Cell Signaling Technology

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines, using SUV39H1 Histone Methyltransferase Antibody.

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.

  1. Rea, S. et al. (2000) Nature 406, 593-599.
  2. Koonin, E. V. et al. (1995) Nucleic Acids Res. 23, 4229-4232.
  3. Jenuwein, T. et al. (1998) Cell. Mol. Life Sci. 54, 80-93.
  4. Lachner, M. et al. (2001) Nature 410, 116-120.
  5. Bannister, A. J. et al. (2001) Nature 410, 120-123.

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