ANKRD11 is a member of a family of ankyrin repeat-containing cofactors that interacts with p160 nuclear receptor coactivators and inhibits ligand-dependent transcriptional activation by recruiting histone deacetylases to the complex. Recently, ANKRD11 was shown to bind to the tumor suppressor gene p53 and enhance its activity.
Immunogen
Synthetic peptide directed towards the N terminal region of human ANKRD11
Biochem/physiol Actions
ANKRD11 is a member of a novel family of ankyrin repeats containing cofactors (ANCOs) that interact with p160 coactivators to inhibit ligand-dependent transactivation. ANKRD11 encodes a large nuclear protein with five ankyrin repeats, and parts of its sequences have been reported as nasopharyngeal carcinoma susceptibility protein and medulloblastoma antigen. This gene also colocalizes and interacts with histone deacetylases.
Sequence
Synthetic peptide located within the following region: KRKLPFTAGANGEQKDSDTEKQGPERKRIKKEPVTRKAGLLFGMGLSGIR
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The Journal of biological chemistry, 279(32), 33799-33805 (2004-06-09)
Members of the p160 nuclear receptor coactivators interact with liganded nuclear receptors to enhance transcription of target genes. Here we identify a novel family of ankyrin repeats containing cofactors (ANCOs) that interact with the p160 coactivators. ANCO-1 binds to the
Journal of cell science, 121(Pt 21), 3541-3552 (2008-10-09)
The ability of p53 to act as a transcription factor is critical for its function as a tumor suppressor. Ankyrin repeat domain 11, ANKRD11 (also known as ANR11 or ANCO1), was found to be a novel p53-interacting protein that enhanced
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