| Description | Purified Native Human Alpha 1 Antitrypsin, Human PlasmaBulk Qty Available.An acute-phase plasma protein found at 95-350 mg per 100 ml that functions as a protease inhibitor. Clinically, its deficiency is associated with two major diseases: pulmonary emphysema and early onset/juvenile hepatic Purified Native Human Alpha 1 Antitrypsin, Human PlasmaBulk Qty Available.An acute-phase plasma protein found at 95-350 mg per 100 ml that functions as a protease inhibitor. Clinically, its deficiency is associated with two major diseases: pulmonary emphysema and early onset/juvenile hepatic cirrhosis. It is elevated in inflammatory conditions, malignancies, liver disease and pregnancy and also after surgical trauma and use of oral contraceptives. The simultaneous quantitative determination of alpha-1-PI and ceruloplasmin permits differential diagnosis of liver afflictions.Activity: When tested with active-site titrated porcine pancreatic trypsin using Na-Benzoyl-L-Arginine-para-Nitroanilide Hydrochloride (L-BAPNA) as substrate, it is 75-100% inhibitory.Prepared from plasma shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.For research use or for use in further manufacturing... Read More | Dezamizumab (anti-Serum Amyloid P) is a fully humanized recombinant monoclonal IgG1 anti-serum amyloid P component (SAP) antibody, with potential anti-amyloid activity. Dezamizumab (anti-Serum Amyloid P) triggers immunotherapeutic clearance of amyloid. Dezamizumab (anti-Serum Amyloid P) can be used Dezamizumab (anti-Serum Amyloid P) is a fully humanized recombinant monoclonal IgG1 anti-serum amyloid P component (SAP) antibody, with potential anti-amyloid activity. Dezamizumab (anti-Serum Amyloid P) triggers immunotherapeutic clearance of amyloid. Dezamizumab (anti-Serum Amyloid P) can be used in research of Amyloid light-chain (AL) amyloidosis... Read More | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Usually used industrially for the resolution of chiral compounds and the transesterification production of biodiesel | 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 |