Trypsinogen from bovine pancreas
SIGMA/T1143 - essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein (E1%/280 , after activation to trypsin)
CAS Number: 9002-08-8
EC Number: 232-651-3
Product Type: Chemical
| assay | 85-100% (UV) |
| biological source | bovine pancreas |
| form | essentially salt-free, lyophilized powder |
| mol wt | 23,981 Da by calculation |
| Quality Level | 200  |
| solubility | H2O: soluble 10 mg/mL |
| specific activity | ≥10,000 BAEE units/mg protein (E |
| storage temp. | −20°C |
| technique(s) | mass spectrometry (MS): suitable |
| UniProt accession no. | Q29463  |
| 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) |
| Biochem/physiol Actions: | 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-argin |
| 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. |
| Packaging: | 1 g in glass bottle |
| Packaging: | 250 mg in glass bottle |
| Unit Definition: | 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). |
| Symbol |  GHS08 |
| Signal word | Danger |
| Hazard statements | H315 - H319 - H334 |
| Precautionary statements | P302 + P352 - P305 + P351 + P338 |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | 85-100% (UV) |
| activity | specific activity: ≥10,000 BAEE units/mg protein (E |
| Storage Temp. | −20°C |
| UNSPSC | 12352202 |