Analytical Data
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Gene name
SPARC
- Application
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Alternative Names
SPARC; BM-40; Secreted Protein,Acidic,Cysteine-Rich; Basement-membrane protein 40; Secreted protein acidic and rich in cysteine
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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 90% as determined by SDS-PAGE.
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Uniprot
P09486
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Expression Region
Ala18~Ile303
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Molecular Weight
48&28kDa
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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
SPARC (Secreted Protein Acidic and Rich in Cysteine) is a hallmark matricellular protein that plays pivotal roles in cellular functions such as adhesion, proliferation, and differentiation. Initially identified in bone tissue, SPARC is now recognized as a crucial component in various biological processes, including wound healing, angiogenesis, and tumor biology. Its expression levels have been correlated with several pathologies, notably cancer, where it can influence tumor growth and metastasis. Researchers have focused on SPARC as a potential therapeutic target due to its ability to modulate the tumor microenvironment and ECM interactions. The study of SPARC recombinant proteins has enabled deeper investigations into its functional mechanisms and interactions with other cellular components. These recombinant proteins provide researchers with tools to explore SPARC's role in different contexts by allowing for controlled experiments that elucidate its behavior in the extracellular matrix. Furthermore, the development of SPARC-based biomaterials has shown promise in tissue engineering and regenerative medicine. Overall, the research surrounding SPARC recombinant proteins highlights their significance in understanding complex biological processes and their potential applications in developing novel therapeutic strategies.
