The basal transcription factor TFIID plays a central role in the regulation of gene expression in Eukaryota and is a large protein complex composed of TATA box-binding protein (TBP) and 14 kinds of TBP-associated factors (TAF). TFIID directly recognizes and binds to different kinds of core promoter elements that localize near the transcription initiation site and forms a scaffold for the other basal transcription factors to assemble. At the same time, it transmits transcriptional activation signal originating from transcription regulating factors to RNA polymerase II. Taf10p is one of the subunits of TFIID and in the case of budding yeast, it is composed of 206 amino acid residues. Taf10p is also a subunit of histoneacetylase complex SAGA which is said to have an overlapping function with TFIID?This protein contains histone folds in its interior and forms dimers with Taf3p and Taf8p each. The product is prepared by immunizing rabbit with recombinant protein which was over-expressed in E. coli with a plasmid carrying the entire Taf10p protein (1-206aa) of budding yeast, and purified by chromatography.
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