Analytical Data
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基因名
vlpF
- Application
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别名
(VlpF prolipoprotein)
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种属
Mycoplasma hyorhinis
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表达系统
E. coli
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标签
N- His-KSI
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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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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 is a protein of interest derived from the Vibrio cholerae bacterium, which is known for its role in the pathogenicity of cholera. Research on VlpF has gained attention due to its involvement in the bacterial adhesive mechanisms that facilitate colonization and infection in host organisms. The protein’s structure and function have been characterized to understand its contribution to biofilm formation and virulence. Moreover, VlpF shows potential as a target for novel therapeutic strategies, aiming to disrupt bacterial adhesion and biofilm integrity. The recombinant production of VlpF allows for detailed studies into its biochemical properties, interaction with host cells, and role in immune response. Understanding the molecular dynamics of VlpF is essential for developing vaccines or interventions against cholera, which remains a significant global health issue. Overall, exploring VlpF through recombinant protein technology not only enhances our comprehension of bacterial pathogenesis but also opens doors to innovative solutions for cholera prevention and treatment.
