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  1. Link

    human-sfpq-blocking-peptide-ab39323.pdf

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Epigenetics and Nuclear Signaling DNA / RNA RNA Processing Splicing
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Human SFPQ Blocking peptide  (ab39323)

  • Datasheet
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Key features and details

  • Suitable for: Blocking

Description

  • Product name

    Human SFPQ Blocking peptide 
  • Animal free

    No
  • Nature

    Synthetic
    • Species

      Human
  • Description

    Human SFPQ peptide

Associated products

  • Corresponding Antibody

    • Anti-SFPQ antibody (ab38148)

Specifications

Our Abpromise guarantee covers the use of ab39323 in the following tested applications.

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

  • Applications

    Blocking - Blocking peptide for Anti-SFPQ antibody (ab38148)

  • Form

    Lyophilized
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at -20°C.

    Information available upon request.

  • Reconstitution
    Reconstitute in either water or buffer. If the peptide doesn’t dissolve try an organic solvent like DMSO, then dilute using water or buffer. Gentle warming and sonication can effectively aid peptide solubilisation.

General Info

  • Alternative names

    • 100 kDa DNA pairing protein
    • 100 kDa DNA-pairing protein
    • 100 kDa subunit
    • DNA binding p52/p100 complex 100 kDa subunit
    • DNA-binding p52/p100 complex
    • hPOMp100
    • Polypyrimidine tract binding protein associated splicing factor
    • Polypyrimidine tract-binding protein-associated-splicing factor
    • POMP100
    • PPP1R140
    • proline- and glutamine-rich
    • Protein phosphatase 1 regulatory subunit 140
    • PSF
    • PTB associated splicing factor
    • PTB-associated-splicing factor
    • Sfpq
    • SFPQ_HUMAN
    • Splicing factor
    • Splicing factor proline and glutamine rich
    • Splicing factor proline/glutamine rich
    • Splicing factor proline/glutamine rich (polypyrimidine tract binding protein associated)
    see all
  • Function

    DNA- and RNA binding protein, involved in several nuclear processes. Essential pre-mRNA splicing factor required early in spliceosome formation and for splicing catalytic step II, probably as an heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and specifically binds to intronic polypyrimidine tracts. Interacts with U5 snRNA, probably by binding to a purine-rich sequence located on the 3' side of U5 snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and polyadenylation process as component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play a role in nuclear retention of defective RNAs. SFPQ may be involved in homologous DNA pairing; in vitro, promotes the invasion of ssDNA between a duplex DNA and produces a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA unwinding by modulating the function of topoisomerase I/TOP1; in vitro, stimulates dissociation of TOP1 from DNA after cleavage and enhances its jumping between separate DNA helices. The SFPQ-NONO heteromer may be involved in DNA nonhomologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination and may stabilize paired DNA ends; in vitro, the complex strongly stimulates DNA end joining, binds directly to the DNA substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional preligation complex. SFPQ is involved in transcriptional regulation. Transcriptional repression is probably mediated by an interaction of SFPQ with SIN3A and subsequent recruitment of histone deacetylases (HDACs). The SFPQ-NONO/SF-1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity. SFPQ isoform Long binds to the DNA binding domains (DBD) of nuclear hormone receptors, like RXRA and probably THRA, and acts as transcriptional corepressor in absence of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the insulin-like growth factor response element (IGFRE) and inhibits IGF-I-stimulated transcriptional activity.
  • Involvement in disease

    Note=A chromosomal aberration involving SFPQ may be a cause of papillary renal cell carcinoma (PRCC). Translocation t(X;1)(p11.2;p34) with TFE3.
  • Sequence similarities

    Contains 2 RRM (RNA recognition motif) domains.
  • Post-translational
    modifications

    The N-terminus is blocked.
    Phosphorylated on multiple serine and threonine residues during apoptosis. In vitro phosphorylated by PKC. Phosphorylation stimulates binding to DNA and D-loop formation, but inhibits binding to RNA.
    Arg-7, Arg-9, Arg-19 and Arg-25 are dimethylated, probably to asymmetric dimethylarginine.
  • Cellular localization

    Nucleus matrix. Predominantly in nuclear matrix.
  • Target information above from: UniProt accession P23246 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
  • References (0)

    Publishing research using ab39323? Please let us know so that we can cite the reference in this datasheet.

    ab39323 has not yet been referenced specifically in any publications.

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