| Description | The Collagenase-Hyaluronidase 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 The Collagenase-Hyaluronidase 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 Hyaluronidase. Hyaluronidase is a hyaluronic acid-metabolizing enzyme, who degrades Hyaluronic Acid. Hyaluronic Acid increase tisue and membranes permeability and is one of the main components of the extracellular matrix, contribuing significantly to cell proliferation and migration. Combination of Collagenase and Hyaluronidase is usually used for the isolation of cells from the extracellular matrix... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily and is important in the regulation of myeloid cell activity. The human CD200 R1 cDNA encodes a 325 Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily and is important in the regulation of myeloid cell activity. The human CD200 R1 cDNA encodes a 325 amino acid (aa) precursor that includes a 28 aa signal sequence, a 215 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 61 aa cytoplasmic domain. The ECD is composed of one Ig-like V-type domain and one Ig-like C2-type domain. Within the ECD, human CD200 R1 shares 56% aa sequence identity with both mouse and rat CD200 R1. Alternate splicing of the human CD200 R1 mRNA generates four isoforms, two of which are truncated in the Ig-C2 domain and are likely secreted. In human, a separate CD200 RL gene encodes a protein that shares 81% ECD aa identity with CD200 R1. In mouse, at least four genes for CD200 R1-like molecules have been described. CD200 R1 expression is restricted primarily to mast cells, basophils, macrophages, and dendritic cells, while its ligand, CD200, is widely distributed. Disruption of this receptor-ligand system by knockout of the CD200 gene in mice leads to increased macrophage number and activation and predisposition to autoimmune disorders. Association of CD200 with CD200 R1 takes place between their respective N-terminal Ig-like domains. The capacity of CD200 R1-like molecules to interact with CD200 is controversial. CD200 R1 propagates inhibitory signals despite lacking a cytoplasmic ITIM (immunoreceptor tyrosine-based inhibitory motif). CD200 R1-like molecules, in contrast, are potentially activating receptors by means of their association with DAP12. CD200R1 signaling inhibits the expression of proinflammatory molecules including TNFs, IFNs, and inducible nitric oxide synthase in response to selected stimuli, which implicate that CD200/CD200R1 inhibitory signaling pathway plays a prominent role in limiting inflammation in a wide range of inflammatory diseases. Furthermore, the CD200/CD200R inhibitory signaling constitutes one of the most suitable endogenous immunoregulatory molecule candidate to restore the immune suppressive status of the CNS altered in chronic neuroinflammatory situations... Read More | Purity>95% SDS-PAGEFunctionHas hepatocyte mitogenic activity | Product IntroductionKGF keratinocyte growth factor (KGF), a cytokine identified by Rubin et al (1989) from the culture supernatant of embryonic lung fibroblasts, is an FGF family member, namely FGF-7.KGF is secreted by stromal cells and its receptor is distributed in epithelial cells, where it is a Product IntroductionKGF keratinocyte growth factor (KGF), a cytokine identified by Rubin et al (1989) from the culture supernatant of embryonic lung fibroblasts, is an FGF family member, namely FGF-7.KGF is secreted by stromal cells and its receptor is distributed in epithelial cells, where it is a potent epithelial cell specific growth factor, and its mitogenic activity is mainly expressed in keratinocytes, which can specifically promote epithelial cell proliferation, migration and differentiation, and is closely related to many aspects, such as organ development, wound repair, tumorigenesis and immune reconstitution.Osrhkgf was created using genetic recombination, expressed from rice endosperm cells and through a protein purification process.Specification parametersSource Oryza sativaAppearance white lyophilized powderActivity ≥1.0×105IU/mgpH 6.5-7.5Molecular weight 19.0 kDEndotoxin ≦0.1EU/ugCAS No 148348-15-6Matters needing attentionReconstitution: it is recommended to lyophilize the powder of osrhkgf to 100-200 UG/ml with sterile water to make further dilutions with other solvents.The dissolved osrhkgf could be stored for 2-7 days at 4 ◦ C and used up as soon as possible.To not use for short periods, store at - 20 ℃.Use as soon as possible after opening to avoid contamination.Limitations of useIt is suitable for research, laboratory and production use only and cannot be used directly in humans... Read More | Purity> 97 % by SDS-PAGE and HPLC analyses.FunctionReceptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation whichPurity> 97 % by SDS-PAGE and HPLC analyses.FunctionReceptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase... Read More |