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Beschreibung

Recombinant, rat GGTase I composed of an alpha- and a beta-subunit (74 and 43 kDa, respectively). The alpha-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 alpha- and a beta-subunit (74 and 43 kDa, respectively). The alpha-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.