Anti-SUV39H1 Histone Methyltransferase antibody

Monoclonal Anti-SUV39H1 Histone Methyltransferase (mouse IgG1 isotype) is derived from the 44.1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with the recombinant fusion protein MBP-SUV39H1.

recombinant fusion protein MBP-SUV39H1

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Monoclonal Anti-SUV39H1 Histone Methyltransferase antibody is suitable for use in ELISA, immunoblotting (~47 kDa), immunoprecipitation, and immunoncytochemistry applications.
For immunoblotting, a working concentration of 2-4 mg/mL is recommended using an extract of HeLa nuclear cells.

Combined disruption of both mouse SUV39H1 and 2 causes chromosomal instability and increased risk of tumorigenesis, as well as complete spermatogenic failure that is caused by non-homologous chromosome associations.

Monoclonal Anti-SUV39H1 Histone Methyltransferase recognizes an epitope in the N-terminal (195 amino acids) of human and mouse SUV39H1 Histone Methyltransferase.

Post -translational modification of histones, such as phosphorylation, acetylation, and methylation, are crucial for chromatin remodeling. SUV39H1 and Suv39h1 are the human and mouse homologs of Drosophila Su(var)3-9 protein, respectively. These proteins selectively methylate histone H3 at lysine 9 creating a high-affinity binding site for the HP1 proteins (heterochromatin protein 1). HP1 proteins are known to interact with transcription suppressor proteins, suggesting that the interactions with SUV39H1 and methylated histone H3 mediate a silence effect on the transcription of target genes. Over-expression of SUV39H1 in HeLa cells causes a redistribution of endogenous HP1 proteins and growth retardation, suggesting that SUV39H1-mediated modulation of heterochromatin can impair cell cycle progression.
The overall identity between the human and mouse SUV39H1 amino acid sequences is 95%, both lacking an N-terminal 155 amino acid stretch from Drosophila Su(var)3-9. As a consequence, cross-species amino acid identity reaches 42% between the fly and the two mammalian proteins. The SUV39H1 protein consists of three regions: a SET domain, a 110 amino acid domain containing several cysteine conserved residues, and a chromo domain.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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