9002-08-8

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
• CAS NO: 9002-08-8
• Molecular Formula: C39H55N9O17
• Molecular Weight: 921.9
• EINECS: 232-651-3
• Product Categories: Auxiliary Proteins;Other;Proteins and Derivatives;Peptide and protein standards for mass spectrometry analysisApplication Index;Mass Spectrometry;Proteases;Proteases&Protein Sequencing;Proteomics
• Mol File: 9002-08-8.mol
• Article Data: 0

Chemical Properties

• Appearance: /essentially salt-free, lyophilized powder
• Storage Temp.: 2-8°C
• CAS DataBase Reference: TRYPSINOGEN(CAS DataBase Reference)
• NIST Chemistry Reference: TRYPSINOGEN(9002-08-8)
• EPA Substance Registry System: TRYPSINOGEN(9002-08-8)

Safety Data

• Hazard Codes: Xn
• Statements: 36/37/38-42
• Safety Statements: 22-24-26-36/37
• WGK Germany: 3
• F: 10-21
• Hazardous Substances Data: 9002-08-8(Hazardous Substances Data)

Usage

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 form 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.

Uses

Used in Biochemistry Research:
Trypsinogen is used as a molecular weight standard (24kDa) for SDS-PAGE, a technique used to separate and analyze proteins based on their molecular weight.
Used in Protein Structure Analysis:
Trypsinogen is used for the secondary structure analysis of proteins in H2O solution using single-pass attenuated total reflection Fourier transform infrared (ATR-FT-IR) microscopy. This technique allows for the study of protein secondary structures and their interactions with other molecules.
Used in Mass Spectrometry:
Trypsinogen is used for tuning and calibration of electrospray ionization quadrupole time-of-flight (ESI-Q-TOF) mass spectrometer. This instrument is used to analyze the molecular weight and structure of proteins and other biomolecules.
Used in Infrared Spectroscopy:
Trypsinogen is used for the secondary structure analysis of proteins by infrared (IR) spectroscopy. This technique provides information about the molecular structure and conformation of proteins, as well as their interactions with other molecules.

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.