| Source: |
Pichia Pastoris |
| Molecular Weight: |
Approximately 43.0 kDa, a single glycosylated polypeptide chain containing 235 amino acids. |
| 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 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 following lysine residues.
Recombinant enterokinase (rEK) has been shown to be more effective than native EK in cleaving recombinant proteins. Notably, the light chain alone retains the full enzymatic activity of EK.
Among various species, recombinant bovine enterokinase (rBoEK) exhibits the highest enzymatic activity and finds extensive use in biochemical applications. |
