Anti-GTF2H2 / BTF2 p44 / TFIIH, clone PCRP-GTF2H2-1B9

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Initiation of transcription from protein-coding genes in eukaryotes is a complex process that requires RNA polymerase II, as well as families of basal transcription factors. Binding of the factor TFIID (TBP) to the TATA box is believed to be the first step in the formation of a multiprotein complex containing several additional factors, including TFIIA, TFIIB, TFIIE, TFIIF and TFII. TFIIH (or BTF2) is a multisubunit transcription/DNA repair factor that possesses several enzymatic activities. The core of TFIIH is composed of five subunits, designated p89 (XPB or ERCC3), p62, p52, p44 and p34. Additional subunits of the TFIIH complex are p80 (XPD or ERCC2) and the ternary kinase complex composed of Cdk7, cyclin H and Mat1. Both p89 and p80 have ATP-dependent helicase activity. The p62, p52 and p44 subunits have been shown to be involved in nucleotide excision repair. Protein function: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. The N-terminus of GTF2H2 interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter. [The UniProt Consortium]