MYL12B Antibody (29): sc-130331

MYL12B Antibody (29) is a mouse monoclonal IgG2b antibody that detects MYL12B in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). MYL12B, also known as MRLC2, plays a crucial role in the regulation of smooth muscle and non-muscle cell contraction by interacting with myosin light chain kinase (MLCK) to facilitate phosphorylation. This post-translational modification is essential as it enhances the Actin-activated myosin ATPase activity, which is vital for muscle contraction and various cellular movements. The phosphorylation of MYL12B, in the presence of calcium and calmodulin, not only regulates contractile activity but also influences cellular processes such as migration and division, making MYL12B a key player in maintaining physiological functions. Anti-MYL12B antibody (29) is an invaluable tool for researchers studying muscle physiology, cellular dynamics, and the molecular mechanisms underlying various diseases, providing insights into the intricate regulation of muscle contraction and its implications in health and disease.

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MYL12B Antibody (29) References:

1. Dephosphorylation of distinct sites on the 20 kDa myosin light chain by smooth muscle myosin phosphatase.  |  Feng, J., et al. 1999. FEBS Lett. 448: 101-4. PMID: 10217418
2. Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin.  |  Tóth, A., et al. 2000. FEBS Lett. 484: 113-7. PMID: 11068043
3. Differential signalling by muscarinic receptors in smooth muscle: m2-mediated inactivation of myosin light chain kinase via Gi3, Cdc42/Rac1 and p21-activated kinase 1 pathway, and m3-mediated MLC20 (20 kDa regulatory light chain of myosin II) phosphorylation via Rho-associated kinase/myosin phosphatase targeting subunit 1 and protein kinase C/CPI-17 pathway.  |  Murthy, KS., et al. 2003. Biochem J. 374: 145-55. PMID: 12733988
4. Smooth muscle type isoform of 20 kDa myosin light chain is expressed in monocyte/macrophage cell lineage.  |  Higashihara, M., et al. 2008. J Smooth Muscle Res. 44: 29-40. PMID: 18480596
5. Exchange of 20-kDa myosin light chain-bound phosphate during sustained contraction of arterial smooth muscle.  |  Bárány, M., et al. 1991. Arch Biochem Biophys. 287: 199-203. PMID: 1897990
6. Identification of phosphorylated MYL12B as a potential plasma biomarker for septic acute kidney injury using a quantitative proteomic approach.  |  Wu, F., et al. 2015. Int J Clin Exp Pathol. 8: 14409-16. PMID: 26823757
7. Phosphorylation of brush border myosin at threonine on its 20 kDa light chains by a calmodulin-independent kinase activates its ATPase.  |  Borysenko, C., et al. 1988. FEBS Lett. 235: 149-52. PMID: 2969828
8. Phosphorylation by protein kinase C of a 20-kDa cytoskeletal polypeptide enhances its susceptibility to digestion by calpain.  |  Pontremoli, S., et al. 1987. Proc Natl Acad Sci U S A. 84: 398-401. PMID: 3025869
9. Inhibition of 20-kDa myosin light chain exchange by monoclonal antibodies against 17-kDa myosin light chain.  |  Higashihara, M. and Ikebe, M. 1995. FEBS Lett. 363: 57-60. PMID: 7729554
10. Phorbol ester-induced potentiation of myogenic tone is not associated with increases in Ca2+ influx, myoplasmic free Ca2+ concentration, or 20-kDa myosin light chain phosphorylation.  |  Laporte, R., et al. 1994. J Mol Cell Cardiol. 26: 297-302. PMID: 8028013

The preferred MYL9/MYL12A/B antibody is MYL9/MYL12A/B Antibody (E-4): sc-28329.