CAS Number: 9002-07-7
EC Number: 232-650-8
Enzyme Commission (EC) Number: 3.4.21.4
MDL Number: MFCD00082094
Analysis Note
One BTEE unit = 320 ATEE units
General description
Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa.
Preparation Note
Derived from New Zealand-sourced pancreas
TPCK-treated and dialyzed. Treatment with L-1-Tosylamide-2-phenylethyl chloromethyl ketone (TPCK) reduces the chymotrypsin activity which is usually present in trypsin.
Unit Definition
One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 ml (1 cm light path).
Application
Trypsin can be used to release adherent cells from tissue culture plates for passaging. Trypsin is used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins 3. Trypsin has been used in a study to assess the efficacy of polyethyleneglycol/sodium citrate aqueous two-phase extraction systems. 1 Trypsin has also been used in a study to investigate peptide-ligand affinity chromatography adsorbents. 2
Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins 3.
Biochem/physiol Actions
Trypsin cleaves peptide chains, amides and esters mainly at the carboxyl side of the amino acids lysine or arginine. Trypsin originates in the pancreas in the form of the zymogen trypsinogen3.
Form: essentially salt-free, lyophilized powder
Mol. Wt.: mol wt 23.8 kDa
Foreign Activity: Chymotrypsin ≤0.1 BTEE units/mg protein
Storage Temp.: −20°C