Anti-Histone H3 (di methyl Lys36) Rabbit Antibody [L23A20]

Catalog No.: F3399

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Biological Description

Specificity Anti-Histone H3 (di methyl Lys36) Rabbit Antibody [L23A20] detects endogenous levels of total Histone H3 protein, only when di-methylated on Lys36.
Background The nucleosome, composed of the four core histones H2A, H2B, H3, and H4, represents the fundamental unit of chromatin. Once regarded as a passive structural framework for DNA packaging, histones are now recognized as highly dynamic proteins that undergo diverse post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination. Among these, histone methylation plays a central role in defining transcriptionally active and inactive chromatin states and is essential for proper genome regulation during development. Arginine methylation of histones H3 (at residues Arg2, Arg17, and Arg26) and H4 (at Arg3) is generally associated with transcriptional activation and is catalyzed by protein arginine methyltransferases (PRMTs), notably co-activators such as PRMT1 and CARM1 (PRMT4). Lysine methylation predominantly occurs on histone H3 (at Lys4, Lys9, Lys27, Lys36, and Lys79) and histone H4 (at Lys20), and can mediate either gene activation or repression, depending on the site and context. These methyl marks serve as docking signals for chromatin-associated factors that contain specialized methyl-lysine binding motifs, including chromodomains (e.g., HP1, PRC1), PHD fingers (e.g., BPTF, ING2), tudor domains (e.g., 53BP1), and WD40 repeats (e.g., WDR5), thereby coordinating downstream chromatin remodeling and transcriptional regulation.

Usage Information

Application WB, IHC, IF, ChIP Dilution
WB IHC IF
1:5000 1:250 1:500
Reactivity Mouse, Rat, Human
Source Rabbit MW 15 kDa
Storage Buffer PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
Storage
(from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

References

  • https://pubmed.ncbi.nlm.nih.gov/15268870/
  • https://pubmed.ncbi.nlm.nih.gov/15479858/

Application Data