Analytical Data
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Gene name
Streptavidin
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简介
Streptavidin forms a strong, non-covalent, specific homotetramer with biotin, with each subunit capable of binding one biotin molecule. Streptavidin Protein (A24C, His) is the recombinant others-derived Streptavidin protein, expressed by E. coli, with C-His labeled tag.
- Application
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Alternative Names
Streptavidin; LSA
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Species
Others
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Source
E. coli
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22629-1
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Expression Region
C24-Q183, A24C
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Protein Length
Partial
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Molecular Weight
20-22 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
Streptavidin is a tetrameric protein derived from the bacterium **Streptomyces avidinii**, known for its high affinity for biotin (vitamin B7). This remarkable binding capability makes streptavidin an invaluable tool in various biochemical and biomedical applications, including molecular biology, diagnostics, and therapeutics. The interaction between streptavidin and biotin is among the strongest non-covalent interactions known, providing a robust system for tagging and detecting proteins or other biomolecules. Research on recombinant streptavidin has gained momentum due to advancements in genetic engineering and protein expression techniques, allowing scientists to produce variants with enhanced properties such as improved solubility, stability, and reduced non-specific binding. Various modifications, including biotinylation, conjugation with fluorescent markers, and integration into affinity chromatography systems, have further expanded its utility. Additionally, the exploration of streptavidin's role in targeted drug delivery systems and biosensor development underscores its significance in current research. As a result, understanding the structure-function relationship of recombinant streptavidin continues to be a crucial area of investigation, with implications for developing more effective diagnostic tools and targeted therapies in modern medicine.
