Enterokinase, Light Chain, Recombinant, Porcine (Enteropeptidase)

Enterokinase is a specific protease that cleaves after a lysine preceded by three 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 if located in the N-terminal section of proteins, useful for removing unwanted tags. \n\nMolecular Weight: Theoretical MW: 21.88kD. Apparent MW on SDS-PAGE: ~40kD\n\nActivity: 2U/ul. \n\nUnit Definition: One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 22 degrees C in a buffer containing 25 mM Tris-HCl, pH 8.0.\n\nSupplied With:\n1X Enterokinase Dilution/Storage Buffer, 1x2ml\n10X Enterokinase Cleavage Buffer, 1x1ml\nCleavage Control Protein (lyophilized), 1x10ug. (The MW of control protein is 26kD before cleavage. After cleavage, the MWs of the two fragments are 17kD and 9kD).\n\nStorage and Stability:\nStore at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. Note: Can stand at 37 degrees C for seven days without losing activity. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

E3300-01A

Size

100U

Form

The enzyme component is supplied as a liquid in proprietary buffer formulation.

Purity

(same/more than) 90%. Enzyme has been extensively purified and tested to ensure that there are no other contaminating proteases.

References

1. Palmai-Pallag, T., et al., (2005) FEBS J. 272: 2901-2911. 2. Liew, O.W., et al., (2005) Protein Expr. Purif. 41: 332-340. 3. Peng, L., et al., (2004) J. Biotechnol. 108: 185-192.