| Description | Extinction Coefficient:1.46Product DescriptionLactoferrin is a glycoprotein present in exocrine secretions and in the secondary granules of polymorphonuclear neutrophils. Lactoferrin is known to regulate intestinal iron absorption, and to participate in the defense against bacteria. Prepared from Extinction Coefficient:1.46Product DescriptionLactoferrin is a glycoprotein present in exocrine secretions and in the secondary granules of polymorphonuclear neutrophils. Lactoferrin is known to regulate intestinal iron absorption, and to participate in the defense against bacteria. Prepared from whole blood shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA-required tests. nproducts are laboratory reagents and are not to be administered to humans or used for any drug purpose. For research or further manufacturing use only... Read More | Inquire | Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Receptor-1, PAR-1 Agonist induces activation of protein kinase C isoenzymes alpha and epsilon in human HT-29 colon carcinoma cells expressing PAR1 endogeneously. On the cellular level, Protease-Activated Receptor-1, PAR-1 Agonist and thrombin prompted HT-29 cell migration and matrix adhesion by a PKCepsilon-dependent mechanism as concluded because of the inhibition of PAR1-mediated effects by the PKC inhibitor bisindolylmaleimide I and the PKCepsilon translocation inhibitory peptide EAVSLKPT but not by the PKC inhibitor Gö 6976. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:PAR-1... Read More | Inquire | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.Animal origin free:eliminate the risk of virus presence, or of any other potential adventitious agents found in animal-derived carboxypeptitase B.Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease activities found in extracted enzymes with lower purity level. 2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 3）Less than 10ppm of recombinant trypsin... Read More |