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Enterokinase, Ultrapure, Porcine (Enteropeptidase)

Cat no: E3300-02

Enterokinase, Ultrapure, Porcine (Enteropeptidase)

Porcine enteropeptidase is a specific protease which cleaves after the lysine at its recognition site: Asp-Asp-Asp-Asp-Lys. Enterokinase will not cleave a site followed by proline. If a fusion tag is located in the N-terminus with an enterokinase site, enterokinase will be able to remove the fusion tag and to generate the protein exactly as you need without adding any unwanted residues. \n\nEnterokinase is a highly purified enterokinase from porcine. The enzyme has been extensively purified and tested to ensure that there are no other contaminating proteases\n\nComponents:\nE3300-02A: Enterokinase 5x100u\nE3300-02B: Cleavage Control 5x10ug\nE3300-02C: Cleavage Buffer 5x1 vial\nE3300-02D: Storage Buffer 5x1vial\n\nUnit Definition:\nOne unit is defined as the amount of E3300-02 needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25 degrees C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.\n\nDilution Buffer:\n50mM Tris-Hcl, pH 8.0, 500mM sodium chloride, 50% glycerol. \n\nAssay Conditions:\nEach reaction contains 3ug of partially purified thioredoxin-NP-27 fusion protein and varying amounts of Porcine EK. Reactions were incubated at 25 degrees C for 16 hours and analyzed on a Coomassie-stained 15% SDS gel. \n\nStorage and Stability:\nFor long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. 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

E3300-02

Size

100U

Form

Supplied as a liquid in 50mM Tris-HCl, pH 8.0, 0.5M sodium chloride, 50% glycerol.

References

1. Matsushima M, et al., (1999) J Biochem (Tokyo) May;125(5):947-51. 2. Matsushima M, et al., (1994) J Biol Chem Aug 5;269(31):19976-82. 3. Barns RJ, Elmslie RG, (1977) Biochim Biophys Acta Feb 9;480(2):450-60. 4. Baratti J, Maroux S, (1976) Biochim Biophys Acta Dec 8;452(2):488-96. 5. B arns RJ, Elmslie RG, (1976) Biochim Biophys Acta Nov 8;452(1):161-4. 6. Barns RJ, Elmslie RG, (1974) Biochim Biophys Acta Jun 18;350(2):495-8.

Alternative Names

EC=3.4.21.9

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