A phospho synthetic peptide corresponding to residues surrounding serine 1801 of human Pol II was used as an immunogen. This antibody detects Pol II phosphorylated at serine 1801.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
DNA-dependent RNA polymerase II (Pol II), a complex multisubunit enzyme, is responsible for the transcription of protein-coding genes. This complex interacts with the promoter regions of genes as well as with a variety of elements and transcription factors to determine essentially all of the parameters that govern transcription. A fraction of the large subunit of Pol II is ubiquitinated after exposing cells to UV radiation or cisplatin suggesting that ubiquitination of Pol II plays a role in the recognition and/or repair of damage to actively transcribed genes (1). Evidence demonstrates that pol II transcription termination involves two distinct and temporally separate events. The first event, termed pretermination cleavage (PTC), is mediated by sequence tracts located downstream of the poly(A) site which appear to promote heterogeneous cleavage of the nascent transcript. The second event, in which pol II disengages from the DNA template, requires that polymerase has transcribed both a PTC sequence tract and a functional poly(A) site (2).
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Western blot analysis on human brain lysates using anti-Phospho-Pol II (pS1801), 1:200,000 dilution. Cells were either (A) untreated (B) treated with AP.
