| Description | Collagenase AF-1 is derived from C. histolyticum using a production process completely free of any animal based components. Thus, any risk of transmission of potential animal-derived pathogens is excluded. This highly purified collagenase, often in combination with Neutral Protease AF is suitable Collagenase AF-1 is derived from C. histolyticum using a production process completely free of any animal based components. Thus, any risk of transmission of potential animal-derived pathogens is excluded. This highly purified collagenase, often in combination with Neutral Protease AF is suitable for the dissociation of sensitive cells from several tissues. The animal-free enzymes have been shown to be highly effective for the isolation of islets of Langerhans from human pancreas intended for transplantation and stromal vascular fraction (SVF) from adipose tissue and tumor cells.ApplicationCollagenase AF-1 can be used for several cell isolations. Our bigger packaging size of 2000 U is ideal for human islet isolation, whereas the smaller size of 150 U can be used for tumor cell isolation, isolation of TILs or SVF from adipose tissue. SpecificationsActivity (Wünsch) ≥ 3.00 U/mg*.Endotoxin ≤ 10.0 EU**/mg (Ph. Eur.)Microbiological examination: Total aerobic microbial count (TAMC), total combined yeast/moulds count (TYMC), absence of Clostridia.Endproduct is 0.22 µm filtered. (Clostridiopeptidase A, Collagenase A)EC 3.4.24.3 • Mr Mr 70 000 - 120 000 (collagenase) • CAS [9001-12-1]References and Definitions*Unit definitions:Collagenase: 1 U according to Wünsch (2) catalyzes the hydrolysis of 1 µmol 4-phenylazobenzyloxycarbonyl-L-prolyl-L-leucylglycyl-L-prolyl-D-arginine per minute at 25 °C, pH 7.1.**Endotoxin: Ph. Eur. [1 Endotoxin Unit is equal to 1 International Unit of a WHO appoved reference standard endotoxin (RSE)].References1. Bond, M.D. & van Wart, H.E. (1984) Biochemistry 23, 3077-30912. Wünsch, E. & Heidrich, H.G. (1963) Hoppe-Seyler´s Z. Physiol. Chem. 333, 149-51... Read More | FunctionSignal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. Binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. Does not FunctionSignal-transducing molecule. The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize gp130 for initiating signal transmission. Binds to IL6/IL6R (alpha chain) complex, resulting in the formation of high-affinity IL6 binding sites, and transduces the signal. Does not bind IL6. May have a role in embryonic development (By similarity). The type I OSM receptor is capable of transducing OSM-specific signaling events.Post-translationalPhosphorylation of Ser-782 down-regulates cell surface expression. Heavily N-glycosylated... 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 visualized with Coomassie® Blue StainingDescription:NG2, also known as CSPG4, MCSP, and AN2, is a 400-500 kDa transmembrane chondroitin sulfate proteoglycan (CSPG) with a protein core of approximately 300 kDa. The extracellular region can be proteolytically shed fromPurity:>95%, by SDS-PAGE visualized with Coomassie® Blue StainingDescription:NG2, also known as CSPG4, MCSP, and AN2, is a 400-500 kDa transmembrane chondroitin sulfate proteoglycan (CSPG) with a protein core of approximately 300 kDa. The extracellular region can be proteolytically shed from the cell surface. Mature human NG2 consists of a 2195 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 77 aa cytoplasmic domain. Within aa 1583-2224, human NG2/CSPG4 shares 83% aa sequence identity with mouse and rat CSPG4. NG2 binds to the extracellular matrix proteins Laminin, Tenascin, and Collagens II, V, and VI as well as to the growth factors FGF-2 and PDGF-AA. NG2 is expressed on glial cell progenitors known as O2A cells or NG2 glia. These cells are neuronally responsive and differentiate primarily into oligodendrocytes but also into astrocytes. NG2 associates with PDGF R alpha and the AMPA R subunit GluR2. It is up-regulated on microglial cells during inflammation and contributes to the induction of inflammatory mediators. Various CSPGs in the brain inhibit neurite outgrowth through interactions with Nogo Receptor/NgR1 and NgR3. This recombinant protein product corresponds to the last 5 CSPG repeats, a region which can independently inhibit neurite outgrowth. NG2 is also expressed on vascular mural cells and capillaries. It promotes vascular endothelial cell (EC) migration and angiogenesis through interactions with Galectin-3 and Integrin alpha 3 beta 1 on EC, Plasminogen, and Angiostatin. NG2 is also expressed on a variety of tumors where it contributes to tumor cell adhesion, motility, and invasion... Read More | Background：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisitsBackground：Tumor necrosis factor alpha (TNF-alpha ), also known as cachectin and TNFSF2, is the prototypic ligand of the TNF superfamily. It is a pleiotropic molecule that plays a central role in inflammation, immune system development, apoptosis, and lipid metabolism. Rat TNF-alpha consisits of a 35 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 179 aa extracellular domain (ECD). Within the ECD, rat TNF-alpha shares 94% aa sequence identity with mouse and 69%-76% with bovine, canine, cotton rat, equine, feline, human, porcine, and rhesus TNF-alpha. TNF-alpha is produced by a wide variety of immune, epithelial, endothelial, and tumor cells. TNF-alpha is assembled intracellularly to form a noncovalently linked homotrimer which is expressed on the cell surface. Cell surface TNF-alpha can induce the lysis of neighboring tumor cells and virus infected cells, and it can generate its own downstream cell signaling following ligation by soluble TNFR I. Shedding of membrane bound TNF-alpha by TACE/ADAM17 releases the bioactive cytokine, a 55 kDa soluble trimer of the TNF-alpha extracellular domain. TNF-alpha binds the ubiquitous 55-60 kDa TNF RI and the hematopoietic cell-restricted 80 kDa TNF RII, both of which are also expressed as homotrimers. Both type I and type II receptors bind TNF-alpha with comparable affinity, although only TNF RI contains a cytoplasmic death domain which triggers the activation of apoptosis. Soluble forms of both types of receptors are released and can neutralize the biological activity of TNF-alpha. Post-translational modificationsThe soluble form derives from the membrane form by proteolytic processing.The membrane form, but not the soluble form, is phosphorylated on serine residues.Dephosphorylation of the membrane form occurs by binding to soluble TNFRSF1A/TNFR1.O-glycosylated; glycans contain galactose, N-acetylgalactosamine and N-acetylneuraminic acid... Read More |