Analytical Data
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Gene name
CAV2
- Application
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Alternative Names
CAV2；Caveolin-2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P51636
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Expression Region
1-162aa
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AA Sequence
MGLETEKADVQLFMDDDSYSHHSGLEYADPEKFADSDQDRDPHRLNSHLK LGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIA GILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVIIAPLCTSVGR CFSSVSLQLSQD
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Molecular Weight
44 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
CAV2, or caveolin-2, is a member of the caveolin protein family, which plays a crucial role in the formation of caveolae, small invaginations in the plasma membrane that are implicated in various cellular processes, including signal transduction, lipid metabolism, and endocytosis. Research on CAV2 has gained prominence due to its potential involvement in various pathological conditions, including cancer, cardiovascular diseases, and metabolic disorders. The study of CAV2 recombinant protein is particularly significant for understanding its structure-function relationship and elucidating its role in cellular dynamics. Recombinant protein expression allows for the production of large quantities of CAV2 for functional assays and structural studies. By utilizing techniques such as bacterial or eukaryotic cell expression systems, researchers can generate purified CAV2 protein to investigate its biochemical properties, interaction with membrane components, and effects on cellular signaling pathways. Furthermore, insights gained from CAV2 recombinant protein studies can inform therapeutic strategies targeting caveolar mechanisms, potentially leading to novel interventions in diseases where caveolin dynamics are altered. This area of research holds promise in enhancing our understanding of membrane biology and developing targeted therapies that exploit the unique properties of caveolin proteins in disease contexts. Ultimately, the continued exploration of CAV2 through recombinant protein studies may pave the way for significant advances in biomedical research and clinical applications.
