Analytical Data
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基因名
yst
- Application
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别名
yst；Probable 3'.5'-cyclic-AMP phosphodiesterase pde-4
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P31518
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表达区间
51-66aa
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氨基酸序列
SDWCCEVCCNPACAGC
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分子量
17.1 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
Yst, or yeast sacramento strain, is a model organism widely used in biological research due to its simplicity and similarity to higher eukaryotic systems. The study of Yst recombinant proteins has gained momentum as researchers explore the potential of these proteins in various applications, including industrial enzymes, pharmaceuticals, and vaccine development. The ability to manipulate the yeast genome allows for precise alterations in protein expression, leading to the production of novel proteins with enhanced properties or specific functionalities. Furthermore, Yst's eukaryotic nature enables proper post-translational modifications, which are essential for the biological activity of many complex proteins. As the demand for efficient and sustainable production methods grows, Yst recombinant proteins are increasingly seen as a viable alternative to traditional expression systems, facilitating advances in biotechnology and medicine. Current research focuses on optimizing expression systems, improving protein yield and stability, and understanding the biological roles of these proteins. Overall, the exploration of Yst recombinant proteins holds promise for innovative solutions to address various scientific and industrial challenges.
