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  1. Link

    recombinant-human-rna-polymerase-ii-ctd-repeat-ysptsps-protein-ab81834.pdf

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Epigenetics and Nuclear Signaling Transcription Polymerase associated factors Pol II Transcription
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Recombinant Human RNA polymerase II CTD repeat YSPTSPS protein (ab81834)

  • Datasheet
Reviews (1)Q&A (1)

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Key features and details

  • Expression system: Escherichia coli
  • Purity: > 95% SDS-PAGE
  • Tags: GST tag N-Terminus
  • Suitable for: SDS-PAGE

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Description

  • Product name

    Recombinant Human RNA polymerase II CTD repeat YSPTSPS protein
    See all RNA polymerase II CTD repeat YSPTSPS proteins and peptides
  • Purity

    > 95 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Accession

    P24928
  • Protein length

    Protein fragment
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGL EFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVL DIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTH PDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIA WPLQGWQATFGGGDHPPKSDLVPRGSPMGHMGSSPSLRSGSVGGAMSPSY SPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSY SPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYS PTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSP TSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPT SPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTS PSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSP TYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPT SPGYSPTSPTYSLTSPAISPDDSDEEN
    • Predicted molecular weight

      68 kDa including tags
    • Amino acids

      1586 to 1970
    • Tags

      GST tag N-Terminus
    • Additional sequence information

      Recombinant protein isolated from an E. coli strain that carries the coding sequence of human RNA pol II c-terminal domain under control of a T7 promoter. Heptapeptide seq Tyr-Ser-Pro-Thr-Ser-Pro-Ser.

Specifications

Our Abpromise guarantee covers the use of ab81834 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    pH: 7.9
    Constituents: 0.75% Potassium chloride, 0.0154% DTT, 0.316% Tris HCl, 0.00584% EDTA, 20% Glycerol (glycerin, glycerine)

General Info

  • Alternative names

    • DNA directed RNA polymerase II A
    • DNA-directed RNA polymerase II largest subunit RNA polymerase II 220 kd subunit
    • DNA-directed RNA polymerase II subunit A
    • DNA-directed RNA polymerase II subunit RPB1
    • DNA-directed RNA polymerase III largest subunit
    • hRPB220
    • hsRPB1
    • POLR2
    • Polr2a
    • POLRA
    • Polymerase (RNA) II (DNA directed) polypeptide A
    • Polymerase (RNA) II (DNA directed) polypeptide A 220kDa
    • RNA polymerase II subunit B1
    • RNA-directed RNA polymerase II subunit RPB1
    • RPB1
    • RPB1_HUMAN
    • RPBh1
    • RpIILS
    • RPO2
    • RPOL2
    see all
  • 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. Acts as an 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 similarities

    Belongs to the RNA polymerase beta' chain family.
  • Domain

    The C-terminal domain (CTD) serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing.
  • Post-translational
    modifications

    The tandem heptapeptide 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 heptapeptide 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.
    Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. EP300 is one of the enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-consensus heptapeptide repeats is associated with 'Ser-2' phosphorylation and active transcription. It may regulate initiation or early elongation steps of transcription specially for inducible genes.
    Methylated at Arg-1810 prior to transcription initiation when the CTD is hypophosphorylated, phosphorylation at Ser-1805 and Ser-1808 preventing this methylation. Symmetrically or asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1 respectively. Symmetric or asymmetric dimethylation modulates interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3. SMN1/SMN2 interacts preferentially with the symmetrically dimethylated form while TDRD3 interacts with the asymmetric form. Through the recruitment of SMN1/SMN2, symmetric dimethylation is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination. CTD dimethylation may also facilitate the expression of select RNAs. Among tandem heptapeptide repeats of the C-terminal domain (CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-consensus heptapeptide repeats can be alternatively acetylated, methylated and dimethylated. Methylation occurs in the earliest transcription stages and precedes or is concomitant to 'Ser-5' and 'Ser-7' phosphorylation.
    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.
  • Cellular localization

    Nucleus.
  • 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

Protocols

To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.

Click here to view the general protocols

Datasheets and documents

  • Datasheet download

    Download

References (0)

Publishing research using ab81834? Please let us know so that we can cite the reference in this datasheet.

ab81834 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

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1-2 of 2 Abreviews or Q&A

ab81834 is phosphorylated at Ser7 position

Excellent
Abreviews
Abreviews
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Application
Functional Studies
We purchased "ab81834 - Recombinant Human RNA polymerase II CTD repeat YSPTSPS protein" for kinase assay but it seems that the CTD is already phosphorylated at Serine 7th position. The MW is mentioned 68 KDa in the data sheet but in my WB (with Rbp1 CTD Ab) you can see 2 bands - one at 68 and other above 75 KDa marker - showing massive phosphorylation (Ser7p only). If you are using this for kinase assay, i would recommend to check the phosphorylation status in your lot.

Ata Abbas

Verified customer

Submitted Mar 02 2018

Question

Hi, what is the full molecular weight of this protein? Also, is there a possibility of larger/custom sizes for this product? Thanks.

Read More

Abcam community

Verified customer

Asked on Oct 11 2011

Answer

Thank you for contacting Abcam. The molecular weight for this protein is 217kDa. I used the following sequence to determine the molecular weight: http://www.uniprot.org/uniprot/P24928 As for larger/custom sizes, that is something that we can accommodate and if it something you are interested in, I can forward your details to the appropriate person. If there is anything else I can help you with, please do not hesitate to contact me.

Read More

Abcam Scientific Support

Answered on Oct 11 2011

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