| Cat# | TRA-043 |
| Specification | 2KU,20KU,200KU,2MU,20MU |
| Description | Enterokinase (EK) is a highly specific serine protease that recognizes the DDDDK sequence and cleaves at the C-terminus of lysine residues (where proline cannot follow K). . Hanhai recombinant enterokinase (rEK) is expressed in Escherichia coli and engineered from the natural enterokinase light chain fragment (containing a 6×His-tag). It exhibits higher specific activity and cleavage specificity, making it particularly suitable for the production of peptide drugs such as GLP-1 and its analogues. |
| Applications | Removes labeled peptides from N-terminal and Met-N-terminal fusion proteins using DDDDK as the cleavage site, leaving no residual amino acids. |
| Form | Clear, colorless to pale yellow liquid |
| Unit Definition | One unit is defined as the amount of enzyme required to cleave 95% of a fusion protein stored in 25 mM Tris-HCl (pH 8.0) buffer at 25°C within 12 to 16 hours. |
| Molecular Weight | 27.0 kDa |
| Purity | ≥ 95% by SDS-PAGE |
| Storage | Store at -25°C to -15°C maintains stability for up to 2 years. |
| Download Datasheet: |  |
