Trypsin Protease

Name: Trypsin Protease
Brand: SIGMA

Hydrolyzes peptide bonds at the carboxyl side of arginine and lysine residues, suitable for mass spectrometry, recombinant, expressed in Pichia pastoris

Synonym(s):

Dimethylated rTrypsin, Mass Spectrometry Trypsin, Proteomics grade rTrypsin

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About This Item

UNSPSC Code:

12352204

NACRES:

NA.26

Specific activity:

≥10,000 units/mg protein

Recombinant:

expressed in Pichia pastoris

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Properties

Product Name

Recombinant Trypsin Dimethlyated, Proteomics Grade, lyophilized powder, recombinant, expressed in Pichia pastoris

recombinant

expressed in Pichia pastoris

Quality Level

200

grade

Proteomics Grade

form

lyophilized powder

specific activity

≥10,000 units/mg protein

suitability

suitable for mass spectrometry

UniProt accession no.

P00761

shipped in

wet ice

storage temp.

2-8°C

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.