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Symmetric Di-Methyl Histone H4 (Arg3) (E5Z6W) Rabbit Monoclonal Antibody #92326

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  • WB
  • IP

    Product Specifications

    REACTIVITY H M R Mk
    SENSITIVITY Endogenous
    MW (kDa) 11
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Symmetric Di-Methyl Histone H4 (Arg3) (E5Z6W) Rabbit Monoclonal Antibody recognizes endogenous levels of total H4 protein only when symmetrically di-methylated at Arg3. This antibody does not cross-react with histone H4 when mono-methylated or asymmetrically di-methylated at Arg3. This antibody does not cross-react with any other known methylated arginine residues on histone H4. This antibody may detect a band of unknown origin at 100 kDa.

    Species Reactivity:

    Human, Mouse, Rat, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human histone H4 protein in which Arg3 is symmetrically di-methylated.

    Background

    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 methyltransferases (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 peptidyl 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).

    Alternate Names

    H4; H4 clustered histone 1; H4 histone family, member A; H4-16; H4/A; H4/B; H4/C; H4/D; H4/E; H4/G; H4/H; H4/I; H4/J; H4/K; H4/M; H4/N; H4/O; H4C1; H4C11; H4C12; H4C13; H4C14; H4C15; H4C2; H4C3; H4C4; H4C5; H4C6; H4C8; H4C9; H4F2; H4FA; H4FB; H4FC; H4FD; H4FE; H4FG; H4FH; H4FI; H4FJ; H4FK; H4FM; H4FN; H4FO; HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4L; HIST2H4; HIST2H4A; HIST2H4B; HIST4H4; histone 1, H4a; histone cluster 1 H4 family member a; histone cluster 1, H4a; Histone H4

    For Research Use Only. Not for Use in Diagnostic Procedures.
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