MYL2
MYL2 (myosin light chain 2, also known as CMH10) is the ventricular/cardiac isoform of the myosin regulatory light chain. It is a contractile sarcomeric protein that supports heart development and cardiac muscle function. Browse Assay Genie's current range of MYL2 research reagents below, or read on for the biology behind the target.
MYL2 is a contractile protein that plays a role in heart development and function. Once phosphorylated, it influences cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion. The result is a higher maximum contraction force and greater calcium sensitivity of contraction force. Together these events slow myosin kinetics and prolong the duty cycle, so that accumulated myosins are cooperatively recruited to actin binding sites. This sustains thin filament activation and fine-tunes the calcium sensitivity of force in the myofilament.
The MYL2 gene encodes a major sarcomeric protein of mammalian striated muscle. UniProt places the protein in the cytoplasm, within the myofibril, at the sarcomere A band. During cardiogenesis it acts early in cardiac contractility by promoting cardiac myofibril assembly. According to the NCBI Gene summary, the protein contributes to embryonic heart muscle structure and function. In adults, its phosphorylation is involved in cardiac myosin cycling kinetics, torsion and function. Orthologous genes are named Myl2 in both mouse and rat, which makes rodent models a common route for studying the protein.
The protein is formally named myosin regulatory light chain 2, ventricular/cardiac muscle isoform, and HGNC classifies the gene in the group of class 2 myosin light chains. Earlier names described it as the cardiac, slow regulatory myosin light chain, and CMH10 is a recorded alias. Mutations in the MYL2 gene are associated with hypertrophic cardiomyopathy 10 and with infant-onset myopathy, so the protein is relevant to studies of inherited cardiac and muscle disease.
Phosphorylation of MYL2 alters cross-bridge cycling kinetics, lever arm stiffness and calcium sensitivity of force, making it central to studies of cardiac contraction.
MYL2 promotes cardiac myofibril assembly during cardiogenesis and contributes to embryonic heart muscle structure and function.
As a major sarcomeric protein of striated muscle located at the A band, MYL2 is a relevant target for myofilament organisation studies.
Mutations in MYL2 are associated with hypertrophic cardiomyopathy 10 and infant-onset myopathy, linking the gene to inherited heart and muscle disease.
MYL2 is a contractile protein of cardiac muscle that supports heart development and function. When phosphorylated, it increases myosin lever arm stiffness and promotes myosin head diffusion, which raises contraction force and calcium sensitivity. During cardiogenesis it also promotes cardiac myofibril assembly.
MYL2 is also called CMH10, and its full HGNC name is myosin light chain 2. Previous names describe it as the cardiac, slow regulatory myosin light chain. The UniProt name is myosin regulatory light chain 2, ventricular/cardiac muscle isoform.
Mutations in MYL2 are associated with hypertrophic cardiomyopathy 10 and infant-onset myopathy. The gene has orthologues named Myl2 in mouse and rat, so rodent studies are possible. Check the datasheet of any product for its validated reactivity.
Other myosin light chains and the myosin light chain kinase, relevant to muscle contraction and sarcomere research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P10916; product specifications from Assay Genie datasheets.