STOM Human

Stomatin is characterized by its palmitoylation, oligomerization, and hydrophobic “hairpin” structure, which shows similarity to caveolins and other integral scaffolding proteins . The protein forms homo-oligomers and associates with cholesterol-rich membranes, playing a crucial role in maintaining membrane integrity and function . The conserved PHB/SPFH domain of stomatin is essential for its structure and function, with specific amino acid residues and subdomains being critical for its interaction with cholesterol-rich membranes .

Recombinant human stomatin is produced using DNA sequences encoding the human STOM gene, which are expressed in host cells such as HEK293 cells . The recombinant protein typically consists of 468 amino acids and has a predicted molecular mass of 52.1 kDa . It is often purified to a high degree of purity (>95%) and is formulated in sterile PBS for stability .

The recombinant protein is used in various research applications to study the biochemical properties and functions of stomatin. It is also utilized in structural and functional analyses to understand the role of specific domains and residues in stomatin’s interaction with membranes and other cellular components .

Research on stomatin has revealed its importance in various cellular processes, including its role in membrane organization, signal transduction, and interaction with the cortical actin cytoskeleton . Studies have shown that stomatin is a cholesterol-binding protein, and its association with cholesterol-rich membranes is crucial for its function . The protein’s coiled-coil domain is necessary for oligomerization, while the C-terminus is involved in lateral mobility and binding to the actin cytoskeleton .

Overall, recombinant human stomatin is a valuable tool for researchers studying membrane biology and the molecular mechanisms underlying stomatin’s functions in cells.