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 >  Protein>VP0 (Coxsackievirus A16) >VP0-C52H3

Coxsackievirus A16 (strain G-10) VP0 Protein, His Tag

表达区间及表达系统(Source)

Coxsackievirus A16 (strain G-10) VP0 Protein, His Tag (VP0-C52H3) is expressed from human 293 cells (HEK293). It contains AA Gly 2 - Gln 323 (Accession # Q65900-1).

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蛋白结构(Molecular Characterization)

VP0 (Coxsackievirus A16) Structure

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 37.6 kDa. The protein migrates as 40-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>90% as determined by SDS-PAGE.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.
 

电泳(SDS-PAGE)

VP0 (Coxsackievirus A16) SDS-PAGE

Coxsackievirus A16 (strain G-10) VP0 Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

 

背景(Background)

Cox A16 infection is very common in China, and the pathogenicity of Cox A16 is significantly different from enterovirus 71. Cox A16 can induce the production of a variety of micribonucleic acid, which affects the conduction of inflammatory signaling pathway, leading to the occurrence of pathological damage. Cox A16 capsid protein VP1, as an important target protein, interacts with host cell receptors to provide virion attachment to target host cells.

 

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