Histone H1⁰ Antibody (F-10): sc-377468

Histone H10 Antibody (F-10) is a mouse monoclonal IgG1 kappa light chain antibody that detects Histone H10 (H10) protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). H10 monoclonal antibody (F-10), also known as H1 histone family, member 0, plays a crucial role in chromatin structure and function, acting as a linker histone that facilitates DNA compaction into higher-order chromatin structures. Anti-H10 antibody (F-10) recognizes a protein particularly important in terminally differentiated cells and those with low rates of division, distinguishing H10 from other somatic H1 histones typically associated with proliferating cells. The unique expression pattern of H10 across various tissues in vertebrates suggests involvement in maintaining chromatin integrity during cellular differentiation. H10 is derived from an intronless gene, H1F0, located on chromosome 22q13.1 in humans. H10 undergoes various post-translational modifications, including methylation, acetylation, and phosphorylation, which can influence function and interactions with other chromatin-associated proteins, thereby impacting gene expression and cellular processes. Anti-H10 antibody (F-10) serves as an essential tool for researchers studying chromatin dynamics, differentiation, and regulatory mechanisms of gene expression in diverse biological contexts.

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Histone H1⁰ Antibody (F-10) References:

1. Ultraviolet laser footprinting of histone H1(0)-four-way junction DNA complexes.  |  Angelov, D., et al. 1999. Biochemistry. 38: 11333-9. PMID: 10471283
2. Accessibility of histone H1(0) and its structural domains to antibody binding in extended and folded chromatin.  |  Banchev, TB., et al. 1990. Mol Cell Biochem. 95: 167-75. PMID: 1694955
3. Calorimetric studies of the interactions of linker histone H1(0) and its carboxyl (H1(0)-C) and globular (H1(0)-G) domains with calf-thymus DNA.  |  Machha, VR., et al. 2013. Biophys Chem. 184: 22-8. PMID: 24036047
4. Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H10, Its carboxyl domain (H10-C) or globular domain (H10-G) to B-DNA.  |  Machha, VR., et al. 2017. Biochem Biophys Rep. 12: 158-165. PMID: 29090277
5. Effect of Phosphorylation on the Structural Behaviour of Peptides Derived from the Intrinsically Disordered C-Terminal Domain of Histone H1.0.  |  Chaves-Arquero, B., et al. 2020. Chemistry. 26: 5970-5981. PMID: 32073728
6. Selective inhibition of cancer cell self-renewal through a Quisinostat-histone H1.0 axis.  |  Morales Torres, C., et al. 2020. Nat Commun. 11: 1792. PMID: 32286289
7. Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges.  |  Martinsen, JH., et al. 2022. Protein Sci. 31: 918-932. PMID: 35066947
8. Effects of butyric acid on cell cycle regulation and induction of histone H1(0) in mouse cells and tissue culture. Inducibility of H1 (0)in the late S-G2 phase of the cell cycle.  |  Chabanas, A., et al. 1985. J Mol Biol. 183: 141-51. PMID: 4009723
9. Relationship between core histone acetylation and histone H1(0) gene activity.  |  Girardot, V., et al. 1994. Eur J Biochem. 224: 885-92. PMID: 7925412
10. Uncoordinated regulation of histone H1(0)synthesis and H1(0) mRNA level.  |  Rousseau, D. 1996. Biochem Mol Biol Int. 38: 1023-32. PMID: 9132149

The preferred Histone H1⁰ antibody is Histone H1⁰ Antibody (34): sc-56695.