Analytical Data
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基因名
vlpF
- Application
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别名
vlpF;Variant surface antigen F
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种属
Mycoplasma
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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
Q49538
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表达区间
30-67aa
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氨基酸序列
CGQTNTDQSQQPGSGSGSGSGTSNGSGSTPTPEQGNNQ
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分子量
18.9 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
VlpF, a vital recombinant protein, has garnered significant attention in the fields of microbiology and biotechnology due to its role in various biological processes. This protein is primarily associated with the pathogenic mechanisms of certain bacteria, particularly in the context of virulence and immune evasion. Researchers have been focused on characterizing VlpF to better understand its structure, function, and potential applications. The interest in VlpF is driven by its unique properties that allow it to interact with host immune systems, providing insights into bacterial survival strategies. Furthermore, the recombinant expression of VlpF opens avenues for developing novel vaccines or therapeutic agents that could aid in combating bacterial infections. Enhanced production techniques, along with advanced molecular biology tools, have improved the yield and functionality of VlpF, making it possible to conduct extensive studies on its biochemical properties and functional implications in host-pathogen interactions. Understanding VlpF's mechanisms could also pave the way for innovative strategies in disease prevention and treatment, thereby addressing the growing challenge of antibiotic resistance. Overall, the research surrounding VlpF not only contributes to fundamental biological knowledge but also holds promise for practical applications in medicine and public health.












