Recombinant Human KAT13A / SRC1 protein (ab81945)



  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionQ15788
    • SpeciesHuman
    • Amino acids627 to 786


Our Abpromise guarantee covers the use of ab81945 in the following tested applications.

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

  • Biological activity1 unit equals 1 nanogram of purified protein.
  • Applications


  • Purity> 95 % SDS-PAGE.
    ab81945 is purified by an affinity column.
  • FormLiquid
  • Additional notes1 unit equals 1 nanogram of purified protein.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    Preservative: None
    Constituents: 20% Glycerol, 20mM Tris HCl, 100mM Potassium chloride, 1mM DTT, 0.2mM EDTA, pH 8.0

General Info

  • Alternative names
    • bHLHe74
    • Class E basic helix-loop-helix protein 74
    • F SRC 1
    • Hin 2 protein
    • Hin2 protein
    • MGC129719
    • MGC129720
    • mNRC 1
    • NCoA 1
    • NCoA-1
    • Ncoa1
    • Nuclear receptor coactivator 1
    • Nuclear receptor coactivator protein 1
    • NY REN 52 antigen
    • Protein Hin 2
    • Protein Hin-2
    • Protein Hin2
    • Renal carcinoma antigen NY REN 52
    • Renal carcinoma antigen NY-REN-52
    • RIP 160
    • RIP160
    • SRC 1
    • SRC-1
    • Steroid receptor coactivator 1
    see all
  • FunctionNuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3.
  • Tissue specificityWidely expressed.
  • Involvement in diseaseNote=A chromosomal aberration involving NCOA1 is a cause of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with PAX3 generates the NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and the C-terminus part of NCOA1. The fusion protein acts as a transcriptional activator. Rhabdomyosarcoma is the most common soft tissue carcinoma in childhood, representing 5-8% of all malignancies in children.
  • Sequence similaritiesBelongs to the SRC/p160 nuclear receptor coactivator family.
    Contains 1 basic helix-loop-helix (bHLH) domain.
    Contains 1 PAS (PER-ARNT-SIM) domain.
  • DomainThe C-terminal (1107-1441) part mediates the histone acetyltransferase (HAT) activity.
    Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3, 4 and 5 are essential for the association with nuclear receptors. LXXLL motif 7, which is not present in isoform 2, increases the affinity for steroid receptors in vitro.
  • Post-translational
    Sumoylated; sumoylation increases its interaction with PGR and prolongs its retention in the nucleus. It does not prevent its ubiquitination and does not exert a clear effect on the stability of the protein.
    Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites.
    Phosphorylated upon DNA damage, probably by ATM or ATR.
  • Cellular localizationNucleus.
  • Information by UniProt

References for Recombinant Human KAT13A / SRC1 protein (ab81945)

ab81945 has not yet been referenced specifically in any publications.

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