Analytical Data
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基因名
Viperin
- Application
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别名
Cig5; RSAD2; vig1; Radical S-Adenosyl Methionine Domain Containing 2; Viperin,Endoplasmic Reticulum-Associated,Interferon-Inducible; Cytomegalovirus-induced gene 5
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种属
Mouse
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
-
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表达区间
Met1~Trp362
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分子量
45&42kDa
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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
Viperin, an interferon-inducible protein, plays a critical role in the host's immune response against viral infections, showcasing its potential as a target for antiviral therapies. Initially identified in studies on the immune response, Viperin exhibits a broad range of antiviral activities against various RNA and DNA viruses, including influenza, hepatitis C, and dengue virus, through mechanisms such as inhibiting viral replication and promoting the activation of immune cells. The protein is known to interfere with the lipid metabolism and the assembly of viral particles, thereby limiting the virus's ability to propagate. Research into Viperin has garnered interest due to its unique structure and function, which can be leveraged to understand the immune evasion strategies of viruses and develop novel therapeutic strategies. Moreover, ongoing studies focus on understanding the post-translational modifications of Viperin, which may influence its antiviral properties and interactions. As the discovery of new viral pathogens continues, the characterization of Viperin and its recombinant protein forms may provide insights into designing effective antiviral agents and enhancing vaccine strategies, underscoring the importance of this protein in the field of virology and immunology.
