Human/Mouse Myl9/12 (F6) rabbit mAb

Myosin regulatory light chain (Myl) 9 is a regulatory subunit of the ATPase myosin protein. Myl9 regulates actin rearrangement to direct cellular migration, shape, and adhesion. Myl9 itself is regulated by post-translational modifications, including phosphorylation, acetylation and methylation. Phosphorylation of Myl9 at Thr18 and Ser19 promotes myosin ATPase activity and interaction with actin. Nα-acetylation of Myl9 has been shown to increase Ser19 phosphorylation and cytoplasmic activity, while Nα-methylation promotes DNA binding in the nucleus. Myl9, Myl12a, and Myl12b (Myl9/12) have been identified as functional ligands for CD69 in inflamed lungs, playing a major role in chronic inflammatory disorders such as chronic rhinosinusitis. Homozygous deletion in the MYL9 gene in humans has been identified as a putative molecular basis of the disease megacystis-microcolon-intestinal hypoperistalsis (MMIHS) syndrome, especially considering Myl9’s role in contracting smooth muscle cell.