2-hydroxyisobutyryl-HIST1H1C (K80) Antibody
Description
Introduction to 2-Hydroxyisobutyryl-HIST1H1C (K80) Antibody
The 2-hydroxyisobutyryl-HIST1H1C (K80) Antibody is a polyclonal rabbit-derived antibody designed to specifically recognize the 2-hydroxyisobutyrylation post-translational modification at lysine 80 (K80) of the histone H1.2 protein (encoded by HIST1H1C). This modification is part of a growing class of histone acylations that regulate chromatin structure, transcriptional activity, and cellular responses .
Histone H1.2 is a linker histone critical for chromatin compaction and nucleosome stability. Its 2-hydroxyisobutyrylation at K80 is implicated in epigenetic regulation and nuclear signaling, though its precise biological roles remain under investigation .
Epigenetic and Chromatin Studies
The antibody is validated for detecting 2-hydroxyisobutyrylated H1.2 in human samples. Key applications include:
-
ELISA: Quantification of 2-hydroxyisobutyryl-H1.2 levels in cell lysates.
-
ChIP: Mapping genomic regions enriched with 2-hydroxyisobutyrylated H1.2, enabling analysis of its role in chromatin accessibility and transcriptional regulation .
Role in Chromatin Dynamics
H1.2 variants, including H1.2, are distributed genome-wide, with distinct patterns at promoters and regulatory regions . The 2-hydroxyisobutyrylation at K80 may modulate H1.2’s interaction with DNA or chromatin-associated proteins, affecting nucleosome stability.
Link to Nuclear Signaling
Histone acylations, such as 2-hydroxyisobutyrylation, are emerging as regulators of nuclear signaling pathways. For example, histone H1.2 influences STAT3 activation in hepatocellular carcinoma , and similar mechanisms may apply to 2-hydroxyisobutyrylated H1.2.
Limitations and Challenges
-
Specificity: Polyclonal antibodies may cross-react with other acylated histones. Validation against non-modified H1.2 is critical.
-
Reactivity: Currently validated for human samples; cross-reactivity with other species is unconfirmed .
Optimized Protocols
-
ChIP: Ensure proper fixation and sonication to preserve chromatin integrity.
-
ELISA: Use blocking agents to minimize non-specific binding.
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 regulation by H1.2. H1.2 enhances the global association of pRb with chromatin, amplifies 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 observed histones H1.2 and H1.4 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. Additionally, the study reports the observation of the H1.2 SNP variant A18V in MCF-10A cells. PMID: 26209608
- Interactions 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. 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 contribute to the pathogenesis of follicular lymphoma. PMID: 24435047
- These findings 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, along with a single internal acetylation site. Phosphorylation sites were 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 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
- Studies have indicated 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
