| Description | The Collagenase-Elastase blend is a tissue dissociation enzyme cocktail for cell isolation. The tissue dissociation process consists in the release of functional and viable cells from animal tissue, with minimal impact on the cell’s viability. The main reagent used for the tissue dissociation The Collagenase-Elastase blend is a tissue dissociation enzyme cocktail for cell isolation. The tissue dissociation process consists in the release of functional and viable cells from animal tissue, with minimal impact on the cell’s viability. The main reagent used for the tissue dissociation process is Collagenase. Collagenases are enzymes that break down the native collagen that holds animal tissues together. The second enzyme found in our blend is Elastase: a serine protease that also hydrolyzes amides and esters. It is produced in the pancreas as an inactive zymogen and activated in the duodenum by trypsin. While elastase will hydrolyze a wide variety of protein substrates, it is unique among proteases in its ability to hydrolyze native elastin, a substrate not attacked by trypsin, chymotrypsin or pepsin. Elastin, a matrix component of tissues involved in stretching processes, is found in highest concentrations in the elastic fibers of connective tissues. Elastase is frequently used to dissociate tissues which contain extensive intercellular fiber networks. For this purpose, it is usually used with other enzymes such as collagenase, trypsin, and chymotrypsin. Elastase is the enzyme of choice for the isolation of Type II cells from the lung... Read More | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Ubiquitin-like protein of the SUMO family; conjugated to lysine residues of target proteins; associates with transcriptionally active genes; regulates chromatid cohesion, chromosome segregation, APC-Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Ubiquitin-like protein of the SUMO family; conjugated to lysine residues of target proteins; associates with transcriptionally active genes; regulates chromatid cohesion, chromosome segregation, APC-mediated proteolysis, DNA replication and septin ring dynamics; human homolog SUMO1 can complement yeast null mutant... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Binds electronegative LDL (LDL-) and mediates the cytokine release induced by LDL-... Read More | Purity>95% SDS-PAGEFunctionLipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus | 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 |