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Enterokinase, human recombinant, BioVision

Supplier: BioVision
>90% Pure active Human Recombinant Enterokinase.

Sequentially cleaves carboxyl side of D-D-D-D-K.

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light consists of 235 amino acid residues.



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Size Supplier No. VWR Catalog Number Unit Price Quantity
10 μg 7136-10 10009-204 Each (10µG) Retrieving Restricted
50 μg 7136-50 10009-206 Each (50µG) Retrieving Restricted
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SPECIFICATIONS

Enzyme Name Enterokinase
Species Human
Source CHO cells
Purity ≥90%
Molecular Weight 97.5 kDa
Formulation Sterile filtered through a 0.2 micron filter. Lyophilized from 10 mM Sodium Phosphate, pH 7.5 and 1 mM Calcium Chloride.
Reconstitution Instructions Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml.
Synonyms Serine protease 7, transmembrane protease serine 15
Type Recombinant
Endotoxin Content < 0.2 ng/μg of protein (<2EU/μg).
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