STOM Antibody

Stomatin is an integral membrane protein found in lipid/protein-rich microdomains of almost all human tissues. It was named after the rare human disease, haemolytic anaemia hereditary stomatocytosis. Stomatin is implicated in signal transduction and cell communication, and it may regulate cation movement through ion channels and transporters .

Stomatin is a 31 kDa monotopic integral membrane protein that is palmitoylated, forms homo-oligomers, and associates with cholesterol-rich membrane domains, also known as lipid rafts . It is part of the SPFH superfamily, which includes stomatin-like proteins, prohibitins, flotillin/reggie proteins, bacterial HflK/C proteins, and erlins . The protein’s structure includes a conserved PHB/SPFH domain, which is essential for its function and association with cholesterol-rich membranes .

The absence of stomatin in red cells is associated with Overhydrated Hereditary Stomatocytosis (OHSt), a condition characterized by the leakage of sodium and potassium ions into and from erythrocytes . However, stomatin knockout mice are viable and do not exhibit stomatocytosis, suggesting that the absence of stomatin in OHSt erythrocytes is due to mistrafficking during terminal erythropoiesis .

The mouse anti-human stomatin antibody is a monoclonal antibody that detects the stomatin protein of human origin. It is used in various applications, including Western blotting, immunoprecipitation, immunofluorescence, immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA) . The antibody is available in both non-conjugated and conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates .

Stomatin has been extensively studied for its role in cellular processes and its association with lipid rafts. Recent studies have focused on the structure-function analysis of stomatin, revealing the importance of specific amino acid residues and domains for its function . These studies have shown that stomatin is a cholesterol-binding protein and that its association with cholesterol-rich membranes is crucial for its oligomerization and function .