Trypsin from bovine pancreas(Purified,Sequencing Grade II) - ≥150 units/mg protein (at least 8,625 BAEE/2875 USP/NF units/mg protein), high purity , CAS No.9002-07-7

Item Number

T128770

• Synonyms: Peptidyl peptide hydrolase
• Specifications & Purity: ≥150 units/mg protein (at least 8,625 BAEE/2875 USP/NF units/mg protein)
• Storage Temp: Store at -20°C
• Shipped In: Dry ice
• Grade: EnzymoPure™

Product Description

Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.
Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins