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分子别名
Trypsin(pig),Porcine pancreas,Recombinant Trypsin分子量
24 kDa (Reducing)
纯度
＞95% by SDS-PAGE活性
≥4000USP/mg标签
No Tag性状
Lyophilized Powder缓冲体系
2mM HCl，2mM Ca2+，ph3.0 @ 25°C
溶解方法
Recombinant trypsin should be dissolved by adding an appropriate amount of 2 mM HCl. The resulting solution should be at an appropriate concentration.
储存条件
Store at -25 ~ -15℃ for 2 years
文献引用
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
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.
- In a 3.2ml reaction system using BAEE as substrate, the UV absorption at 253nm increased by 0.003 per min using cuvette with 1 cm optical path, which was defined as 1 USP trypsin activity unit
生物活性
ΔA/min 0.056
Specific Activity≥4000USP/mg
电泳
2μg (R: reducing condition, N: non-reducing condition).
反相高效液相色谱(RP-HPLC)
≥95%
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