Human KAT13A / SRC1 peptide (ab5848)
Key features and details
- Purity: > 95% SDS-PAGE
- Suitable for: Blocking
Description
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Product name
Human KAT13A / SRC1 peptide
See all KAT13A / SRC1 proteins and peptides -
Purity
> 95 % SDS-PAGE. -
Accession
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Animal free
No -
Nature
Synthetic -
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Species
Human -
Sequence
SSDPANPDSHKRKGSPC -
Amino acids
8 to 24
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Associated products
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Positive Controls
Specifications
Our Abpromise guarantee covers the use of ab5848 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Blocking
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Form
Lyophilized -
Additional notes
This peptide may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and SRC1, catalog ab2859. Using a solution of peptide of equal volume and concentration to the corresponding antibody will yield a large molar excess of peptide (~70-fold) for competitive inhibition of antibody-protein binding reactions.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
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ReconstitutionReconstitute with 0.1 ml of distilled water.
General Info
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Alternative names
- bHLHe74
- Class E basic helix-loop-helix protein 74
- F SRC 1
see all -
Function
Nuclear 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 specificity
Widely expressed. -
Involvement in disease
Note=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 similarities
Belongs to the SRC/p160 nuclear receptor coactivator family.
Contains 1 basic helix-loop-helix (bHLH) domain.
Contains 1 PAS (PER-ARNT-SIM) domain. -
Domain
The 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
modificationsSumoylated; 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 localization
Nucleus. - 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.
Datasheets and documents
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Datasheet download
References (0)
ab5848 has not yet been referenced specifically in any publications.