Analytical Data
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Gene name
SA
- Application
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Species
Pan-species (General)
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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
P22629
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Expression Region
Asp25~Gln183
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Molecular Weight
18&84kDa
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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
The study of SA (Streptavidin-Avidin) recombinant proteins originates from the need for high-affinity binding applications in molecular biology and biotechnology. Streptavidin, a protein derived from the bacterium *Streptomyces avidinii*, has a strong and specific affinity for biotin, a vitamin that plays a crucial role in cell metabolism. This exceptional binding strength has led to its widespread use in various applications, including protein purification, detection assays, and targeted drug delivery systems. The ability to produce recombinant forms of streptavidin enhances its utility by allowing researchers to modify the protein for specific purposes, such as improving binding kinetics, enhancing stability, or attaching other functional molecules. Additionally, the use of recombinant technology enables the production of streptavidin in large quantities and in a controlled environment, ensuring consistency and reliability in experimental outcomes. This has opened new avenues in the development of advanced diagnostic tools, biosensors, and therapeutic strategies, making SA recombinant proteins an important focus of ongoing research in both fundamental and applied sciences. Through this work, scientists are advancing our understanding of protein interactions and finding innovative solutions to complex biological problems.
