| Quantity | 500unit, 100U, 2.5KU | 10mg, 5mg, 50mg, 1mg, 25mg | 100mg, 5mg, 50mg, 1mg, 10mg | 100µg, 10µg, 50µg, 1mg | 5×1ml, 1ml |
| Description | α-amylase is the main secretory protein constituent of saliva. It contains 496 amino acids and has two isoforms, glycosylated and non-glycosylated. α-amylase gene is located on human chromosome 1p21.1. α-amylase is mainly produced in pancreas and saliva.We are committed to bringing α-amylase is the main secretory protein constituent of saliva. It contains 496 amino acids and has two isoforms, glycosylated and non-glycosylated. α-amylase gene is located on human chromosome 1p21.1. α-amylase is mainly produced in pancreas and saliva.We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.Application:α-amylase from human saliva has been used to test α-amylase inhibitors using HPLC (high performance liquid chromatography). It also has been used to study the digestibility of human milk oligosaccharides (HMO)... Read More | Proteasome-activating peptide 1 TFA is a peptide and a potent proteasome activator. Proteasome-activating peptide 1 TFA increases the chymotrypsin-like proteasomal catalytic activity and, consequently, proteolytic rates both in vitro and in culture. Proteasome-activating peptide 1 TFA prevents Proteasome-activating peptide 1 TFA is a peptide and a potent proteasome activator. Proteasome-activating peptide 1 TFA increases the chymotrypsin-like proteasomal catalytic activity and, consequently, proteolytic rates both in vitro and in culture. Proteasome-activating peptide 1 TFA prevents protein aggregation in a cellular model of amyotrophic lateral sclerosis... Read More | 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 | Purity>95% SDS-PAGE.FunctionProbable cell adhesion protein | Inquire |