GeneTex, a leading manufacturer of antibodies and antibody-related reagents, is set to launch a new antibody against phosphorylated Histone H3. Histone proteins package and organize the DNA of eukaryotic cells into structural units referred to as nucleosomes, and the modification of histone tails plays a critical role in the modulation of gene transcription.
The phosphorylation of Histone H3 at serine residue 10 by Msk1 during interphase marks transcriptional activation. Aurora kinase B also phosphorylates Ser10, along with Ser28, at the onset of mitosis to initiate chromosome condensation. More recent evidence suggests that the phosphorylation of Histone H3 at Ser10 stimulates Lys14 acetylation and may also act as a "master switch" that prevents the abnormal phosphorylation of Histone H3 at other sites during mitosis.
GeneTex's new Histone H3 (phospho Ser10) antibody will allow researchers to further examine the role that histone phosphorylation plays in complex epigenetic processes. The antibody has been validated for western blotting in both human and mouse samples as well as for immunocytochemistry/immunofluorescence.