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Enterokinase/EK Protein, Bovine, Recombinant
Catalog No. TMPY-04626
Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.
Enterokinase/EK Protein, Bovine, Recombinant
Catalog No. TMPY-04626
Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.
| Pack Size | Price | Availability | Quantity |
|---|---|---|---|
| 100 U | $91 | In Stock |
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| Biological Activity | One unit is defined as the amount of enzyme needed to cleave 50μg fusion protein in 16 hours at 20℃ in a buffer containing 20 mM Tris-HCl, 50 mM NaCl, and 2 mM CaCl2>, pH 7.4. |
| Description | Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins. |
| Species | Bovine |
| Expression System | P. pastoris (Yeast) |
| Tag | Tag Free |
| Synonyms | EK, Enterokinase, PRSS7, Enteropeptidase, EC 3.4.21.9, Serine protease 7, ENTK, MGC133046. |
| Construction | A DNA sequence encoding the light chain (Ile 801-His 1035) of bovine Enterokinase (NP_776864) was expressed. |
| Protein Purity | > 95%, as determined by SDS-PAGE and SEC-HPLC Analysis |
| Molecular Weight | 26.1kDa (predicted); 45kDa (reducing condition, due to glycosylation) |
| Endotoxin | < 1.0 EU/μg of the cytokine as determined by the LAL method |
| Reconstitution | Resuspend the enzyme powder with sterile water. Keep reconstituted enzyme at -20℃ in aliquots. |
| Stability & Storage | It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots. |
| Shipping | In general, Lyophilized powders are shipping with blue ice. |
| Research Background | Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins. |
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