EMS0006

Sigma-Aldrich

Recombinant Trypsin

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

Synonym(s):
Mass Spectrometry Trypsin
NACRES:
NA.26

Quality Level

recombinant

expressed in Pichia pastoris

assay

≥10,000 unit/mg protein

form

lyophilized powder

suitability

suitable for
suitable for mass spectrometry

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

Related Categories

General description

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 activity. This high-quality trypsin is suitable for proteomics use.

Biochem/physiol Actions

Trypsin plays an important role in the digestion of consumed protein and contributes to the activation of other proteolytic enzymes like chemotrypsin and elastase.

Signal Word

Danger

Target Organs

Respiratory system

Supp Hazards

EUH071

RIDADR

UN 1789 8 / PGIII

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Structural properties of trypsin from cold-adapted fish, arabesque greenling (Pleurogrammus azonus)
Kanno G, et al.
European Food Research and Technology, 232(3), 381-388 (2011)
Molecular characterization and gene expression of six trypsinogens in the flatfish Senegalese sole (Solea senegalensis Kaup) during larval development and in tissues
Manchado M, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 149(2), 334-344 (2008)
Handbook of Proteolytic Enzymes (2012)

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