Anti-dimethyl-Histone H4 (Arg3) Symmetric Antibody

Control
HeLa acid extract

Evaluated by Western Blot in HeLa acid extract.

Western Blot Analysis: 0.1 µg/mL of this antibody detected Histone H4 on 10 µg of HeLa acid extract.

Immunocytochemistry Analysis: 1:500 dilution from a representative lot detected Histone H4 in HeLa and A431 cells.

Peptide Dot Blot Analysis: 0.5 µg/mL of this antibody detected Histone H4 dimethyl Arg3 (symmetric) peptides, but did not detect Histone H4 dimethyl Arg3 (assymmetric) peptide, other modified peptides, or non-methyated histone H4 peptides.

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Histones

Use Anti-dimethyl-Histone H4 (Arg3) Symmetric Antibody (rabbit polyclonal antibody) validated in WB, ICC, DB to detect dimethyl-Histone H4 (Arg3) Symmetric also known as histone H4, histone cluster 4 H4.

Broad species cross-reactivity expected based on sequence similarity.

This antibody recognizes Histone H4 symmetrically dimethylated at Arg3.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Histones are highly conserved proteins that serve as the structural scaffold for the organization of nuclear DNA into chromatin. The four core histones, H2A, H2B, H3, and H4, assemble into an octamer (2 molecules of each). Histones are modified post-translationally by the actions of enzymes in both the nucleus and cytoplasm. These modifications, which include acetylation, phosphorylation, methylation, and ubiquitin-ation, occur predominantly on the N-terminal and C-terminal tails that extend beyond the nucleosome core particle. Arginine modifications of histones proteins are mediated by two classes of protein arginine methyltransferases (PRMTs), class I and II. Class I PRMTs place two methyl groups on the one nitrogen atom of the arginine guanidino group, resulting in an asymmetric modification. In contrast class II PRMTs place two methyl groups on two nitrogen atoms of the guanidino group producing a symmetric dimethylation. Although there are exceptions, asymmetric modifications are typically associated with transcription activation while symmetric modifications are most commonly associated with transcriptional repression.

~13 kDa observed. Crossreacting band at ~58 kDa has been observed in some lysates.

Epitope: Symmetrically dimethylated Arg3

KLH-conjugated linear peptide corresponding to human Histone H4 when symmetrically dimethylated at Arg3.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Affinity purified

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.