Histone H1 (Phospho-Thr17) polyclonal antibody

Histones are evolutionarily conserved proteins that play a vital role in the compaction, storage, and regulation of DNA within the eukaryotic nucleus. The basic subunit of chromatin, the nucleosome core particle, is composed of DNA wound around two copies each of the core histone proteins H2A, H2B, H3, and H4. Formation of higher order chromatin structure is facilitated through the binding of linker histone H1 to the nucleosome particle (chromatosome) . In humans and mice, there are 11 distinct histone H1 variants, which include the somatic variants (H1.1, H1.2, H1.3, H1.4, and H1.5) that are expressed ubiquitously, and cell type specific variants such as H1t found in the testis and H1.0 expressed in terminally differentiated cells. Binding of histone H1 to chromatin limits accessibility of DNA to other proteins by stabilizing nucleosome positioning, competing for binding sites, and limiting the activity of chromatin remodeling proteins such as the SWI/SNF complex. Histone H1 binding is highly dynamic and is thought to be regulated by post-translational modifications. For example, cell cycle regulated phosphorylation of histone H1 leads to chromatin condensation and decondensation depending on the site of phosphorylation and histone H1.4 Lys34 acetylation by GCN5 has been linked to increased mobility of H1.4 and transcriptional activation.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of Histone H1 (Phospho-Thr17) polyclonal antibody at 1:500 dilution Lane1:Hela treated with λ-phosphatase whole cell lysate (30ug) Lane2:HeLa whole cell lysate (30ug)