Analytical Data
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基因名
X31S
- Application
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别名
X31S;
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种属
Griffithsia sp
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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
P84801
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表达区间
1-121aa
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氨基酸序列
SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDSIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY
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分子量
16.6 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
Research on the recombinant protein X31S has emerged as a significant area within the field of virology and vaccine development. X31S is derived from the X31 strain of the influenza virus and has been engineered to include specific mutations that enhance its stability and immunogenicity. This protein serves as a valuable model for studying antigenic properties and immune responses to influenza infections. The increasing prevalence of influenza outbreaks and the limited efficacy of existing vaccines underscore the need for innovative approaches in vaccine development. Researchers are particularly interested in X31S due to its potential to elicit robust immune responses while minimizing the risks associated with traditional live-attenuated or inactivated vaccines. Furthermore, the recombinant nature of X31S allows for easier production and purification, making it a practical candidate for further exploration. The ongoing investigations aim not only to elucidate the mechanisms of immune recognition and response but also to assess the effectiveness of X31S in preclinical and clinical settings as a potential vaccine candidate. Overall, the study of X31S represents a promising avenue towards enhancing influenza vaccination strategies and ultimately reducing the burden of influenza-related diseases globally.












