Analytical Data
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Gene name
Stomatin/STOM
- Application
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Alternative Names
Protein 7.2b Stomatin
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27105
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Expression Region
1-288aa
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Molecular Weight
47.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Stomatin, encoded by the STOM gene, is an integral membrane protein predominantly found in the lipid rafts of various cell types, including erythrocytes and epithelial cells. Its function has been linked to multiple cellular processes, including ion channel regulation, membrane microdomain formation, and cellular signaling. Research has shown that stomatin plays a critical role in maintaining the integrity of the cell membrane and influencing the activity of various ion channels, particularly those involved in potassium and sodium transport. Moreover, stomatin has been implicated in the pathology of several diseases, such as hypertension, chronic obstructive pulmonary disease (COPD), and certain types of cancer, highlighting its potential as a therapeutic target. Given its significant role in modifying membrane properties and cellular responses, the study of Stomatin/STOM recombinant proteins has gained traction as a means to elucidate the protein's structure-function relationship. Recent advancements in recombinant protein technology allow for the production of these proteins in sufficient quantities for in vitro studies, enabling researchers to investigate their interaction with lipids and other membrane proteins. Understanding the mechanisms by which stomatin modulates ion channels and cellular functions could pave the way for innovative treatments leveraging its regulatory capabilities in various health disorders. As such, research into Stomatin/STOM recombinant proteins is of high relevance, not only for basic biomedical research but also for potential clinical applications in targeting disorders associated with dysregulated ionic homeostasis and membrane function.
