Mono-methyl-HIST1H1C (K118) Antibody
Description
Definition and Target Specificity
The Mono-methyl-HIST1H1C (K118) Antibody is a polyclonal rabbit-derived antibody designed to detect the mono-methylation of lysine residue 118 (K118) on the histone H1.2 protein (encoded by HIST1H1C). This antibody is highly specific to the methylated form of the protein, making it a valuable tool for studying epigenetic modifications and chromatin dynamics .
Research Applications and Validation
The antibody has been optimized for:
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ELISA: Detecting methylated HIST1H1C in lysates or purified histones .
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Immunofluorescence: Visualizing nuclear localization of methylated HIST1H1C in fixed cells .
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ChIP: Mapping genomic regions bound by methylated HIST1H1C .
Example Validation Data:
In HeLa cells, the antibody successfully demonstrated nuclear staining via IF and enriched chromatin binding at the beta-globin promoter in ChIP assays .
Role of HIST1H1C in Disease Pathogenesis
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Cancer: HIST1H1C is upregulated in hepatocellular carcinoma (HCC) and promotes tumor growth via STAT3 activation .
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Autophagy: Overexpression of HIST1H1C induces autophagy and inflammation in retinal cells, linking it to diabetic retinopathy .
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Epigenetic Regulation: Histone H1 variants like HIST1H1C modulate chromatin structure and gene expression, with methylation serving as a key regulatory mark .
Mechanistic Insights
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STAT3 Pathway: HIST1H1C interacts with STAT3 to form a feed-forward loop driving oncogenic signaling .
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Epigenetic Crosstalk: Methylation of HIST1H1C at K118 may influence chromatin compaction and transcriptional activity, though specific downstream targets remain under investigation .
Critical Considerations
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Specificity: Ensure cross-reactivity testing with non-methylated HIST1H1C or other histone variants .
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Optimization: Recommended dilutions vary by application (e.g., ELISA: 1:2000–1:10,000; IF: 1:50–1:200) .
Future Directions
Research using this antibody could elucidate the role of K118 methylation in:
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Cancer Progression: Investigating its prognostic value in HCC or other malignancies.
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Epigenetic Therapies: Exploring how targeting HIST1H1C methylation impacts chromatin remodeling drugs.
Product Specs
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Target Background
- Research indicates that Histone H1.2 regulates a network of E2F target genes. It enhances the association of the retinoblastoma protein (pRb) with chromatin, promoting transcriptional repression by pRb and contributing to cell cycle arrest. PMID: 28614707
- BRG1, a chromatin remodeling factor, participates in gene repression through its interaction with Histone H1.2. This interaction facilitates the deposition of Histone H1.2 and stabilizes nucleosome positioning around the transcription start site. PMID: 27390128
- Studies have shown that Histone H1.2 and Histone H1.4 are present in MDA-MB-231 metastatic breast cancer cells. The phosphorylation of specific residues on these histone variants, particularly S173 of Histone H1.2 and S172, S187, T18, T146, and T154 of Histone H1.4, significantly increases during the M phase of the cell cycle, suggesting cell cycle-dependent regulation. Additionally, a single nucleotide polymorphism (SNP) variant, A18V, of Histone H1.2 has been observed in MCF-10A cells. PMID: 26209608
- Interactions between Histone H1 isoforms and apoptotic intermediates, particularly through the C-terminal tail, may represent a broader function of these isoforms in apoptotic pathways. PMID: 24525734
- Post-translational modifications of Histone H1.2 at T165 are not essential for chromatin binding or cell proliferation, while modifications at K26 of Histone H1.4 are crucial for proper cell cycle progression. PMID: 24873882
- Histone H1.2 interacts with Cul4A and PAF1, two proteins involved in protein degradation and transcription regulation, respectively, to activate developmental regulatory genes. PMID: 24360965
- Histone H1.2 is found in lower abundance compared to other Histone H1 variants at the transcription start sites of inactive genes. Promoters enriched in Histone H1.2 differ from those enriched in other Histone H1 variants and are often associated with gene repression. PMID: 24476918
- Mutations in genes encoding linker histone variants, including HIST1H1 B, C, D, and E, as well as other genes such as OCT2 (POU2F2), IRF8, and ARID1A, have been implicated in the pathogenesis of follicular lymphoma. PMID: 24435047
- Evidence suggests that a cascade involving p53 acetylation and Histone H1.2 phosphorylation plays a critical role in activating p53-dependent DNA damage response pathways. PMID: 22249259
- Research has confirmed N-terminal acetylation on all Histone H1 isoforms, along with a single internal acetylation site. Phosphorylation sites have been identified 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 common role in diseases associated with amyloid-like fibrils. PMID: 16854430
- Histone H1.2 has been observed to translocate from the nucleus to the mitochondria following treatment with bleomycin. It co-localizes with Bak, a pro-apoptotic protein, within the mitochondria. PMID: 17879944
- Studies have indicated that the recruitment of YB1, PURalpha, and Histone H1.2 to the p53 target gene Bax is required for repression of p53-induced transcription. PMID: 18258596
