MYL9 Human

Myosin Light Chain 9 (MYL9), also known as Myosin Regulatory Light Chain 2, is a protein encoded by the MYL9 gene in humans. This protein is a crucial component of the myosin complex, which plays a significant role in muscle contraction and various cellular processes. Myosin is composed of two heavy chains and four light chains, with MYL9 being one of the light chains that regulate the ATPase activity of myosin heads, thereby modulating muscle contraction .

MYL9 is a regulatory subunit that binds calcium and is activated by myosin light chain kinase. This activation is essential for the regulation of both smooth muscle and non-muscle cell contractile activity. The phosphorylation of MYL9 is implicated in several cellular processes, including cytokinesis, receptor capping, and cell locomotion .

The recombinant form of MYL9 is typically produced using bacterial expression systems. The gene encoding MYL9 is cloned into an expression vector, which is then introduced into a bacterial host, such as Escherichia coli. The bacteria are cultured, and the recombinant protein is expressed and subsequently purified using techniques such as affinity chromatography. This method ensures the production of high-purity MYL9 for research and therapeutic applications.

MYL9 undergoes several post-translational modifications, including phosphorylation, which is critical for its function. The phosphorylation state of MYL9 can be analyzed using techniques such as Western blotting and mass spectrometry. These methods allow researchers to study the regulatory mechanisms of MYL9 and its role in various cellular processes.

MYL9 has been implicated in various diseases, including Megacystis-Microcolon-Intestinal Hypoperistalsis Syndrome and certain types of cancer. Recent studies have shown that MYL9 plays a vital role in immune infiltration, tumor invasion, and metastasis. Its expression levels are associated with prognosis in several cancers, making it a potential biomarker for cancer diagnosis and treatment .