Product Pathways - Chromatin Regulation
SUV39H1 Histone Methyltransferase Antibody #2991
| Applications | Reactivity | MW (kDa) | Source |
|---|---|---|---|
| W | H | 48 | Rabbit |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
SUV39H1 Histone Methyltransferase Antibody detects endogenous levels of total SUV39H1 histone methyltransferase. The antibody does not cross-react with other related proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to the amino-terminal sequence of human SUV39H1. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Human histone methyltransferase SUV39H1 is the homologue of the dominant Drosophila PEV modifier Su(var)3-9 and is composed of 412 amino acid residues (1). It combines two of the most evolutionarily conserved domains of the "chromatin regulators": the chromo and SET domains (2,3). The 60 amino acid chromo domain represents an ancient histone-like fold that directs heterochromatic localizations. It has been demonstrated that the 130 amino acid SET domain contains the methyltransferase catalytic motif, which cooperates with the adjacent cystein-rich regions to confer histone metheytransfersase activity (1). This enzyme selectively methylates histone H3 on lysine 9, which generates a binding site for HP1 proteins, a family of heterochromatic adaptor molecules involved in both gene silencing and supra-nucleosomal chromatin structure (4,5). SUV39H1 histone methyltransferase plays in important role in modification of histone amino termini and regulation of gene expression.
- Rea, S. et al. (2000) Nature 406, 593-599.
- Koonin, E. V. et al. (1995) Nucleic Acids Res. 23, 4229-4232.
- Jenuwein, T. et al. (1998) Cell. Mol. Life Sci. 54, 80-93.
- Lachner, M. et al. (2001) Nature 410, 116-120.
- Bannister, A. J. et al. (2001) Nature 410, 120-123.
Application References
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