Geranylgeranyltransferase I, GST-Fusion, His•Tag^®, Rat, Recombinant, E. coli

Recombinant, rat GGTase I composed of an α- and a β-subunit (74 and 43 kDa, respectively). The α-subunit is expressed as a GST-fusion construct with an N-terminal His•Tag sequence. Both the GST moiety and the His•Tag sequence can be utilized to facilitate enzyme capturing in prenylation and binding studies or, when desired, can also be cleaved by TEV protease. Requires Zn²⁺ for optimal activity. The enzyme is purified with Zn²⁺ tightly bound, so addition of Zn²⁺ to the reaction mix is not necessary unless further manipulation of the enzyme results in release of the ions.

Recombinant, rat GGTase I composed of an α- and a β-subunit (74 and 43 kDa, respectively). The α-subunit is expressed as a GST-fusion construct with an N-terminal His•Tag sequence. Both the GST moiety and the His•Tag sequence can be utilized to facilitate enzyme capturing in prenylation and binding studies or, when desired, can also be cleaved off by TEV protease. Requires Zn²⁺ for optimal activity.

1 pmol enzyme will transfer ≥3 pmol geranylgeranyl to RhoA in 10 min at 37°C, pH 7.2.

Toxicity: Standard Handling (A)

In 40 mM NaCl, 25 mM HEPES, 5 mM DTT, pH 7.2.

Following initial thaw, aliquot and freeze (-70°C).

Kalinin, A., et al. 2001. Protein Expr. Purif.22, 84.
Zhang, F.L., et al. 1994. J. Biol. Chem.269, 23465.
Moomaw, J.F., and Casey, P.J., 1992. J. Biol. Chem.267, 17438.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

HIS TAG is a registered trademark of Merck KGaA, Darmstadt, Germany