| Description | A serine protease that releases bradykinin from kininogen. Present in plasma as an inactive precursor prokallikrein.Activity: 15 units per mg. One unit is defined as the amount of enzyme that hydrolyzes one umole of D-Pro-Phe-Arg-pNA per minute at 25°C, pH 7.8.Prepared from plasma shown to be A serine protease that releases bradykinin from kininogen. Present in plasma as an inactive precursor prokallikrein.Activity: 15 units per mg. One unit is defined as the amount of enzyme that hydrolyzes one umole of D-Pro-Phe-Arg-pNA per minute at 25°C, pH 7.8.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests... Read More | Inquire | Inquire | Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Fibronectin (FN) is a particularly important and well-studied component of the extracellular matrix, and is known to play a key role in cell adhesion, growth, spreading, migration, differentiation and proliferation. Fn is a 200-250 kDa glycoprotein composed of 2 subunits bound via a disulfide bond. Currently, the Fn is purified from the plasma, which however is limited by the availability of supply. The the recombinant human fibronectin (OsrhFN) was expressed in the rice endosperm platform, which is animal component free and has high purity, and has been demonstrated has the same physical and chemical with the plasma derived Fn. OsrhFN provides a safety solution to replace the plasma derived FN.pH value: 6.0-8.0... 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 |