Analytical Data
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基因名
X27S,X28S,X29S
- Application
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别名
(Ag35)(Virion envelope protein p35)(Fragments)
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种属
Vaccinia virus
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表达系统
E. coli
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标签
C- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P30895
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表达区间
1-56aa(X27S,X28S,X29S)
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分子量
7.5 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
The recombinant proteins X27S, X28S, and X29S are part of an ongoing investigation into the functional and structural properties of proteins derived from specific organisms. These proteins are of interest due to their potential applications in biotechnology and medicine, including their roles in molecular interactions and enzymatic activities. Each variant, differentiated by minor sequence changes, may exhibit unique characteristics that can influence their stability, activity, or interaction with other biomolecules. Research on these proteins focuses on understanding the mechanisms underlying their functions, exploring their potential as therapeutic agents, and leveraging their properties for industrial applications. By employing techniques such as protein expression, purification, and characterization, scientists aim to elucidate the biological relevance and practical utility of X27S, X28S, and X29S. This work contributes to a broader understanding of protein engineering and opens avenues for innovations in drug development and synthetic biology.
