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Bovine Enterokinase / PRSS7 Protein (His Tag)

DatasheetSpecific ReferencesReviewsRelated ProductsProtocols
Bovine TMPRSS15 Protein Product Information
Synonym:ENTK, PRSS7
Protein Construction:A DNA sequence encoding the bovine TMPRSS15 (NP_776864.1) (Ile801-His1035) was expressed with a polyhistidine tag at the C-terminus.
Expressed Host:Yeast
Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Bovine TMPRSS15 Protein QC Testing
Purity:> 95 % as determined by SDS-PAGE.
Endotoxin:Please contact us for more information.
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Ile 801
Molecule Mass:The recombinant bovine TMPRSS15 consists 241 amino acids and predicts a molecular mass of 27.1 kDa.
Formulation:Lyophilized from sterile 10 mM Tris-HCL, 2 mM CaCL2, 100 mM Nacl, 50 % glycerol, pH 7.2.
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Bovine TMPRSS15 Protein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Bovine TMPRSS15 Protein SDS-PAGE
Bovine Enterokinase / PRSS7 Protein (His Tag) SDS-PAGE
Other TMPRSS15 Recombinant Protein Products
Enterokinase / PRSS7 Background

Enterokinase, or Enteropeptidase is a type II transmembrane, which is a member of the trypsin family of serine proteases, and plays a key role in mammalian metabolism. It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, either trypsin or possibly duodenase. Active enteropeptidase then converts the pancreatic precursor, trypsinogen, to trypsin by cleavage of the specific trypsinogen activation peptide, Asp-Asp-Asp-Asp-Lys- Ile that is highly conserved in vertebrates. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. Enterokinase consists of two subunits linked by a disulfide bond. The heavy chain achors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which has the same mechanism of action as trypsin and chymotrypsin. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. Because of its high specificity towards the amino acid sequence (Asp)(4)-Lys, enterokinase is a potential tool for the cleavage of fusion proteins, which are gaining more importance in biopharmaceutical production. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.

Bovine Enterokinase / PRSS7 References
  • Light A, et al. (1989) Enterokinase (enteropeptidase): comparative aspects. Trends Biochem Sci. 14(3): 110-2.
  • Kubitzki T, et al. (2009) Application of immobilized bovine enterokinase in repetitive fusion protein cleavage for the production of mucin 1. Biotechnol J. 4(11): 1610-8.
  • Zheng XL, et al. (2009) Enteropeptidase, a type II transmembrane serine protease. Front Biosci (Elite Ed). 1: 242-9.
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    Catalog: 10002-B08Y-20
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