anti-EP400 antibody from antibodies-online

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anti-EP400 antibody

Description

Product Characteristics:
NuAR is a multi-protein histone acetyltransferase complex that functions to acetylate the nucleosomal Histones H4 and H2A, thereby activating transcription of select target genes. p400, also known as EP400 (E1A binding protein p400) or mDomino, localizes to the nucleus and is a component of the NuAR complex. Expressed in brain, liver, thymus, lung, spleen, colon and kidney, p400 regulates the transcriptional activity of proteins such as MZF-1 and contributes to the ATPase and helicase activities of NuA4. p400 is a SWI2/ SNF2-related protein that can interact with the adenovirus oncoprotein E1A, thus activating the proapoptotic activity of E1A. The ability of p400 to regulate transcriptional and apoptotic activity suggests that the NuAR complex may be a crucial component of cell proliferation, transformation and, possibly, carcinogenesis. Five isoforms of p400 exist due to alternative splicing events.

Subcellular location: Nucleus

Synonyms: CAG repeat protein 32, CAGH32, DKFZP434I225, Domino homolog, E1A binding protein p400, EP 400, EP400, FLJ42018, FLJ45115, hDomino, KIAA1498, KIAA1818, p400 kDa SWI2/SNF2 related protein, P400 SWI2/SNF2-related protein, TNRC12, Trinucleotide repeat containing 12, Trinucleotide repeat containing gene 12 protein, EP400_HUMAN.

Target Information: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400 (By similarity). Regulates transcriptional activity of ZNF42