Anti-RNA polymerase II CTD repeat YSPTSPS (phospho S2) antibody (ab70324)

Overview

• Product nameAnti-RNA polymerase II CTD repeat YSPTSPS (phospho S2) antibodySee all RNA polymerase II CTD repeat YSPTSPS primary antibodies ...
• Description
  Rabbit polyclonal to RNA polymerase II CTD repeat YSPTSPS (phospho S2)
• Tested applicationsWB more details
• Species reactivity
  Reacts with: Human
  
• Immunogen

  A phosphorylated synthetic peptide of human RNA Polymerase II, from around serine 2 of the C-terminal repeated sequence YSPTSPS.

• Positive controlWhole cell lysate from HeLa cells

Properties

• FormLiquid
• Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
• Storage bufferPreservative: 0.09% Sodium Azide
  Constituents: 0.1% BSA, Tris buffered saline
• Concentration information loading...
• PurityImmunogen affinity purified
• Clonality Polyclonal
• IsotypeIgG
• Research Areas
  • Epigenetics and Nuclear Signaling
  • Transcription
  • Polymerase associated factors
  • Pol II Transcription
  • Polymerase

  • Epigenetics and Nuclear Signaling
  • Transcription
  • RNA polymerase

Applications

Target

• FunctionDNA-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. Acts as a RNA-dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome.
• Sequence similaritiesBelongs to the RNA polymerase beta' chain family.
• Post-translational
  modificationsThe tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA promotes transcription initiation by triggering dissociation from DNA. Phosphorylation also takes place at 'Ser-7' of the heptapepdtide repeat, which is required for efficient transcription of snRNA genes and processing of the transcripts. The phosphorylation state is believed to result from the balanced action of site-specific CTD kinases and phosphatases, and a 'CTD code' that specifies the position of Pol II within the transcription cycle has been proposed.
  Dephosphorylated by the protein phosphatase CTDSP1.
  Ubiquitinated by WWP2 leading to proteasomal degradation (By similarity). Following UV treatment, the elongating form of RNA polymerase II (RNA pol IIo) is ubiquitinated UV damage sites without leading to degradation: ubiquitination is facilitated by KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow access to the nucleotide excision repair machinery.
  Methylated at Arg-1810 by CARM1. Methylation occurs only when the CTD is hypophosphorylated, and phosphorylation at Ser-1805 and Ser-1808 prevent methylation (in vitro). It is assumed that methylation occurs prior to phosphorylation and transcription initiation. CTD methylation may facilitate the expression of select RNAs.
• Cellular localizationNucleus.

Target information above from: UniProt accession P24928 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 5430 Human
  • Omim: 180660 Human
  • SwissProt: P24928 Human
  • Unigene: 270017 Human

• Alternative names
  B220 antibodyDNA directed RNA polymerase II A antibodyDNA-directed RNA polymerase II largest subunit antibody

  DNA-directed RNA polymerase II largest subunit RNA polymerase II 220 kd subunit antibodyDNA-directed RNA polymerase II subunit A antibodyDNA-directed RNA polymerase II subunit RPB1 antibodyDNA-directed RNA polymerase III largest subunit antibodyhRPB220 antibodyhsRPB1 antibodyMGC75453 antibodyPOLR2 antibodyPOLR2A antibodyPOLRA antibodyPolymerase (RNA) II (DNA directed) polypeptide A 220kDa antibodyPolymerase (RNA) II (DNA directed) polypeptide A antibodyRNA polymerase II subunit B1 antibodyRNA-directed RNA polymerase II subunit RPB1 antibodyRPB1 antibodyRPB1_HUMAN antibodyRPB220 antibodyRPBh1 antibodyRpIILS antibodyRPO2 antibodyRPOL2 antibody

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Anti-RNA polymerase II CTD repeat YSPTSPS (phospho S2) antibody images

• 

  Western blot - RNA polymerase II (phospho S2) antibody (ab70324)
  All lanes : Anti-RNA polymerase II CTD repeat YSPTSPS (phospho S2) antibody (ab70324) at 0.02 µg/ml
  
  Lane 1 : Whole cell lysate from HeLa cells with no peptide
  Lane 2 : Whole cell lysate from HeLa cells with non-phosphorylated peptide
  Lane 3 : Whole cell lysate from HeLa cells with phosphorylated S2 peptide
  Lane 4 : Whole cell lysate from HeLa cells with phosphorylated S5 peptide
  
  Lysates/proteins at 50 µg per lane.
  
  
  Observed band size : 270 kDa (why is the actual band size different from the predicted?)