TrypsinA serine protease

Trypsin (CAS 9002-07-7)

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Synonym: Trypsin 1:250 (Porcine)
Application: A serine protease
CAS Number: 9002-07-7
Molecular Weight: 23.4 kDA
* Refer to Certificate of Analysis for lot specific data (including water content).

Trypsin is a single chain polypeptide of 223 amino acid residues and is a member of the serine protease family. The active site amino acid residues of trypsin include HIs46 and Ser183. Trypsin is produced by removing the N-terminal hexapeptide from trypsinogen which is cleaved at the peptide bonds at Lys6 - lle7. This cleavage yields a single chain native form of trypsin called β-Trypsin. Ensuing autolysis of β-Trypsin results in α-Trypsin having two peptide chains bound by disulphide bonds. This enzyme predominantly cleaves peptide chains at the carboxyl side of Arginine and Lysine, with an exception when either one is followed by a Proline.

Form: Powder stabilized with lactose.
Activity: ≥ 250,000 USP units/gm
Chymotrypsin: ≥ 75,000 USP units/gm.
Unit Definition: One unit causes a change in absorbance of 0.003/min with BAEE as a substrate at 25°C, pH 7.6.

Formulation :
Trypsin (1:250)
Appearance :
Physical State :
Derived From :
Porcine pancrease
Solubility :
Soluble in Hank's Balanced Salt Solution (35 mg/ml), HCl (1 mM), and water. Insoluble in clycerol, and alcohol.
Storage :
Store at 4° C
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
WGK Germany :
Merck Index :
14: 9795
MDL Number :
EC Number :

Download SDS (MSDS)

Certificate of Analysis

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Trypsin  Product Citations

See how others have used Trypsin. Click on the entry to view the PubMed entry .

Citations 1 to 1 of 1 total

PMID: # 29805628  Liu, ZG. et al. 2018. Oncol Lett. 15: 8935-8940.

Citations 1 to 1 of 1 total
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