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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 lysine 16 acetylation (H4K16ac) is a key regulator of higher-order chromatin structure and nucleosome interaction dynamics. H4K16ac Antibody (clone RM204) detects this modification, which directly controls chromatin fiber folding and the transition between compact and relaxed chromatin states. Among histone H4 modifications, lysine 16 acetylation is one of the most influential determinants of global chromatin architecture. 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.
H4K16ac antibody, also referred to as Histone H4 K16 acetyl antibody or HIST1H4 acetylation antibody in the literature, is widely used to study chromatin structure and epigenetic regulation. Acetylation at lysine 16 is catalyzed by the histone acetyltransferase MOF (KAT8), which plays a central role in regulating chromatin organization and genome accessibility. This modification has been extensively linked to the control of chromatin compaction at a structural level.
Mechanistically, acetylation at lysine 16 disrupts interactions between the histone H4 tail and adjacent nucleosomes, preventing tight chromatin packing. This interference with nucleosome-nucleosome contacts leads to reduced chromatin fiber condensation and promotes a more open chromatin configuration. Unlike other acetylation sites that primarily influence local chromatin accessibility, H4K16ac has a direct impact on higher-order chromatin folding across extended genomic regions.
The histone H4 tail is essential for mediating chromatin fiber interactions, and modification at lysine 16 specifically alters these interactions to control global chromatin structure. This makes H4K16ac a key marker for studying large-scale chromatin organization, chromatin decondensation, and structural epigenetic regulation.
In addition to its structural role, H4K16 acetylation is involved in DNA repair processes, where localized chromatin relaxation is required to allow access to damaged DNA. Altered levels of H4K16ac have been associated with genome instability and disease, particularly in cancer, where disruption of chromatin architecture contributes to abnormal gene regulation.
A recombinant rabbit monoclonal antibody such as clone RM204 enables specific detection of this modification in studies focused on higher-order chromatin structure, chromatin relaxation, and epigenetic control of genome organization.
The stated application concentrations are suggested starting points. Titration of the H4K16ac Antibody / Histone H4 Lysine 16 Acetylation Chromatin Structure Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
An acetyl-peptide corresponding to Acetyl-Histone H4 (Lys16) was used as the immunogen for this H4K16ac Antibody / Histone H4 Lysine 16 Acetylation Chromatin Structure Antibody.
Store the recombinant H4K16ac antibody at -20oC (with glycerol) or aliquot and store at -20oC (without glycerol).
H4K16ac antibody, Histone H4 acetyl lysine 16 antibody, HIST1H4 acetylation antibody, H4 chromatin structure antibody
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