MYL5 (1-173 a.a.) Human

The recombinant form of MYL5, specifically the 1-173 amino acid (a.a.) sequence, is produced in E. coli. This recombinant protein is a single, non-glycosylated polypeptide chain containing 197 amino acids, including a 24 amino acid His-tag at the N-terminus . The His-tag is often used to facilitate purification of the protein through affinity chromatography techniques.

MYL5 is involved in the regulation of myosin ATPase activity, which is essential for muscle contraction. The light chains of myosin, including MYL5, bind to the neck region of the myosin heavy chain and modulate its interaction with actin filaments. This interaction is critical for the conversion of chemical energy (from ATP hydrolysis) into mechanical work, enabling muscle contraction and other cellular movements.

Recombinant MYL5 is used in various research applications, including studies on muscle physiology, cellular motility, and signal transduction pathways. It is also utilized in biochemical assays to investigate the mechanisms of myosin function and regulation. The availability of recombinant MYL5 allows researchers to study its properties in a controlled environment, free from the complexities of whole-cell systems.

The production of recombinant MYL5 involves cloning the gene encoding the protein into an expression vector, which is then introduced into E. coli cells. The bacteria are cultured, and the recombinant protein is expressed and subsequently purified using chromatographic techniques. The His-tag at the N-terminus of MYL5 facilitates its purification by binding to nickel or cobalt ions immobilized on a resin, allowing for efficient isolation of the protein .