hRPB6 is a highly conserved subunit shared by all three RNA polymerases, consisting of 142 amino acid residues (1). The gene for yeast RPB6 is essential for cell viability and homologues of this subunit exist in archaeal and some viral RNA polymerases. For example the bacterial w (the fifth subunit of the bacterial RNAP core enzyme) and eukaryotic RPB6 are structural homologs. RPB6 has been shown to promote pol II complex assembly, and/or increase its stability, through specific interactions with the largest subunit of RNA pol II (2). In addition, RPB6 was found to make contact with three small subunits, RPB5, RPB7, and RPB8 and to play a role in the interaction between RNA polymerase II and the transcription elongation factor TFIIS (3).
Recombinant human RPB6 is isolated from an E. coli strain that carries the coding sequence of human RPB5 under the control of a T7 promoter.
RPB6 has been applied in protein-protein interactions assays (3). Purified protein is greater than 95% homogeneous based on SDS-PAGE analysis. 1 unit equals 1 nanogram of purified protein. 100 units are sufficient for a protein-protein interactions 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. Woychik N.A., et al.,(1990) Genes Dev 4, 313-323 2. Minakhin, L., et al., (2001) Proc. Natl. Acad. Sci. USA 98, 892-897 3. Ishiguro, A., et al., (2000) Mol. Cell Biol. 20, 1263-1270
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