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EMS0006

Sigma-Aldrich

Recombinant Trypsin

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

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Synonym(s):
Mass Spectrometry Trypsin, Proteomics grade Trypsin, rTrypsin
NACRES:
NA.26

recombinant

expressed in Pichia pastoris

Quality Level

grade

Proteomics Grade

form

lyophilized powder

specific activity

≥10,000 units/mg protein

suitability

suitable for
suitable for mass spectrometry

UniProt accession no.

shipped in

wet ice

storage temp.

2-8°C

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Trypsin from bovine pancreas suitable for protein sequencing, lyophilized powder

T8658

Trypsin from bovine pancreas

grade

Proteomics Grade

grade

Proteomics Grade

grade

Proteomics Grade

grade

Proteomics Grade

suitability

suitable for , suitable for mass spectrometry

suitability

suitable for mass spectrometry

suitability

suitable for mass spectrometry

suitability

suitable for protein sequencing

form

lyophilized powder

form

ready-to-use solution

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

UniProt accession no.

P00761

UniProt accession no.

P00761

UniProt accession no.

P00761

UniProt accession no.

-

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

Hazard Classifications

Aquatic Chronic 2 - Eye Dam. 1 - Met. Corr. 1 - Resp. Sens. 1 - Skin Corr. 1A - Skin Sens. 1 - STOT SE 3

Target Organs

Respiratory system

Supplementary Hazards

Storage Class Code

8A - Combustible, corrosive hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Handbook of Proteolytic Enzymes (2012)
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Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 149(2), 334-344 (2008)
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Nature Communications, 14, 2855-2855 (2023)
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)

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