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T1143

Sigma-Aldrich

Trypsinogen from bovine pancreas

essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein (E1%/280, after activation to trypsin)

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About This Item

Numéro CAS:
Numéro CE :
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.56

Source biologique

bovine pancreas

Pureté

85-100% (UV)

Forme

essentially salt-free, lyophilized powder

Activité spécifique

≥10,000 BAEE units/mg protein (E1%/280, after activation to trypsin)

Poids mol.

23,981 Da by calculation

Technique(s)

mass spectrometry (MS): suitable

Solubilité

H2O: soluble 10 mg/mL

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

bovine ... TRYP8(282603)

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Description générale

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.

Application

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)

Actions biochimiques/physiologiques

Phytic acid complexed with calcium has been shown to increase the secretion of trypsinogen unable to be cleaved for activation. It also reduced the stabilization effect of calcium on activated trypsin. The active form of trypsinogen, referred to as trypsin, cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. It also hydrolyzes ester and amide linkages of synthetic derivatives of amino acids such as, benzoyl L-arginine ethyl ester (BAEE), p-toluenesulfonyl-L-arginine methyl ester (TAME), etc.

Définition de l'unité

One BAEE unit is equal to a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C and a reaction volume of 3.2 mL (1 cm light path).

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Classification des risques

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Faceshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

An effect of calcium ions on the activity, heat stability, and structure of trypsin.
T Sipos et al.
Biochemistry, 9(14), 2766-2775 (1970-07-07)
TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS.
K A WALSH et al.
Proceedings of the National Academy of Sciences of the United States of America, 52, 884-889 (1964-10-01)
Thomas M Dillon et al.
Journal of chromatography. A, 1053(1-2), 299-305 (2004-11-17)
Analytical characterization of monoclonal antibodies has been hindered by the lack of appropriate chromatographic methods to be used in conjunction with high-resolution MS. Current methodologies for standard RP-HPLC are incompatible with antibodies due to irreproducibility, low recovery, short column lifetimes
The effect of calcium and phytic acid on the activation of trypsinogen and stability of trypsin.
Caldwell, R.
Journal of Agricultural and Food Chemistry, 40, 43-46 (1992)
Keil B, et al.
The Enzymes, 3, 250-275 null

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