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Enterokinase, Light Chain, Porcine


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Z01003 Enterokinase, Light Chain, Porcine
100 IU
$65.00



Synonyms Enterokinase; EK
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.
Source P. pastoris
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.

Molecular Weight Theoretical MW: 21,880 Da
The apparent MW on SDS-PAGE: about 40,000 Da
Concentration 50 ul, 2 U/ul
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.

Enterokinase, Light Chain, Porcine
Enterokinase, Light Chain, Porcine

Fig.1. Each reaction contains 50 μg of purified IL-8 fusion protein and varying amount of GenScript recombinant porcine enterokinase.
The reactions were incubated at 22°C for 16 hours and analysed on a coomassie-stained SDS-PAGE (15%). Units of enzyme used per
reaction is listed below :
Lane 1. 1 U
Lane 2. 0.1 U
Lane 3. 0.01 U
Lane 4. 0.001 U
Lane 5. 0.0001 U
Lane 6. 0.00001 U
Lane 7. 0.000001 U
Lane 8. 0 U

Enterokinase, Light Chain, Porcine

Enterokinase, Light Chain, Porcine

Enterokinase, Light Chain, Porcine

Enterokinase, Light Chain, Porcine

Enterokinase, Light Chain, Porcine


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.

Petersen J., et al. T-cell receptor recognition of HLA-DQ2–gliadin complexes associated with celiac disease. Nat Struct Mol Biol. 2014May;21(5):480-8

Chen RR., et al. A CADHERIN‐LIKE PROTEIN FROM THE BEET ARMYWORM Spodoptera exigua (LEPIDOPTERA: NOCTUIDAE) IS A PUTATIVE Cry1Ac RECEPTOR. Arch Insect Biochem Physiol. 2014May;86(1):58-71

Petersen J., et al. T-cell receptor recognition of HLA-DQ2–gliadin complexes associated with celiac disease. Nat Struct Mol Biol. 2014May;21(5):480-8

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