24 kDa (Reducing)
2mM HCl，2mM Ca2+，ph3.0 @ 25°C
Recombinant trypsin should be dissolved by adding an appropriate amount of 2 mM HCl. The resulting solution should be at an appropriate concentration.
Store at -25 ~ -15℃ for 2 years
1. Kunitz,M. Crystalline soybean trypsin inhibitor. 2. General properties. J. Gen. Physiol. 30: 291-307[J]. Journal of General Physiology, 1947, 30(4):291-310.
2. Olsen, J. V . Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues[J].Molecular & Cellular Proteomics, 2004, 3(6):608-614.
Trypsin specifically cleaves peptide bonds at the carboxyl side of the amino acids lysine and arginine, making it highly effective in breaking down proteins into smaller peptides. This specificity is due to the structure of its active site, which accommodates these positively charged amino acids. The enzyme operates optimally at a slightly alkaline pH, which is consistent with the pH environment of the small intestine.
In addition to its digestive function, trypsin has significant applications in biotechnology and research. It is commonly used in cell culture to dissociate adherent cells from surfaces, a process known as trypsinization. Furthermore, trypsin is employed in proteomics for protein digestion prior to mass spectrometry analysis, enabling the identification and characterization of proteins.
Recombinant trypsin lyophilized powder
This product is a recombinantly expressed porcine trypsin that is free from animal-derived components. It is suitable for applications in cell culture, cell fermentation, enzymatic hydrolysis of proteins, tissue dissociation, and insulin production. The exact dosage should be optimized based on specific experimental conditions.
1. Substrate must be in phosphate-free buffer to prevent calcium precipitation with both reconstituted enzyme and enzyme buffer.
2. Storage buffer:2mM HCl, pH3.0.
ΔA/min 0.056
Specific Activity≥4000USP/mg
2μg (R: reducing condition, N: non-reducing condition).
≥95%
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