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EMS0007 Sigma-Aldrich

Recombinant Trypsin Dimethlyated

Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris

Synonym: Mass Spectrometry Trypsin

  •  NACRES NA.26

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Description

General description

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 and the lysine residues have been dimethylated to further restrict autolysis. It is naturally devoid of chymotryptic activity. This high quality trypsin is suitable for proteomics use.
Specific activity: >= 10,000 BAEE units per mg protein.

Safety & Documentation

Safety Information

Signal word 
Danger
Target organs 
Respiratory system
RIDADR 
UN 1789 8 / PGIII
WGK Germany 
WGK 1
Flash Point(F) 
Not applicable
Flash Point(C) 
Not applicable

Documents

Certificate of Analysis (COA)

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Protocols & Articles

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