Anti-Myosin Light Chain (N-terminal region) Antibody

Both smooth muscle and nonmuscle myosin II activity is regulated by the phosphorylation state of the myosin regulatory light chain (MLC, MRLC, MLC20, Myl9) . Phosphorylation of MLC at Thr-18 and Ser-19 activates myosin II motor activity and increases myosin filament stability. This activation has important roles in various cell motile processes. By contrast, other phosphorylation sites on MLC may inhibit myosin II activity. PKC phosphorylates Ser-1/Ser-2 and Thr-9 in MLC, and this phosphorylation decreases activated myosin II interaction with actin, as well as inhibits MLC interaction with the activation site kinase, myosin light-chain kinase. The Ser-1/Ser-2 region may be the major inhibitory site since Ser-1 is phosphorylated during PDGF-induced stress fiber disassembly and expression of unphosphorylatable MLC20 at the Ser-1/Ser-2 site suppresses this disassembly. Thus, inhibition of myosin II activity through phosphorylation of Ser-1/Ser-2 may have important roles in growth factor-induced reorganization of actomyosin filaments.

Our Myosin Light Chain (N-terminal region) rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects chicken, human, mouse, and rat Myosin Light Chain (N-terminal region) and is antigen affinity purified. It is great for use in WB, ICC.

MLC synthetic peptide (coupled to KLH) corresponds to amino acid residues in the N-terminus of human myosin regulatory light chain 12A (Myl12A) . This peptide sequence is highly conserved in human, rat, mouse, chicken, and zebrafish Myl12A, and in other smooth muscle and non-muscle MLCs.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.