Protein Modification Reagents
Sigma Aldrich Fine Chemicals Biosciences Recombinant Trypsin Proteo
Trypsin is a major proteolytic enzyme synthesized as a preproenzyme by pancreas and is stored as proenzyme trypsinogen in secretory granules. Trypsin belongs to the family of serine proteases that are characterized by the catalytic triad His57 Asp102 and Ser195. Trypsin is routinely used in proteomics research for peptide mapping and protein sequence work due to its highly specific cleavage resulting in a limited number of tryptic peptides. Trypsin is a pancreatic serine endoprotease which hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues. The rate of hydrolysis is slower if an acidic residue is on either side of the cleavage site and cleavage may not occur if a proline residue is on the carboxyl side. The enzyme also exhibits esterase and amidase activities. Trypsin has an average molecular mass of 23.29 kDa and a pH optimum near 8.0. This product is prepared from recombinant trypsin porcine sequence. It is naturally devoid of chymotryptic a
ABclonal Technology MAN1C1 Rabbit pAb
Predicted to enable mannosyl-oligosaccharide 1,2-alpha-mannosidase activity. Predicted to be involved in N-glycan processing. Located in extracellular exosome.
ABclonal Technology PLA2G7 Rabbit pAb
The protein encoded by this gene is a secreted enzyme that catalyzes the degradation of platelet-activating factor to biologically inactive products. Defects in this gene are a cause of platelet-activating factor acetylhydrolase deficiency. Two transcript variants encoding the same protein have been found for this gene.