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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 phosphorylation at serine 1 (H4 pSer1) represents a rapid and early chromatin signaling event in response to DNA damage and cellular stress. Phospho-Histone H4 Antibody (pSer1) (clone RM194) detects this modification, which occurs at the extreme N-terminus of histone H4 and directly influences chromatin accessibility during genome surveillance and repair. Unlike acetylation or methylation marks that define relatively stable chromatin states, serine 1 phosphorylation functions as a dynamic signal that marks chromatin undergoing active DNA damage response. 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.
H4 pSer1 antibody, also referred to as phospho Histone H4 serine 1 antibody or HIST1H4 phosphorylation antibody in the literature, is widely used to study early chromatin responses to genotoxic stress. Phosphorylation at serine 1 is mediated by stress-responsive kinases, including pathways linked to ATM and ATR signaling, and is rapidly induced following DNA damage. This modification serves as a molecular switch that promotes chromatin relaxation at sites requiring repair, distinguishing it from structural chromatin marks associated with compaction or long-term regulation.
Mechanistically, phosphorylation at serine 1 introduces a negative charge at the histone H4 N-terminal tail, altering its interaction with negatively charged DNA and adjacent nucleosomes. This reduces histone-DNA affinity and disrupts inter-nucleosomal contacts, leading to localized chromatin decondensation. These structural changes are essential for enabling DNA repair machinery to access damaged DNA regions efficiently. As a result, H4 pSer1 is closely associated with chromatin remodeling events that occur immediately following DNA damage rather than steady-state chromatin organization.
The histone H4 tail plays a central role in nucleosome stability and chromatin fiber interactions, and modification at serine 1 uniquely affects these interactions at the earliest stages of chromatin response. This positions H4 serine 1 phosphorylation as a marker of acute chromatin signaling, particularly in contrast to lysine-based modifications that regulate transcription, chromatin assembly, or higher-order structure over longer timescales.
H4 pSer1 is also linked to coordination of downstream chromatin modifications, acting in concert with other histone marks to regulate recruitment of DNA repair complexes. This crosstalk between phosphorylation and other histone modifications contributes to precise control of chromatin accessibility during genome maintenance. Dysregulation of these signaling pathways has been associated with impaired DNA repair capacity and increased genomic instability in disease states, including cancer.
A recombinant rabbit monoclonal antibody such as clone RM194 enables specific detection of histone H4 serine 1 phosphorylation in studies focused on DNA damage signaling, chromatin remodeling under stress conditions, and early-stage chromatin response mechanisms.
The stated application concentrations are suggested starting points. Titration of the Phospho-Histone H4 Antibody (pSer1) / Histone H4 Serine 1 Phosphorylation DNA Damage Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
A phospho-peptide corresponding to phospho-Histone H4 (pSer1) was used as the immunogen for this Phospho-Histone H4 Antibody (pSer1) / Histone H4 Serine 1 Phosphorylation DNA Damage Antibody.
Store the recombinant phospho-Histone H4 antibody at -20oC (with glycerol) or aliquot and store at -20oC (without glycerol).
H4 pSer1 antibody, Phospho Histone H4 Ser1 antibody, HIST1H4 phosphorylation antibody, H4 DNA damage phosphorylation antibody
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