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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

product line

BioReagent

solubility

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

shipped in

wet ice

storage temp.

2-8°C

Related Categories

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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pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Certificates of Analysis (COA)

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Pauline Floch et al.
Gut pathogens, 6, 20-20 (2014-07-06)
A gamma-glutamyl transpeptidase (GGT) is produced by up to 31% of strains of Campylobacter jejuni isolates. C. jejuni GGT is close to Helicobacter pylori GGT suggesting a conserved activity but unlike the latter, C. jejuni GGT has not been studied
Yusuke Murasawa et al.
The Journal of biological chemistry, 288(40), 29170-29181 (2013-08-22)
Versican G1 domain-containing fragments (VG1Fs) have been identified in extracts from the dermis in which hyaluronan (HA)-versican-fibrillin complexes are found. However, the molecular assembly of VG1Fs in the HA-versican-microfibril macrocomplex has not yet been elucidated. Here, we clarify 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)
Maciej Suski et al.
Biochimica et biophysica acta, 1834(12), 2463-2469 (2013-08-31)
Excessive action of angiotensin II on mitochondria has been shown to play an important role in mitochondrial dysfunction, a common feature of atherogenesis and kidney injury. Angiotensin-(1-7)/Mas receptor axis constitutes a countermeasure to the detrimental effects of angiotensin II on
View All Related Papers

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

Validation of RNAi Knockdown Using Multiple Reaction Monitoring and Protein-AQUA

The field of proteomics is continually looking for new ways to investigate protein dynamics within complex biological samples. Recently, many researchers have begun to use RNA interference (RNAi) as a method of manipulating protein levels within their samples, but the ability to accurately determine these protein amounts remains a challenge. Fortunately, over the past decade, the field of proteomics has witnessed significant advances in the area of mass spectrometry. These advances, both in instrumentation and methodology, are providing researchers with sensitive assays for both identification and quantification of proteins within complex samples. This discussion will highlight some of these methodologies, namely the use of Multiple Reaction Monitoring (MRM) and Protein-AQUA.

Protocols

Procedure for Enzymatic Assay of Trypsin (EC 3.4.21.4)

This procedure is for products with a specification for Trypsin activity using Na-Benzoyl-L-arginine ethyl ester (BAEE) as a substrate. The procedure is a continuous spectrophotometric rate determination (A253, Light path = 1 cm).

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