MonoMethyl-Histone H3-R2 Rabbit Monoclonal Antibody (Q16695/P68431) – Validated for WB, DB, ELISA, CUT&Tag

Core Product Specifications and Parameters

Biological Background: Histone H3.1/H3.1t Function and Localization

Histone H3.1 (and the testis-specific H3.1t) are core components of the nucleosome, the fundamental repeating unit of chromatin. As histones, they wrap and compact DNA, thereby limiting its accessibility to the cellular machinery. Histones play a central role in transcription regulation, DNA repair, DNA replication, and chromosomal stability.

The dynamic regulation of DNA accessibility is achieved through a complex set of post-translational modifications (PTMs) on histone tails, collectively known as the histone code. These modifications include acetylation, methylation, phosphorylation, and many others, and are recognized by specific reader proteins that translate them into biological outcomes.

Histone H3.1 is localized exclusively to the nucleus and associated with chromosomes. Its expression is replication-dependent and highly enriched in somatic cells, while the H3.1t variant (Q16695) is expressed specifically in testicular cells.

Methylation of arginine 2 (R2) of histone H3 is a key modification catalyzed by protein arginine methyltransferases (PRMTs) such as PRMT6. This modification can exist in mono- or dimethylated states and is involved in regulating chromatin structure and gene expression. The monomethylated form (H3R2me1) is a critical intermediate that can influence the binding of effector proteins and is often enriched at active gene promoters.

Related references: PMID:17898714 (PRMT6-mediated methylation of H3R2) PMID:18077460 (H3R2 methylation and transcriptional regulation)

Experimental Guidance and Technical Tips

• The immunogen was a synthetic monomethylated peptide around R2 of human Histone H3. For Western blot and dot blot applications, consider including a non-methylated peptide competition control to confirm methylation-specific binding.
• For CUT&Tag assays, the antibody's specificity for monomethyl-R2 may allow precise mapping of H3R2me1 enrichment. Always validate in the relevant sample system with appropriate positive and negative controls.
• Dilution and incubation conditions should be optimized empirically. The antibody may cross-react with similar methylation states on other histone H3 variants; verify with known protein extracts if necessary.

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