This Myl2 protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Myl2 is a crucial component involved in muscle contraction regulation. In the vertebrate skeletal muscles, Myl2 undergoes reversible phosphorylation, affecting myosin head orientation and myosin filaments' conformation [1]. Phosphorylation of Myl2 is central to controlling muscle contraction strength [2]. Specifically, in cardiac muscle, myosin light chain kinase 3 (MYLK3) phosphorylates cardiac Myl2, enhancing actin-myosin interactions and contractile force in the heart [3].
Smooth muscle contraction is primarily regulated by the phosphorylation of myosin light chains by a Ca2+/calmodulin-dependent myosin light chain kinase [4]. This phosphorylation of the regulatory light chain of smooth muscle myosin increases actin-activated MgATPase activity, initiating smooth muscle contraction [5]. Furthermore, myosin light chain kinases (MLCKs) phosphorylate the regulatory myosin light chain (MLC)-2, inducing actomyosin contraction and regulating vascular function [6].
References:
[1] Y. Borovikov and D. Levitsky, The effect of myosin light chain phosphorylation and mg2+ on the conformation of myosin in thick filaments of glycerinated fibers of rabbit skeletal muscle, European Journal of Biochemistry, vol. 183, no. 1, p. 83-88, 1989. https://doi.org/10.1111/j.1432-1033.1989.tb14899.x
[2] G. Smith, Angiotensin ii type 1 receptor and the activation of myosin light-chain kinase and protein kinase c-βii: mini review, Journal of Cardiology and Cardiovascular Medicine, vol. 5, no. 1, p. 024-028, 2020. https://doi.org/10.29328/journal.jccm.1001081
[3] T. Tobita, S. Nomura, H. Morita, T. Ko, T. Fujita, H. Tokoet al., Identification of mylk3 mutations in familial dilated cardiomyopathy, Scientific Reports, vol. 7, no. 1, 2017. https://doi.org/10.1038/s41598-017-17769-1
[4] P. Graceffa, L. Adam, & K. Morgan, Strong interaction between caldesmon and calponin, Journal of Biological Chemistry, vol. 271, no. 48, p. 30336-30339, 1996. https://doi.org/10.1074/jbc.271.48.30336
[5] D. Tang, Y. Kubota, & K. Kamm, Gtp/ggs‐induced phosphorylation of myosin light chain kinase in smooth muscle, Febs Letters, vol. 331, no. 3, p. 272-275, 1993. https://doi.org/10.1016/0014-5793(93)80351-t
[6] F. Wu, X. Guo, J. Xu, W. Wang, B. Li, Q. Huanget al., Role of myosin light chain and myosin light chain kinase in advanced glycation end product–induced endothelial hyperpermeability in vitro and in vivo, Diabetes and Vascular Disease Research, vol. 13, no. 2, p. 137-144, 2015. https://doi.org/10.1177/1479164115610469
