|Application ||WB, IHC, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||217176 Da|
|Other Names||DNA-directed RNA polymerase II subunit RPB1, RNA polymerase II subunit B1, DNA-directed RNA polymerase II subunit A, DNA-directed RNA polymerase III largest subunit, RNA-directed RNA polymerase II subunit RPB1, POLR2A, POLR2|
|Target/Specificity||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.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Pol II Antibody Phospho (pS1801) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Regulation of gene expression levels depends on the balance between methylation and acetylation levels of tha CTD-lysines (By similarity). Initiation or early elongation steps of transcription of growth-factors- induced immediate early genes are regulated by the acetylation status of the CTD (PubMed:24207025). Methylation and dimethylation have a repressive effect on target genes expression (By similarity).|
|Cellular Location||Nucleus. Cytoplasm. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear.|
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Provided below are standard protocols that you may find useful for product applications.
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).
1. Bregman DB, et al. Proc Natl Acad 93(21):11586-90, 1996
2. Dye MJ, et al. Cell 105(5):669-81, 2001
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