Anti-RNA polymerase II subunit B1 (phospho-CTD Ser-7) Antibody, clone 4E12

RPB1 (RNA polymerase II subunit B1) is the catalytic component of RNA polymerase II which synthesizes mRNA and non-coding RNAs. During transcription, elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of RPB1, which acts as an assembly platform for factors regulating transcription initiation, elongation, termination and mRNA processing. Phosphorylation occurs mainly at residues ′Ser-2′ and ′Ser-5′ of the tandem 7 residue repeats in the C-terminal domain (CTD), which activates Pol II. This phosphorylation also can occur at ′Ser-7′ of the heptapepdtide repeat. This antibody recognizes the ′Ser-7′ CTD residue of RPB1.

~220 kDa observed

Epitope: Phosphorylated Ser7 of the C-terminal domain (CTD)

Ovalbumin-conjugated linear peptide corresponding to human RNA polymerase II subunit B1 phosphorylated at Ser7 of the C-terminal domain (CTD).

Anti-RNA polymerase II subunit B1 (phospho-CTD Ser-7) Antibody, clone 4E12 is a highly specific rat monoclonal antibody & that targets RNA Polymerase & has been tested in western blotting.

Chromatin Immunoprecipitation Analysis: A representative lot was used by an independent laboratory to immunoprecipitate RNA polymerase II subunit B1 (phospho-CTD Ser-5) in ChIP (Chapman, R., et al. (2007). Science. 318(5857):1780-1782.).
Demonstrated to react with human RBP1 in Ni et al., 2011. Transcription 2:5, 237-242

Demonstrated to react with human RBP1 in Ni et al., 2011. Transcription 2:5, 237-242

This antibody recognizes RNA polymerase II subunit B1 phosphorylated at Ser7 of the C-terminal domain (CTD).

Rat monoclonal IgG1κ with 0.05% sodium azide.

Evaluated by Western Blotting in untreated and lambda phosphatase treated NIH/3T3 cell lysate.

Western Blotting Analysis: A 1:2,000 dilution from a representative lot detected RNA polymerase II subunit B1 (phospho-CTD Ser-7) in 10 μg of untreated NIH/3T3 cell lysate.

Replaces: 04-1570