Trypsin, Sequencing Grade, modified – TRSEQZ

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 Worthington 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.

TRSEQZ is typically used for protein sequencing, mapping and structure studies.

Trypsin, treated with L-(tosylamido-2-phenyl) ethyl chloromethyl ketone to inhibit contaminating chymotryptic activity, chemically modified to promote stability and further purified to remove autolysis fragments, resulting in a highly stable trypsin product resistant to autolysis while retaining specificity.

• SUPPLIER:

  Worthington Biochemical

• STATUS:

  In Stock

• SIZE:

  100 µg