| Quantity | 5mg, 25mg | 500µg, 1mg | 100µg, 10µg, 50µg, 1mg | 100mg, 5mg, 50mg, 1mg, 10mg | 50mg, 10mg, 100mg, 5mg, 25mg, 1mg |
| Description | α-Lactalbumin (α-LA) is a small, acidic, whey protein that constitutes about 22% of the total proteins in human milk. It is produced by the epithelial cells of the mammary gland. α-LA is made up of two domains, a large α-helical domain, and a small β-sheet domain.Applicationα-Lactalbumin (α-LA) is a small, acidic, whey protein that constitutes about 22% of the total proteins in human milk. It is produced by the epithelial cells of the mammary gland. α-LA is made up of two domains, a large α-helical domain, and a small β-sheet domain.Application:α-Lactalbumin (α-LA) has been used as a standardto study the partitioning behavior of different monomeric proteins with exposure to amino acids on the protein surfaceto study the interaction between α-LA and cathepsin Dto study the ability of breast milk fractions to enhance the transepithelial flux of extrinsic iron in colon carcinoma cell line... Read More | Inquire | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Ubiquitin-like protein of the SUMO family; conjugated to lysine residues of target proteins; associates with transcriptionally active genes; regulates chromatid cohesion, chromosome segregation, APC-Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Ubiquitin-like protein of the SUMO family; conjugated to lysine residues of target proteins; associates with transcriptionally active genes; regulates chromatid cohesion, chromosome segregation, APC-mediated proteolysis, DNA replication and septin ring dynamics; human homolog SUMO1 can complement yeast null mutant... 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 | SHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has beenSHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has been degraded) values of 2.6 nM and 6.0 nM for MV4;11 and KYSE520 cells, respectively. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... Read More |