| Quantity | 250µg, 1mg | 100mg, 50mg, 2mg, 10mg | 50mg, 10mg, 100mg, 5mg, 25mg, 1mg | 100mg, 5mg, 50mg, 1mg, 10mg | 100µg, 50µg, 1mg |
| Description | Chylomicrons are the large triglyceride-rich lipoproteins of enteric origin that carry exogenous triglycerides into the plasma. Circulation of chylomicrons distributes dietary triglyceride to adipose tissue and to muscle. Found in post prandial plasma, chylomicrons generally clear the blood stream Chylomicrons are the large triglyceride-rich lipoproteins of enteric origin that carry exogenous triglycerides into the plasma. Circulation of chylomicrons distributes dietary triglyceride to adipose tissue and to muscle. Found in post prandial plasma, chylomicrons generally clear the blood stream in a few hours.Purity: Essentially free of other plasma lipoproteins as determined by electrophoresis using a SPIFE Vis Cholesterol gel kit for lipids and Coomassie Blue for proteins. >=95% of total lipoprotein content by electrophoresis.Product Citation:Moreno-Gordaliza E, van der Lee SJ, Demirkan A, van Duijn CM, Kuiper J, Lindenburg PW, Hankemeier T.A novel method for serum lipoprotein profiling using high performance capillary isotachophoresis.Anal Chim Acta. 2016 Nov 9;944:57-69. doi: 10.1016/j.aca.2016.09.038. Epub 2016 Oct 5.Ref:Segal,P. et al. 1984. Clinical Diagnosis and Management by Laboratory Methods, 181... Read More | 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent 4-Methylumbelliferyl α-L-iduronide (free acid) is a fluorogenic substrate for α-L-iduronidase. This is found in cell lysosomes, which is involved in the degradation of glycosaminoglycans. 4-Methylumbelliferyl-α-L-iduronide is cleaved by α-L-iduronidase to release the fluorescent moiety 4-methylumbelliferyl (4-MU). This 4-Methylumbelliferyl α-L-iduronide form is the free acid, which offers a considerable weight for weight advantage over the 4-MU iduronide salt in terms of its application dose.:For further studies, use α-L-iduronidase gene silencing:siRNA and shRNA:reagents and α-L-iduronidase gene editing:CRISPR:knockout and activation products... 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 | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Function：Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence |