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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Histone H4 (HIST1H4) is a core nucleosomal histone whose N-terminal tail is a major substrate for arginine methylation events that regulate chromatin compaction and genome stability. H4R3me1 Antibody (clone RM195) detects monomethylation at arginine 3, a modification positioned within PRMT5-driven methylation pathways that shape chromatin architecture and repressive chromatin states. This residue is a key regulatory site controlling how histone H4 participates in nucleosome-nucleosome interactions and chromatin fiber organization. This antibody is part of our broader Histone H4 antibody collection, including acetylation, methylation, phosphorylation, and total H4 detection reagents for chromatin and epigenetics research.
Arginine 3 methylation represents a critical entry point into PRMT5-mediated chromatin regulation. While PRMT5 catalyzes symmetric dimethylation at this site, the monomethyl state reflects dynamic pathway activity and substrate engagement, making H4R3me1 a sensitive indicator of arginine methylation flux within chromatin. This positions H4R3me1 as a valuable marker for studying PRMT5 biology and chromatin compaction mechanisms rather than transcriptional activation processes.
HIST1H4 antibody, also referred to as Histone H4 antibody and H4R3 methylation antibody in the literature, is frequently used to investigate chromatin states associated with structural repression and genome organization. Methylation at arginine 3 promotes stabilization of nucleosomal arrays and contributes to reduced chromatin accessibility, supporting compact chromatin configurations that maintain genome integrity. This function distinguishes H4R3 methylation from many lysine-based histone modifications that are more closely linked to transcriptional regulation.
The histone H4 tail plays a direct structural role in mediating interactions between adjacent nucleosomes, and modification at arginine 3 alters the recruitment of chromatin-associated effector proteins. These changes reinforce chromatin condensation and support genome stability by limiting inappropriate DNA exposure. As a result, H4R3 methylation is closely associated with repressive chromatin environments and coordinated chromatin folding.
Dysregulation of PRMT5 activity and H4 arginine methylation has been implicated in cancer and other diseases characterized by altered chromatin compaction and epigenetic control. Monitoring H4R3me1 provides insight into PRMT5 pathway activity, chromatin structural states, and genome stability mechanisms.
A recombinant rabbit monoclonal antibody such as clone RM195 enables specific detection of this modification in studies focused on PRMT5 signaling, chromatin condensation, and higher-order chromatin organization.
The stated application concentrations are suggested starting points. Titration of the H4R3me1 Antibody / Histone H4 Arginine 3 Monomethylation PRMT5 Pathway Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
A monomethyl-peptide corresponding to Monomethyl-Histone H4 (Arg3) was used as the immunogen for this H4R3me1 Antibody / Histone H4 Arginine 3 Monomethylation PRMT5 Pathway Antibody
Store the recombinant H4R3me1 antibody at -20oC (with glycerol) or aliquot and store at -20oC (without glycerol).
H4R3me1 antibody, Histone H4 arginine methylation antibody, PRMT5 histone H4 antibody, HIST1H4 R3 methyl antibody
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