Analytical Data
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基因名
HCVNS5B
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简介
POLG proteins play multiple roles in the viral life cycle, contributing to viral RNA packaging, budding, and particle production. It exhibits RNA-binding and RNA chaperone activities, affecting translation initiation through interactions with viral IRES and ribosomal subunits. HCVNS5B Protein, HCV is the recombinant HCVNS5B, expressed by E. coli, with tag-free.
- Application
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种属
Others
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O92972
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表达区间
P1216-S1650
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蛋白长度
Partial
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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
HCV NS5B (Hepatitis C Virus Non-structural Protein 5B) is a crucial enzyme that plays a significant role in the replication of the hepatitis C virus (HCV), making it a prime target for antiviral drug development. The NS5B protein is an RNA-dependent RNA polymerase that facilitates the replication of the viral genome, leading to the production of new viral particles. Understanding the structure and function of the NS5B protein is essential for designing effective inhibitors that can disrupt its activity and thus impede viral replication. Over the years, researchers have focused on recombinant forms of the NS5B protein to study its enzymatic properties, identify potential drug-binding sites, and evaluate the efficacy of novel antiviral compounds. Recombinant NS5B proteins generated in various expression systems can be used to conduct in vitro assays for screening inhibitors and understanding the molecular mechanisms of drug resistance. Additionally, structural studies, such as X-ray crystallography and cryo-electron microscopy, have revealed intricate details about the protein’s conformation, further aiding in the rational design of targeted therapies. As HCV continues to pose a significant public health challenge worldwide, ongoing research on NS5B and its inhibitors remains pivotal in the quest for effective treatments and potential cures for hepatitis C.












