RNA Polymerase II, Carboxy-terminal Repeat Domain antibody

Details for Product No. ABIN123793
Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Antigen
Reactivity
Human
Host
Mouse
Application
Western Blotting (WB)
Pubmed 11 references available
Catalog no. ABIN123793
Quantity 125 µL
Price
457.38 $   Plus shipping costs $45.00
Shipping to United States (Change)
Availability Will be delivered in 5 to 6 Business Days

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Specificity Alpha-RNA Pol II (CTD) reacts with the CTD subunit in HeLa nuclear extract by Western blotting.
Background The carboxy-terminal repeat domain (CTD) of the largest subunit of RNA Pol II contains tandem repeats of a heptapeptide sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser which is highly conserved among eukaryotic organisms. There are two forms of RNA Pol II in vivo, designated IIO, which is extensively phosphorylated at the CTD, and IIA, which is not phosphorylated. The IIA form preferentially enters the pre-initiation complex (PIC), whereas IIO is found in the elongating complex. The kinase activity of TFIIH can mediate CTD phosphorylation, although other kinases, including Cdc2, Ctk 1, the Srb10-Srb11 kinase-cyclin pair, and P-TEF beta, have also been implicated in CTD phosphorylation. A phosphatase responsible for the dephosphorylation of the CTD has also been identified. CTD phosphatase activity is regulated by TFIIB and TFIIF. The CTD has also been implicated in pre-mRNA processing, most likely functioning as a platform for the recruitment and assembly of factors involved in pre-mRNA processing. alpha-RNA Pol II (CTD) is a mouse monoclonal antibody (ascites) without further purification.
Application Notes Recommended dilution range for Western blot analysis: 1:2000 - 1:5000.
Restrictions For Research Use only
Format Liquid
Storage -80 °C
General Lee, Greenleaf: "CTD kinase large subunit is encoded by CTK1, a gene required for normal growth of Saccharomyces cerevisiae." in: Gene expression, Vol. 1, Issue 2, pp. 149-67, 1992 (PubMed).

Feaver, Gileadi, Li et al.: "CTD kinase associated with yeast RNA polymerase II initiation factor b." in: Cell, Vol. 67, Issue 6, pp. 1223-30, 1992 (PubMed).

Lu, Flores, Weinmann et al.: "The nonphosphorylated form of RNA polymerase II preferentially associates with the preinitiation complex." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, Issue 22, pp. 10004-8, 1991 (PubMed).

Cisek, Corden: "Phosphorylation of RNA polymerase by the murine homologue of the cell-cycle control protein cdc2." in: Nature, Vol. 339, Issue 6227, pp. 679-84, 1989 (PubMed).

Moorman, Ackerman, Kowdley et al.: "Unitary anion currents through phospholemman channel molecules." in: Nature, Vol. 377, Issue 6551, pp. 737-40, 1995 (PubMed).

Chambers, Wang, Burton et al.: "The activity of COOH-terminal domain phosphatase is regulated by a docking site on RNA polymerase II and by the general transcription factors IIF and IIB." in: The Journal of biological chemistry, Vol. 270, Issue 25, pp. 14962-9, 1995 (PubMed).

Liao, Zhang, Jeffery et al.: "A kinase-cyclin pair in the RNA polymerase II holoenzyme." in: Nature, Vol. 374, Issue 6518, pp. 193-6, 1995 (PubMed).

Chambers, Dahmus: "Purification and characterization of a phosphatase from HeLa cells which dephosphorylates the C-terminal domain of RNA polymerase II." in: The Journal of biological chemistry, Vol. 269, Issue 42, pp. 26243-8, 1994 (PubMed).

Dahmus: "The role of multisite phosphorylation in the regulation of RNA polymerase II activity." in: Progress in nucleic acid research and molecular biology, Vol. 48, pp. 143-79, 1994 (PubMed).

Marshall, Peng, Xie et al.: "Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase." in: The Journal of biological chemistry, Vol. 271, Issue 43, pp. 27176-83, 1996 (PubMed).

McCracken, Fong, Yankulov et al.: "The C-terminal domain of RNA polymerase II couples mRNA processing to transcription." in: Nature, Vol. 385, Issue 6614, pp. 357-61, 1997 (PubMed).

Request Want additional data for this product?

The Independent Validation Initiative strives to provide you with high quality data. Find out more

Order hotline:

  • +1 404 474 4654
  • +1 888 205 9894 (TF)
Validation Images
back to top