||The human Transcription Factor IIE (TFIIE) is composed of56 kDa (α) and 34 kDa (β) subunits and is shown to be a heterotetramer. The 56 kDa subunit contains a region similar to a zincbinding domain and a region sharing homology with the catalytic loop of a kinase domain. TFIIE binds to RNA Polymerase II in solution and joins the preinitiation complex probably concomitant with RNA Polymerase II and TFIIF. The recombinant protein is purified from anE. colistrain that contains the coding sequence of human TFIIE α -subunit under the control of T7 promoter. Although 56 kDa subunit of the TFIIE contains a zincbinding domain like region, both subunits are required to reconstitute the functional transcription factor. Protein is purified greater than 95% homogeneous and contains no detectable protease, DNase, and RNase activity.
||For in vitro use only.
||Liquid. Supplied in 20 mM Tris-HCl pH 8.0, 100 Mm KCl, 0.2 mM EDTA, 1 mM DTT and 20% glycerol.
||20 ng are sufficient for an in vitro reconstituted transcription assay in the presence of 34 kDa subunit, 100 ng are sufficient for a protein-protein interaction assay.
||> 95% by SDS-PAGE.
||Quality guaranteed for 12 months, store at -80℃. Avoid freeze / thaw cycles.