Description
Trypsin is a serine protease secreted by the pancreas, which recognizes the sites of lysine or arginine in proteins and cuts at the carboxyl end of the lysine or arginine residues. This product is a recombinant porcine trypsin expressed by Pichia pastoris, produced under GMP regulations, free of any animal-derived components, and free from animal virus contamination (such as swine influenza virus, porcine parvovirus, etc.). It naturally lacks chymotrypsin activity and has been filtered to remove bacteria. The activity of this product is inhibited by serine protease inhibitors such as PMSF and TLCK, and metal ion chelating agents such as EDTA.
Yeasen Recombinant Trypsin activity is based on the internationally accepted activity (USP) and is superior to imported similar products. The HPLC content of β-Trypsin can reach over 80%, with high storage stability and a proteomics enzymatic digestion miss-cut rate that is 50% lower than imported products.
Features
1.High activity，good stability.
2.Free of any protease inhibitors，such as PMSF.
Applications
Protein analysis, such as protein mass spectrometry, sequencing, and peptide mapping analysis.
Specifications
|
Source |
Yeast recombinant expression |
|
Purity |
＞95% |
|
Concentration |
2.0 mg/mL |
|
Specific activity |
＞6800 USP Unit/mg |
|
β-Trypsin |
＞80% |
|
α-Trypsin |
＜20% |
|
Storage Buffer |
1 mM HCL |
|
Unit Definition |
At 25°C, pH 7.6, in a reaction system of 3.2 mL (1 cm light path), the increase in absorbance at 253 nm by 0.003 per minute during the enzymatic digestion of BAEE is defined as one USP unit. |
Storage
The product can be stored at -25 ~ -15℃ for two years.