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Enterokinase, Light Chain, Porcine



Cat. No.
Name
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Z01003
100 IU
$65

Protein Enterokinase, Light Chain, Porcine
Synonyms
Enterokinase; EK
Documents
Enterokinase, Light Chain, PorcineDocument-MSDS: 1447_20060502233525.PDF (PDF)
Enterokinase, Light Chain, PorcineTECHNICAL MANUAL: 2444_20061122042342.PDF (PDF)
Figures
Enterokinase, Light Chain, Porcine zoomEnterokinase, Light Chain, Porcine
Species
Porcine
Biological Activity
One unit is defined as the amount of enzyme needed to cleave 50 μg of fusion protein in 16 hours to 95% completion at 22°C in a buffer containing 25 mM Tris-HCl, pH 8.0.
Source
P. pastoris
Molecular Weight
Theoretical MW: 21,880 Da
The apparent MW on SDS-PAGE: about 40,000 Da
Description
GenScript Enterokinase is a highly purified recombinant porcine enterokinase. The enzyme has been extensively purified and tested to ensure that there are no other contaminating proteases. Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. Enterokinase will not cleave, however, if this lysine is followed by a proline. Enterokinase can remove fusion tags is located in the N-terminal section of proteins, useful for removing unwanted tags.
Formulation
GenScript enterokinase, formulated using GenScript's proprietary technology, can be shipped at room temperature. It will remain stable at 37°C for one week without losing any activity.
Storage
Store at -20°C after delivery.
Concentration
50 ul, 2 U/ul
Document-COA
  • 11726_20100125024403.PDF
  • 11904_20100220214710.PDF
  • 12262_20100310220154.PDF
  • 14297_20111114035438.PDF
  • 14298_20111114035438.PDF
  • C40111312_Z01003_COA.pdf
  • Z01003_C40211211_COA.pdf
  • Citation
    Palmai-Pallag T, et al. The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane-tethered mucins. FEBS J. Jun 2005; 272(11): 2901-2911.

    Liew OW, et al. Preparation of recombinant thioredoxin fused N-terminal proCNP: Analysis of enterokinase cleavage products reveals new enterokinase cleavage sites. Protein Expr. Purif. Jun 2005; 41(2): 332-340.

    Ren XL, .et al A Spodoptera exigua Cadherin Serves as a Putative Receptor for Bacillus thuringiensis Cry1Ca Toxin and Shows Differential Enhancement of Cry1Ca and Cry1Ac Toxicity. Appl Environ Microbiol. 2013 Sep;79(18):5576-83.

    Norbert Kartner, .et al Topology, glycosylation and conformational changes in the membrane domain of the vacuolar H ‐ATPase a subunit. J Cell Biochem. 2013 Jul;114(7):1474-87.

    Luo CH,. et al Molecular structure, expression analysis and functional characterization of APRIL (TNFSF 13) in goat ( Capra hircus). Gene. 2011 Oct 10;485(2):63-8.

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