Analytical Data
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基因名
D15Wsu75e
- Application
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别名
Desi1; D15Wsu75e; Fam152b; Pppde2; Desumoylating isopeptidase 1; DeSI-1; EC 3.4.-.-; PPPDE peptidase domain-containing protein 2
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9CQT7
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表达区间
1-168aa
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氨基酸序列
MEPPNLYPVKLYVYDLSKGLARRLSPIMLGKQLEGIWHTSIVVHKDEFFFGSGGISSCPPGGTLLGPPDSVVDVGSTEVTEEIFLEYLSSLGESLFRGEAYNLFEHNCNTFSNEVAQFLTGRKIPSYITDLPSEVLSTPFGQALRPLLDSIQIQPPGGSSVGRPNGQS
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分子量
44.7 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 D15Wsu75e recombinant protein has garnered interest within the scientific community due to its potential applications in various fields, including vaccine development and therapeutic interventions. This protein, derived from the D15 strain of the Wusida virus, exhibits unique structural features that may enhance immune response mechanisms. Researchers are particularly focused on its role in eliciting antibodies, which could lead to improved vaccine formulations against viral infections. The study of D15Wsu75e involves advanced techniques such as molecular cloning, protein expression, and purification, enabling scientists to explore its functional properties in vitro and in vivo. Furthermore, understanding the immunogenicity of this protein can pave the way for new strategies in tackling infectious diseases, contributing to public health efforts worldwide. The ongoing research aims to characterize the protein’s structure-function relationships, assess its stability, and investigate its mechanisms of action, ultimately contributing to the development of effective health interventions. As the landscape of infectious diseases evolves, the D15Wsu75e protein holds promise for future therapeutic and preventative measures, highlighting the importance of continued exploration in this area of protein research.
