Analytical Data
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基因名
SBP65
- Application
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别名
BP75 Seed biotinylated protein of 65KDA
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种属
Glycine max
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q39846
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表达区间
1-255aa
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分子量
44 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.












