Render Target: SSR
Render Timestamp: 2024-10-24T19:55:06.605Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-09-30 01:58:57.061
Product last modified at: 2024-09-30T08:01:19.659Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

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

Filter:
  • WB
  • IP

    Supporting Data

    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 mAb 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).
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