Product Pathways - Chromatin Regulation / Epigenetics
Symmetric Di-Methyl Histone H3 (Arg8) (E1W5H) Rabbit mAb #13939
|13939S||100 µl ( 10 western blots )||￥4,050.00||现货查询 购买询价 防伪查询|
|13939||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting,
Species predicted to react based on 100% sequence homology: Zebrafish, Bovine, S. cerevisiae,
Specificity / Sensitivity
Symmetric Di-Methyl Histone H3 (Arg8) (E1W5H) Rabbit mAb recognizes endogenous levels of histone H3 protein only when symmetrically di-methylated at Arg8. This antibody may have a slight cross reactivity towards histone H3 protein when mono-methylated at Arg8.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human histone H3 in which Arg8 is symmetrically di-methylated.
Western blot analysis of extracts from various cell lines using Symmetric Di-Methyl Histone H3 (Arg8) (E1W5H) Rabbit mAb.
The specificity of Symmetric Di-Methyl Histone H3 (Arg8) (E1W5H) Rabbit mAb was determined using peptide ELISA. The graph depicts the binding of the antibody to pre-coated, symmetric di-methyl histone H3 (Arg8) peptide in the presence of increasing concentrations of various competitor peptides. As shown, only the symmetric di-methyl histone H3 (Arg8) peptide competed away binding of the antibody.
The nucleosome is the primary chromatin building block and consists of DNA wrapped around an octamer made of paired histone proteins H2A, H2B, H3, and H4. Chromatin remodeling plays a critical role in the regulation of various nuclear activities, including transcription. Histone proteins are targets of post-translational modification, including acetylation, phosphorylation, ubiquitination, and methylation. Modified histone residues are recognized and bound by chromatin modifiers and the transcription machinery to regulate gene expression (1-4). Protein arginine methyl transferases (PRMTs) methylate histone proteins at arginine residues to generate mono-methylated, symmetrically di-methylated, or asymmetrically di-methylated proteins. Asymmetrically di-methylated arginine residues are found on histone H3 (Arg2, 8, 17, 26 and 42), histone H4 (Arg3), and histone H2A (Arg3) proteins. Asymmetric methylation is carried out by type 1 PRMTs, which include PRMT1, PRMT2, PRMT4/CARM1, and PRMT6. These modifications are often associated with actively transcribed genes. Symmetric di-methylation of arginine residues are found on histone H3 (Arg2 and 8), Histones H4 (Arg3), and H2A (Arg3). Symmetrically di-methylated histone arginine residues are generated by type II transferases PRMT5 and PRMT7, and are often associated with transcription repression (5-9). Arginine residues can also be deiminated by a protein arginine deiminase (PADI) to form the non-coded amino acid citrulline. Conversion of arginine to citrulline prevents methylation of this residue and is thought to regulate histone arginine methylation levels (10-13).
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