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Recombinant Bovine Enterokinase

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C46101 500IU $235.00

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  • Product Name Recombinant Bovine Enterokinase
  • Brief Description Recombinant Protein
  • Host Species E.coli
  • Endotoxin Less than 1 EU/μg of rBoEKL as determined by LAL method.
  • Target Name Recombinant Bovine Enterokinase
  • Alternative Names Enterokinase, Serine Protease 7, Transmembrane Protease Serine 15
  • Calculated MW Approximately 28 kDa, a single
  • SDS-PAGE MW Sterile liquid.
  • Formulation 50 mM Tris-HCl, pH 8.0, 0.5 M NaCl and 50 % glycerol.
  • Storage One year when stored at -20 ˚C. Avoid repeated freeze thaw cycles.
Application Details

Unit Definition: One unit is defined as the amount of enzyme needed to cleave 50 μg of fusion protein in 16 hours to 95 % completion at 25 °C in a buffer containing 25 mM Tris-HCl, pH 7.6, 50 mM NaCl, and 2 mM CaCl2. < div>
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Physical Appearance: Sterile liquid< div>
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Endotoxin: Less than 1EU µg of rBoEKL as determined by LAL method< div>

  • Recombinant Bovine Enterokinase - SAB | Signalway Antibody

Enterokinase (EK) is an amino protease existing in duodenum of mammal and is involved in digestion. It consists of a disulfide-linked 82�C140 kDa heavy chain which anchors enterokinase in the intestinal brush border membrane and a 35�C62 kDa light chain which contains the catalytic subunit. Additionally, both of the chains are derived from a single precursor that is cleaved by a trypsin-like protease. EK can specially recognize the amino acid sequence DDDDK, and digest the peptide bond after the lysine residue. rEK was report to be more effective than nature EK in cleaving recombinant proteins,.Furthermore, the light chain possesses the whole enzyme activity of EK. rBoEK has the highest activity than EK of other species and is used wildly in biochemical applications.
1. Yuan LDandHua ZC. 2002. Protein Expr Purif, 25: 300-4. 2. Peng L, Zhong X, Ou J, et al. 2004. J Biotechnol, 108: 185-92. 3. Light AandJanska H. 1991. J Protein Chem, 10: 475-80. 4. Kubitzki T, Minor D, Mackfeld U, et al. 2009. Biotechnol J, 4: 1610-8.
    Please let us know if you have published research using #C46101 so that we can cite your reference.
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