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Enterokinase, light chain |
 | | | | Enterokinase, light chain | | | |
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Substrate Specificity:
Description:
Enterokinase is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate. Enterokinase will not cleave at site followed by proline.
Source:
This preparation is purified from k. lactis containing a clone of the light chain of the bovine enterokinase gene (1,2).
Enzyme Properties
Specificity: Enterokinase is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys'.
Molecular Weight:
Theoretical: 26.3 kDa and Apparent: 31 kDa
Reaction & Storage Conditions
Concentration:
2 μg/ml
Storage Conditions:
20 mM Tris-HCl
200 mM NaCl
2 mM CaCl2
50% Glycerol
pH 7.2 @ 4°C
Storage Temperature:
-20°C
Notes
Usage notes:- Suggested Reaction Conditions: The amount of enzyme required to cleave a fusion protein in a 16 hour reaction at room temperature ranges from 0.0001% to 0.5% (w/w). Cleavage of an MPB-paramyosin-ΔSal fusion protein with an enterokinase site requires 0.0006%.
- Removal: Enterokinase will bind specifically to trypsin inhibitor agarose (e.g., Sigma T-0637).
References
- Collins-Racie, L.A. et al (1995) Biotechnology, 13, 982-987.
- Taron, C. and Colussi, P., unpublished observations.
Companion Products
Factor Xa Protease
Furin
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Proteinase K
Legal
Research Use Assurance:
This product is sold under patent license from WYETH for RESEARCH USE ONLY. Licenses for commercial manufacture or use may be obtained directly from WYETH, 87 Cambridgepark Drive, Cambridge, MA 02140.
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