| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 28 kDa, a single non-glycosylated polypeptide chain containing 241 amino acids，with 6 × His at C-terminus. |
| Physical Appearance: |
Sterile liquid. |
| Formulation: |
50 mM Tris-HCl, pH8.0, 0.5 M NaCl and 50 % glycerol. |
| Endotoxin: |
Less than 1 EU/µg of rBoEKL, His as determined by LAL method. |
| Stability & Storage: |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70°C as supplied.- 3 months, -20 to -70°C under sterile conditions after opening. |
| Synonyms: |
Enterokinase, Serine Protease 7, Transmembrane Protease Serine 15 |
| Background: |
Enterokinase (EK) is an amino protease found in the mammalian duodenum, crucial for digestion. It comprises an 82–140 kDa heavy chain linked by disulfide bonds, anchoring it to the intestinal brush border membrane, and a 35–62 kDa light chain containing the catalytic subunit. Both chains originate from a single precursor cleaved by a trypsin-like protease. EK specifically recognizes the amino acid sequence DDDDK and cleaves peptide bonds after lysine residues.
Recombinant EK (rEK) has been shown to be more efficient than native EK in cleaving recombinant proteins. Interestingly, the light chain alone retains the full enzymatic activity of EK.
Among EK variants, recombinant bovine enterokinase (rBoEK) exhibits the highest enzymatic activity and finds widespread use in biochemical applications. rBoEK, fused with a 6 × His-tag, binds to Ni2+ affinity chromatography columns, facilitating its purification from digestion systems. |
