Basic information Safety Supplier Related

TRYPSINOGEN

Basic information Safety Supplier Related

TRYPSINOGEN Basic information

Product Name:
TRYPSINOGEN
Synonyms:
  • TRYPSINOGEN
  • trypsinogen from bovine pancreas
  • TRYPSINOGEN FROM BEEF PANCREAS
  • Trypsinogen, PMSF treated from bovine pancreas
  • Trypsinogen >2500U/mg from bovine pancreas
  • Trypsinogen >2500 U/mg from bovine
  • Ttrypsinogen
CAS:
9002-08-8
MF:
C39H55N9O17
MW:
921.9
EINECS:
232-651-3
Product Categories:
  • Auxiliary Proteins
  • Other
  • Peptide and protein standards for mass spectrometry analysisApplication Index
  • Mass Spectrometry
  • Proteases
  • Proteins and Derivatives
  • Proteases&Protein Sequencing
  • Proteomics
Mol File:
9002-08-8.mol
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TRYPSINOGEN Chemical Properties

storage temp. 
2-8°C
form 
essentially salt-free, lyophilized powder
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Safety Information

Hazard Codes 
Xn
Risk Statements 
36/37/38-42
Safety Statements 
22-24-26-36/37
WGK Germany 
3
10-21

MSDS

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TRYPSINOGEN Usage And Synthesis

Uses

Trypsinogen from bovine pancreas is suitable for use in:

  • the secondary structure analysis of proteins in H2O solution using single-pass attenuated total reflection Fourier transform infrared (ATR-FT-IR) microscopy
  • tuning and calibration of electrospray ionization quadrupole time-of-flight (ESI-Q-TOF) mass spectrometer
  • the secondary structure analysis of proteins by infrared (IR) spectroscopy
  • SDS-PAGE as a molecular weight standard (24kDa)

General Description

Trypsinogen is a proenzyme (zymogen) that is activated to form trypsin. It is synthesized in the pancreas and activated by enterokinase once it reaches the lumen of the small intestine. Bovine trypsinogen is a single polypeptide chain of 229 amino acids that is cross linked by six disulfide bridges. Enterokinase cleaves a hexapeptide to from the NH2 terminus of trypsinogen at the Lys6 - Ile7 peptide bond and activates it. Trypsin, thus formed, autocatalytically activates more trypsinogen to trypsin. This native form of trypsin is called β-trypsin, which undergoes autolysis at Lys131 - Ser132 resulting in α-trypsin that is held together by disulfide bridges. Trypsin is a serine protease with His46 and Ser183 at the active site. The pH optimum of trypsin is 7 - 9.

Biochem/physiol Actions

Hereditary pancreatitis was shown to be caused by a Arg-His substitution at residue 117 of trypsinogen causing auto-activation of trypsinogen to trypsin.

TRYPSINOGENSupplier

Sigma-Aldrich
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