Analytical Data
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基因名
vif
- Application
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别名
SOR protein
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种属
Human immunodeficiency
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表达系统
Yeast
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标签
N- His-sumostar
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P69721
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表达区间
1-192aa
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分子量
38.5 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
Vif (Virion Infectivity Factor) is a critical accessory protein encoded by the Human Immunodeficiency Virus (HIV) that plays a vital role in viral replication and infectivity. Initially, Vif was identified as a factor that counteracts the host's antiviral defense mechanisms, particularly the APOBEC3 family of cytidine deaminases, which exert potent anti-HIV activity by inducing hypermutation in viral genomes. The research on Vif and its recombinant protein has garnered substantial interest due to its functional significance in the HIV life cycle and its potential as a target for therapeutic intervention. Investigations have demonstrated that Vif’s ability to recruit cellular cofactors is essential for its function, shedding light on the intricate interactions between viral proteins and host factors. Moreover, the development of Vif recombinant proteins has facilitated studies on viral pathogenesis, host-pathogen interactions, and the exploration of novel antiviral strategies. Understanding the structural and functional attributes of Vif is imperative for designing effective HIV treatments and vaccines, making it a focal point in HIV research. The ongoing exploration of Vif’s mechanisms and its recombinant forms continues to provide valuable insights into the complex interplay of HIV with the immune system, paving the way for innovative therapeutic approaches against HIV/AIDS.
