Analytical Data
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Gene name
SBP65
- Application
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Alternative Names
BP75 Seed biotinylated protein of 65KDA
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Species
Glycine max
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q39846
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Expression Region
1-255aa
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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
Related Products
Protein Description
SBP65, a key protein involved in various biological processes, has garnered significant attention in the fields of molecular biology and biotechnology. Research indicates that SBP65 is crucial for plant development, particularly in regulating gene expression during stress responses. Its role as a transcription factor highlights its potential in enhancing stress tolerance in crops, an increasingly important trait given the challenges posed by climate change and food security. The ability to manipulate SBP65 through recombinant DNA technology offers promising avenues for genetically engineering plants with improved resilience to environmental stressors. Additionally, studies have shown that SBP65 can interact with other proteins and regulatory molecules, suggesting a complex network of interactions that could be leveraged for agricultural advancements. The ongoing investigation into the structure-function relationships of SBP65 aims to uncover its mechanistic pathways, ultimately contributing to the development of sustainable agricultural practices. Researchers are particularly interested in creating SBP65 fusion proteins that could serve as tools for studying gene regulation and enhancing crop yields, thus addressing global food demands. As the implications of SBP65 extend beyond basic research into practical applications, it represents a fruitful area for innovation in crop biotechnology and sustainable agriculture.
