|Application ||WB, E|
|Other Accession||Q9JHD2, Q8N1A2|
|Calculated MW||93926 Da|
|Antigen Region||65-94 aa|
|Other Names||Histone acetyltransferase KAT2A, General control of amino acid synthesis protein 5-like 2, Histone acetyltransferase GCN5, HsGCN5, Lysine acetyltransferase 2A, STAF97, KAT2A, GCN5, GCN5L2, HGCN5|
|Target/Specificity||This GCN5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 65-94 amino acids from the N-terminal region of human GCN5.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GCN5 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||GCN5, GCN5L2, HGCN5|
|Function||Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. Also acetylates non- histone proteins, such as CEBPB (PubMed:17301242). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.|
|Tissue Location||Expressed in all tissues tested, with most abundant expression in ovary|
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Provided below are standard protocols that you may find useful for product applications.
GCN5 functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. This protein has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles.
Sabo,A., Mol. Cell. Biol. 28 (7), 2201-2212 (2008)
Wiper-Bergeron,N., Proc. Natl. Acad. Sci. U.S.A. 104 (8), 2703-2708 (2007)
Oishi,H., J. Biol. Chem. 281 (1), 20-26 (2006)
Kikuchi,H., Gene 347 (1), 83-97 (2005)
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