The human Transcription Factor IIE (TFIIE) is composed of 56 kDa (α) and 34 kDa (α) subunits and is shown to be a heterotetramer (1, 2). The 56-kDa subunit contains a region similar to a zinc-binding domain and a region sharing homology with the catalytic loop of a kinase domain (3). TFIIE binds to RNA polymerase II in solution and joins the preinitiation complex probably concomitant with RNA polymerase II and TFIIF (4).
Gene synonym include: Homo sapiens general transcription factor IIE, polypeptide 1, alpha 56kDa (GTF2E1); FE; TF2E1 and TFIIE-A.
The fusion protein is purified from an E. coli strain that contains the coding sequence of human TFIIE α subunit under the control of a T7 promoter (5). GST-TFIIEα has been used for protein-protein interactions assay (6). The purified protein is greater than 95% homogeneous based on SDS-PAGE analysis. 1 unit equals 1 nanogram of purified protein. 100 units (ng) are sufficient for a protein-protein interaction assay. variable in different lots 1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA
References: 1. Ohkuma, Y. et al., (1990) Proc. Natl. Acad. Sci. USA 87, 9163-9167 2. Inostroza, J. et al., (1991) J. Biol. Chem. 266, 9304-9308 3. Peterson, M. et al., (1991) Nature 354, 369-373 4. Flores, O. et al., (1990) J. Biol. Chem. 265, 5629-5634 5. Maldonado, E. et al., (1996) Methods Enzymol. 274, 72-100 6. Kaludov, N., et al., (2000) Nucleic Acids Res. 28, 1921-1928
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