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T6567

Sigma-Aldrich

Trypsin from porcine pancreas

Proteomics Grade, BioReagent, Dimethylated

Synonym(s):

Porcine Trypsin, Trypsin for Mass Spectropetry

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About This Item

EC Number:
232-650-8
MDL number:
MFCD01775455
UNSPSC Code:
12352204
NACRES:
NA.56

biological source

Porcine pancreas

Quality Level

200

product line

BioReagent

solubility

1 mM HCl: soluble 1 mg/mL, clear, colorless

shipped in

wet ice

storage temp.

2-8°C

General description

Trypsin is a serine protease that is usually used in biochemistry and biology as an important enzymatic reagent. This method produces a highly purified trypsin product suitable for proteomics research. Proteomics Grade ideal for use in both solution and in-gel tryptic digestions. Trypsin, a serine protease, is present in the digestive system of several vertebrates.

Application

Trypsin from porcine pancreas is used for the following applications:
  • In-gel protein digestion and MALDI-TOF mass spectrometry analysis
  • Electrospray Ionization Mass Spectrometry (ESI-MS) analysis
  • Surface proteome profiling of L. plantarum
  • Gel Filtration, Ultracentrifugation, and Rotary Shadowing Electron Microscopy
  • Mass spectrometry

Biochem/physiol Actions

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. It hydrolyzes peptide bonds specifically at the carboxyl side of arginine and lysine residues.. The enzyme also exhibits esterase and amidase activities. Trypsin acts as a cell culture tool. It is used to hydrolyze allergenic proteins to produce hypoallergenic milk in industries.

Other Notes

2024 CiteAb Award Winner for Supplier Succeeding in Parkinson′s Research

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Product No.
Description
Pricing

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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Daniela M Remus et al.
Journal of bacteriology, 195(3), 502-509 (2012-11-24)
Sortases are transpeptidases that couple surface proteins to the peptidoglycan of Gram-positive bacteria, and several sortase-dependent proteins (SDPs) have been demonstrated to be crucial for the interactions of pathogenic and nonpathogenic bacteria with their hosts. Here, we studied the role
Masayuki Shimoda et al.
Cell transplantation, 21(2-3), 465-471 (2012-07-17)
Porcine islets are considered to be a promising resource for xenotransplantation. However, it is difficult to isolate porcine islets because of the marked fragility and rapid dissociation. Endogenous trypsin is one of the main factors to damage islets during the
Hui Zheng et al.
Molecules (Basel, Switzerland), 18(11), 13425-13433 (2013-11-02)
A novel chemoenzymatic one-pot multicomponent synthesis of thiazole derivatives was developed. A series of thiazole derivatives were synthesized with high yields up to 94% under mild enzyme-catalyzed conditions. The blank and control experiments reveal that trypsin from porcine pancreas (PPT)
Biomarkers of acute and chronic pancreatitis
Kaphalia BS
Biomarkers in Toxicology, 279-289 (2014)
Cristina C Santini et al.
Scientific reports, 9(1), 10865-10865 (2019-07-28)
Small molecule inhibitors of BRAF and MEK have proven effective at inhibiting tumor growth in melanoma patients, however this efficacy is limited due to the almost universal development of drug resistance. To provide advanced insight into the signaling responses that
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Articles

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

Evaluation of Recombinant, Chemically Treated Trypsin in Proteomics and Protein Characterization Assays

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Protocols

Trypsin Assay Procedure (EC 3.4.21.4)

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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