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Catalog Number | orb90006 |
---|---|
Category | Proteins |
Description | Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The seven-amino-acid recognition site for rTEV is Glu-Asn-Leu-Tyr-Phe-Gln-Gly with cleavage occurring between Gln and Gly. The optimal temperature for cleavage is 30C; however, the enzyme can be used at temperatures as low as c. The rTEV contains His tag.The rTEV is purified by proprietary chromatographic techniques. |
Purity | Greater than 90.0% as determined by RP-HPLC and analysis by SDS-PAGE |
Conjugation | Unconjugated |
Target | TEV |
Biological Origin | E.coli |
Biological Activity | 10,000 Units/1mg. |
Storage | Store rTEV at -80°C for long term or at -20°C for 10 months. Please prevent freeze/thaw cycles. |
Buffer/Preservatives | The rTEV contains 0.50 Tris-HCl pH 8.0, 10mM DTT and mM EDTA. |
Alternative names | rTEV protein, TEV protein, P1 protease protein Read more... |
Note | For research use only |
Application notes | Unit Definition One unit of rTEV cleaves > 85% of ug control substrate in h at 30C. < br>< strong>Experiment Notes: A number of variables can be changed to optimize the cleavage of any specific protein. The amount of rTEV, the temperature of the incubation, and the time needed for cleavage may be examined. If the protein of interest is heat-labile, then 4C incubations are recommended. Reactions at 4C will require longer incubation times and/or more rTEV. |
Expiration Date | 6 months from date of receipt. |
Unconjugated | |
not determined | |
33 kDa (runs at 25–40 kDa on SDS-PAGE) | |
E.coli |
Greater than 90.0% as determined by analysis by SDS-PAGE. | |
Escherichia Coli |
> 95% by SDS-PAGE analyses. | |
28.4 kDa, observed by reducing SDS-PAGE. | |
Escherichia coli. |