Phospho-HIST1H1C (T164) Antibody
Description
Definition and Target Specificity
Phospho-HIST1H1C (T164) Antibody detects the phosphorylation of HIST1H1C (Histone H1.2) at threonine residue 164. This modification occurs in the C-terminal tail of the linker histone H1, which plays a role in chromatin compaction and transcriptional regulation . The antibody is generated using a synthetic peptide corresponding to the phosphorylated T164 epitope of human HIST1H1C (UniProt ID: P16403) .
Mitotic Chromatin Dynamics
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Phosphorylation of HIST1H1C at T164 is associated with mitotic progression. Studies show that H1.2 phosphorylation at T165 (a homologous site in other variants) peaks during metaphase and decreases during anaphase/telophase .
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This modification correlates with chromatin condensation and exclusion from metaphase chromosomes, suggesting a role in mitotic chromatin reorganization .
Subcellular Localization
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Immunofluorescence studies reveal that phosphorylated H1 variants, including HIST1H1C (T164), localize to the perichromosomal layer during mitosis, distinct from unmodified H1 .
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In interphase cells, HIST1H1C (T164) phosphorylation is detectable at low levels, primarily in condensed chromatin regions .
Functional Implications
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HIST1H1C phosphorylation modulates chromatin accessibility, influencing transcriptional activity and DNA repair .
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Aberrant phosphorylation patterns are linked to diseases such as cancer, where histone H1 dysregulation affects tumor progression .
Validation and Challenges
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Specificity: Antibodies targeting phosphorylated H1 require rigorous validation due to sequence homology among H1 variants and overlapping post-translational modifications (PTMs) .
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Mitotic Detection: Phospho-HIST1H1C (T164) Antibody may fail to recognize hyperphosphorylated H1 during certain mitotic stages due to epitope masking .
Comparison with Related Antibodies
The table below contrasts Phospho-HIST1H1C (T164) Antibody with other H1 phosphorylation-targeting tools :
Technical Considerations
Product Specs
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
- Research indicates that a network of E2F target genes is susceptible to the regulatory influence of H1.2. H1.2 enhances the global association of pRb with chromatin, promotes transcriptional repression by pRb, and facilitates pRb-dependent cell-cycle arrest. PMID: 28614707
- BRG1 participates in gene repression by interacting with H1.2, facilitating its deposition and stabilizing nucleosome positioning around the transcription start site. PMID: 27390128
- Studies have shown that histones H1.2 and H1.4 are present in MDA-MB-231 metastatic breast cancer cells. Phosphorylation at S173 of histone H1.2 and S172, S187, T18, T146, and T154 of H1.4 significantly increases during the M phase, suggesting these events are cell cycle-dependent. The study also reports the observation of the H1.2 SNP variant A18V in MCF-10A cells. PMID: 26209608
- Integration with apoptotic intermediates (via C-terminal tail interactions) may represent a generalized function of linker histone isoforms in apoptotic cascades. PMID: 24525734
- Histone H1.2-T165 post-translational modifications are dispensable for chromatin binding and cell proliferation, while H1.4-K26 modifications are essential for proper cell cycle progression. PMID: 24873882
- H1.2 interacts with Cul4A and PAF1 to activate developmental regulatory genes. PMID: 24360965
- H1.2 is less abundant than other histone H1 variants at the transcription start sites of inactive genes, and promoters enriched in H1.2 differ from those enriched in other histone H1 variants and tend to be repressed. PMID: 24476918
- Mutations in linker histone genes HIST1H1 B, C, D, and E; OCT2 (POU2F2); IRF8; and ARID1A have been implicated in the pathogenesis of follicular lymphoma. PMID: 24435047
- Data suggest that the p53 acetylation-H1.2 phosphorylation cascade serves as a unique mechanism for triggering p53-dependent DNA damage response pathways. PMID: 22249259
- Research has confirmed N-terminal acetylation on all isoforms, plus a single internal acetylation site. Phosphorylation sites were located on peptides containing the cyclin dependent kinase (CDK) consensus motif. PMID: 15595731
- The binding of histone H1 to a general amyloid-like motif suggests that histone H1 may play a significant role in diseases associated with amyloid-like fibrils. PMID: 16854430
- Histone H1.2 was translocated from the nucleus to the mitochondria after treatment with bleomycin and co-localized with Bak in mitochondria. PMID: 17879944
- Research suggests that the recruitment of YB1, PURalpha, and H1.2 to the p53 target gene Bax is required for repression of p53-induced transcription. PMID: 18258596
