis, wound healing, and tumorigenesis (1-4). KGF expression is restricted to cells of mesenchymal origin. When secreted, it acts as a paracrine growth factor for nearby epithelial cells (1). KGF speeds wound healing by being dramatically upregulated in response to damage to skin or internal structures that results in high local concentrations of inflammatory mediators such as IL-1 and TNF-alpha. (2, 5). KGF promotes cell migration and invasion, and mediates melanocyte transfer to keratinocytes upon UVB radiation (6, 7). It has been used ectopically to avoid chemotherapy-induced oral mucositis in patients with hematological malignancies (1). Deletion of KGF affects kidney development, producing abnormally small ureteric buds and fewer nephrons (8). It also impedes hair follicle differentiation (9). The 194 amino acid (aa) KGF precursor contains a 31 aa signal sequence and, like all other FGFs, an ~120 aa beta -trefoil scaffold that includes receptor- and heparin-binding sites. KGF signals only through the IIIb splice form of the tyrosine kinase receptor, FGF R2 (FGF R2-IIIb/KGF R) (10). Receptor dimerization requires an octameric or larger heparin or heparin sulfate proteoglycan (11). FGF-10, also called KGF2, shares 51% aa identity and similar function to KGF, but shows more limited expression than KGF and uses an additional receptor, FGF R2-IIIc (12). Following receptor engagement, KGF is typically degraded, while FGF-10 is recycled (12). Mature human KGF, which is active across species, shares 98% aa sequence identity with bovine, equine, ovine and canine, 96% with mouse and porcine, and 92% with rat KGF, respectively... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Function：Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence |