| Cat# | TRA-052 |
| Specification | 100U,500U,1000U |
| Description | Intestinal chymotrypsin is a highly specific serine protease consisting of a structural heavy chain and a catalytic light chain linked by a disulfide bond. The catalytic subunit recognizes the Asp-Asp-Asp-Asp-Lys sequence and cleaves at its carboxyl terminus, activating trypsinogen to initiate the proenzyme cascade. Recombinant bovine enterokinase is a high-purity light chain fragment with broad pH (4.5–9.5) and temperature tolerance, used to remove N-terminal fusion tags containing the DDDDK sequence. |
| Applications | Removal of tag peptides from N-terminal and Met-N-terminal fusion proteins; protein modification and amino acid sequence determination. |
| CAS | 9017-74-8 |
| EC | EC 3.4.21.9 |
| Synonyms | Recombinant enterokinase |
| Form | Clear, colorless to pale yellow liquid |
| Species | Bovine |
| Source | E. coli |
| Unit Definition | One unit is defined as the amount of enzyme required to cleave 95% of a fusion protein (0.5 mg) stored in 25 mM Tris-HCl (pH 8.0) buffer at 25°C within 12 to 16 hours. |
| Molecular Weight | 25.8 kDa |
| Buffer | 50 mM Tris-HCl, pH 8.0, 250 mM NaCl, 2 mM Ca2+, 50% Glycerol. |
| Gene ID | 282009 |
| Accession | P98072 |
| Storage | Store at -20°C for 2 years. |
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