Description:
Transcription Factor IIE, p56 subunit (Cat# P1005)
| Species |
Human |
| Expression Host |
E. coli |
| Tag |
His-tag |
| Purity |
90% |
| Molecular Weight |
51.5 kDa. |
| Gene Accession Number |
NM_005513. |
View Full Specifications |
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| Description | The human Transcription Factor IIE (TFIIE) is composed of 56 kDa (α) and 34 kDa (β) 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).
The His tagged recombinant protein is purified from an E. coli strain that contains the coding sequence of human TFIIE α subunit under the control of T7 promoter (5).
Although the 56-kDa subunit of the TFIIE contains a zinc-binding domain like region, both subunits are required to reconstitute the functional transcription factor. | | Synonym | GTF2E1; FE; TF2E1; TFIIE-A | | Gene Sequnce | MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN SCVKEEDMLE LLKFDRKQLR
SVLNNLKGDK FIKCRMRVET AADGKTTRHN YYFINYRTLV NVVKYKLDHM RRRIETDERD
STNRASFKCP VCSSTFTDLE ANQLFDPMTG TFRCTFCHTE VEEDESAMPK KDARTLLARF
NEQIEPIYAL LRETEDVNLA YEILEPEPTE IPALKQSKDH AATTAGAASL AGGHHREAWA
TKGPSYEDLY TQNVVINMDD QEDLHRASLE GKSAKERPIW LRESTVQGAY GSEDMKEGGI
DMDAFQEREE GHAGPDDNEE VMRALLIHEK KTSSAMAGSV GAAAPVTAAN GSDSESETSE
SDDDSPPRPA AVAVHKREED EEEDDEFEEV ADDPIVMVAG RPFSYSEVSQ RPELVAQMTP
EEKEAYIAMG QRMFEDLFE | | Formulation and Storage | This protein was kept in 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 1 mM DTT and 0.2 mM EDTA. Always keep in -20°c, avoid freeze thaw cycles. | | Applications | 1 unit equals 1 nanogram of purified protein. 20 units are sufficient for an in vitro reconstituted transcription assay in the presence of 34-kDa subunit; 100 units are sufficient for a protein-protein interaction assay. variable in different lots. For research use only. | | Refewences | 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 |
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