Analytical Data
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Gene name
Sorcin/SRI
- Application
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Alternative Names
SCN; CP-22; V19; 22 kDa protein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P30626
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Expression Region
Gly29~Leu169
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Molecular Weight
19kDa
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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
Related Products
Protein Description
Sorcin (soluble resistance-related calcium-binding protein) is a member of the penta-EF-hand family of calcium-binding proteins, primarily known for its role in cellular calcium homeostasis and its involvement in various physiological processes, including apoptosis, cytoskeletal dynamics, and signal transduction. Recent studies have highlighted its significant role in cancer biology, as elevated levels of Sorcin have been associated with chemoresistance and poor prognosis in various cancers. The study of Sorcin/SRI (Sorcin-related protein) recombinant proteins is crucial for unraveling the underlying molecular mechanisms of its functions and interactions in cellular pathways. By producing recombinant Sorcin through molecular cloning techniques and subsequent expression in suitable host systems, researchers can investigate its calcium-binding properties, structural dynamics, and influence on cancer cell behavior. The ability to manipulate and analyze Sorcin's interactions with other cellular proteins also provides valuable insights into potential therapeutic targets for overcoming drug resistance in cancer treatment. Thus, research on Sorcin/SRI recombinant proteins not only contributes to our understanding of fundamental biological processes but also holds promise for developing innovative strategies to enhance the efficacy of existing cancer therapies.
