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STOM encodes a member of a highly conserved family of integral membrane proteins.
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Human Polyclonal STOM Primary Antibody for ELISA, IHC - ABIN4356634
Mrówczyńska, Salzer, Perutková, Iglič, Hägerstrand: Echinophilic proteins stomatin, sorcin, and synexin locate outside gangliosideM1 (GM1) patches in the erythrocyte membrane. in Biochemical and biophysical research communications 2010
These results may suggest that stomatin is a new prognostic indicator for HER2 (show ERBB2 Antibodies)-positive breast cancer
FRAP analyses indicate that the stomatin C-terminus is the dominant entity for lateral mobility and binding site for the cortical actin cytoskeleton
This study showed that cells expressing more stomatin or exposed to exogenous stomatin are more prone to undergoing cell fusion; during osteoclastogenesis, depletion of stomatin inhibited cell fusion but had little effect on tartrate-resistant acid phosphatase (show ACP5 Antibodies) production.
Authors took a proteomic approach to identify stomatin, a member of the integral proteins of lipid rafts, as a cellular protein interacting with hepatitis C virus NS5B.
Stomatin protein expression is down-regulated in 80% of non-small cell lung cancer samples.
upregulation of stomatin by hypoxia and dex may enhance the barrier function of alveolar epithelia and mediate the adaptive role of glucocorticoid to hypoxia
Stomatin interacts with GLUT1/SLC2A1 (show SLC2A1 Antibodies), band 3/SLC4A1 (show SLC4A1 Antibodies), and aquaporin-1 (show AQP1 Antibodies) in human erythrocyte membrane domains
[review] Stomatin family member STOM is oligomeric; it localizes mostly to membrane domains and has been shown to modulate ion channel activity.
The study indicates that stomatin, sorcin, and synexin are echinophilic membrane components that mainly locate outside GM1 rafts in the human erythrocyte membrane.
This study demonstrated the existence of alpha-granular lipid rafts and suggests an important role for stomatin in the organization and function of alpha granules.
Regulation of ASIC channels by a stomatin/STOML3 complex located in a mobile vesicle pool in sensory neurons.
Dimerization of stomatin is crucial for the repression of acid-sensing ion channel 3 (ASIC3 (show ACCN3 Antibodies)) activity.
These observations suggest that stomatin may play important roles in astrocytes and other cells by interacting with Panx1 (show PANX1 Antibodies) carboxyl terminal to limit channel opening.
Provides evidence for a new structural form of stomatin.
stomatin binds to and alters the gating of acid-sensing ion channels
stomatin is required for normal mechanotransduction in a subpopulation of vertebrate sensory neurons
This gene encodes a member of a highly conserved family of integral membrane proteins. The encoded protein localizes to the cell membrane of red blood cells and other cell types, where it may regulate ion channels and transporters. Loss of localization of the encoded protein is associated with hereditary stomatocytosis, a form of hemolytic anemia. There is a pseudogene for this gene on chromosome 6. Alternative splicing results in multiple transcript variants.
erythrocyte band 7 integral membrane protein
, erythrocyte protein band 7.2
, sialyltransferase om
, erythrocyte membrane protein band 7.2 (stomatin)
, erythrocyte surface protein band 7.2
, protein 7.2b
, erythrocyte protein band 7.2; protein 7.2b