Recombinant Human MYO1A protein

MYO1A, a member of the myosin superfamily, is a class I myosin encoded by the MYO1A gene in humans. It belongs to a group of actin-based motor proteins that utilize ATP hydrolysis to generate mechanical force, enabling cellular processes such as membrane-cytoskeleton interactions, intracellular trafficking, and mechanotransduction. MYO1A consists of a conserved N-terminal motor domain responsible for actin binding and ATPase activity, followed by a neck region with light chain-binding motifs and a C-terminal tail domain that mediates membrane association. Unlike other myosins, class I myosins lack a coiled-coil dimerization domain, functioning as monomers.

This protein is predominantly expressed in epithelial tissues, particularly in the intestines and kidneys, where it localizes to microvilli and contributes to maintaining cell polarity and structural integrity. MYO1A facilitates the tethering of plasma membranes to the actin cytoskeleton, stabilizing dynamic cellular protrusions and regulating vesicle transport. Its role in membrane remodeling and signal transduction has implicated MYO1A in processes like nutrient absorption, cell migration, and immune responses.

Recombinant MYO1A protein is engineered for in vitro studies to dissect its molecular mechanisms, often expressed in bacterial or eukaryotic systems with affinity tags (e.g., His-tag) for purification. Researchers use it to investigate actin-binding kinetics, ATPase activity, and interactions with lipid membranes or signaling molecules. Dysregulation of MYO1A has been linked to pathologies, including colorectal cancer and hearing loss, making its recombinant form valuable for drug screening and structural analyses (e.g., cryo-EM) to design targeted therapies. Studies also explore its potential as a biomarker for epithelial-derived diseases.