The human Transcription Factor IIE (TFIIE) is composed of 56 kDa ( α) and 34 kDa ( β) subunits and is shown to be a heterotetramer. 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. TFIIE binds to RNA polymerase II in solution and joins the pre-initiation complex probably concomitant with RNA polymerase II and TFIIF.
Forma física
Clear and colorless frozen liquid solution
Nota de preparación
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
The Journal of biological chemistry, 266(14), 9304-9308 (1991-05-15)
Mammalian RNA polymerase II transcription factor IIE (TFIIE) was purified to apparent homogeneity. The activity copurified with polypeptides of 34 and 56 kDa. The 56-kDa subunit was sufficient for low levels of transcription activity in a transcription system reconstituted in
Proceedings of the National Academy of Sciences of the United States of America, 87(23), 9163-9167 (1990-12-01)
Human transcription factor TFIIE, a ubiquitous factor required for transcription initiation by RNA polymerase II, was purified to homogeneity by a combination of conventional and HPLC steps. The purified TFIIE contained equimolar amounts of 57-kDa (TFIIE-alpha) and 34-kDa (TFIIE-beta) polypeptides
The general transcription factor IIE (TFIIE) is an essential component of the eukaryotic RNA polymerase II initiation complex. We have isolated human complementary DNA clones for both the subunits of TFIIE. Using purified recombinant proteins we find that both subunits
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