||The Transcription Factor IIA (TFIIA) has been shown to bind to the TBP-DNA complex and to increase the affinity of TBP for the TATA element. Human TFIIA consists of three subunits of 35 kDa (α-subunit), 19 kDa (β-subunit) and 12 kDa (γ-subunit). The α- and β-subunits are derived from the product, p55, of a single gene by an unknown mechanism. However, recombinant p55, in combination with a 12 kDa subunit (γ-subunit), retains native TFIIA activity. The p55 subunit of TFIIA is isolated from a strain of E. coli that contains the coding sequence of human p55 of TFIIA under the control of T7 promoter. The p12 subunit of TFIIA is isolated from a strain ofE. colithat contains the coding sequence for human TFIIA γ-subunit under the control of T7 promoter. Recombinant TFIIA can be used to super-shift TBPDNA complex in a gel mobility shift assay and to stimulate activator-dependent transcriptionin vitro. TFIIA is greater than 95% pure and does not contain any detectable protease, DNase, or RNase activities.
||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, 20% glycerol.
||1 ng is sufficient for a gel mobility shift assay in a 20 μl reaction, 20 ng are sufficient for in vitro transcription assay and 100 ng are sufficient for protein-protein interaction assays.
||> 95% by SDS-PAGE.
||Quality guaranteed for 12 months, store at -80℃. Avoid freeze / thaw cycles.