|Other Names||Histone-lysine N-methyltransferase SETDB1, ERG-associated protein with SET domain, ESET, Histone H3-K9 methyltransferase 4, H3-K9-HMTase 4, Lysine N-methyltransferase 1E, SET domain bifurcated 1, SETDB1, KIAA0067, KMT1E|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1073a was selected from the N-term region of human SETDB1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.|
|Cellular Location||Nucleus. Chromosome. Note=Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin|
|Tissue Location||Widely expressed. High expression in testis.|
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The SET domain is a highly conserved, approximately 150-amino acid motif implicated in the modulation of chromatin structure. It was originally identified as part of a larger conserved region present in the Drosophila Trithorax protein and was subsequently identified in the Drosophila Su(var)3-9 and 'Enhancer of zeste' proteins, from which the acronym SET is derived. Studies have suggested that the SET domain may be a signature of proteins that modulate transcriptionally active or repressed chromatin states through chromatin remodeling activities.
Ichimura, T., et al., J. Biol. Chem. 280(14):13928-13935 (2005).Sarraf, S.A., et al., Mol. Cell 15(4):595-605 (2004).Wang, H., et al., Mol. Cell 12(2):475-487 (2003).Schultz, D.C., et al., Genes Dev. 16(8):919-932 (2002).Yang, L., et al., Biochem. J. 369 (PT 3), 651-657 (2003) (): ().
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