Recombinant Human MYO1G protein

MYO1G (Myosin-1G) is a member of the myosin superfamily of actin-based motor proteins, which play critical roles in cellular processes such as membrane remodeling, vesicle trafficking, and mechanotransduction. As a class I myosin, MYO1G is a single-headed motor protein characterized by a conserved N-terminal motor domain that binds actin and hydrolyzes ATP, a neck region with light chain-binding sites, and a C-terminal tail domain that mediates interactions with cellular membranes or cargo molecules. It is predominantly expressed in immune cells, particularly T lymphocytes and B cells, where it localizes to the plasma membrane and intracellular vesicles. Studies suggest MYO1G contributes to immune cell functions, including adhesion, migration, and receptor clustering, by linking the actin cytoskeleton to membrane components.

Recombinant MYO1G proteins are engineered using expression systems (e.g., bacterial, insect, or mammalian cells) to produce purified, functional forms of the protein for structural and functional studies. These proteins often include affinity tags (e.g., His-tag, GST) to facilitate purification and detection. Researchers utilize recombinant MYO1G to investigate its ATPase activity, actin-binding kinetics, and interactions with signaling molecules or membrane lipids. Its role in immune regulation has spurred interest in MYO1G as a potential therapeutic target for autoimmune diseases or cancers. Additionally, recombinant MYO1G serves as an antigen for antibody development or diagnostic toolkits. Ongoing research aims to elucidate its precise molecular mechanisms in immune cell dynamics and disease contexts, highlighting its relevance in both basic cell biology and translational medicine.