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- 文献和实验
- 技术资料
- 保存条件:
-20℃
- 保质期:
12 months
- 英文名:
Recombinant BVDV Glycoprotein E2 Protein, C-His
- 供应商:
武汉益普生物科技有限公司
- 规格:
50μg/100μg/1mg
| 规格: | 50μg | 产品价格: | ¥1788.0 |
|---|---|---|---|
| 规格: | 100μg | 产品价格: | ¥2868.0 |
| 规格: | 1mg | 产品价格: | ¥17268.0 |
| 产品名称 | Recombinant BVDV Glycoprotein E2 Protein, C-His |
| 货号 | VK778011 |
| 描述 | Recombinant BVDV Glycoprotein E2 Protein, C-His ( VK778011 ) expressed in Mammalian Cells , spanning His693-Asp1030 . Purity: >90% by SDS-PAGE. Highlights His-Tagged — N-terminal 6×His tag for IMAC purification. Mammalian Expression — Proper folding and native glycosylation. High Purity — >90% purity verified by SDS-PAGE. |
| 应用实验 | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| 宿主/表达体系 | Mammalian Cells |
| 基因号 | P19711 |
| 状态 | Lyophilized |
| 蛋白质长度 | His693-Asp1030 |
| 分子量 | 41.38 kDa |
| 纯度 | >90% as determined by SDS-PAGE. |
| 储存温度 | -20℃ |
| 别名 | Genome polyprotein, N-terminal protease, N-pro, 3.4.22.-, Autoprotease p20, Capsid protein C, E(rns) glycoprotein, gp44/48, Envelope glycoprotein E1, gp33, Envelope glycoprotein E2, gp55, Viroporin p7, Non-structural protein 2-3, Cysteine protease NS2, 3.4.22.-, Non-structural protein 2, Serine protease NS3, 3.4.21.113, 3.6.1.15, 3.6.4.13, Non-structural protein 3, Non-structural protein 4A, NS4A, Non-structural protein 4B, NS4B, Non-structural protein 5A, NS5A, RNA-directed RNA polymerase, 2.7.7.48, NS5B |

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recombinant protein in vivo (1 ). Glycosylation is the most extensive source of protein heterogeneity, and many recent developments in analytical biotechnology have enhanced the ability to monitor and structurally define changes in oligosaccharides associated
Expression of Recombinant Cytochromes c in E. coli
for proper folding and stability. However, significant advances in expression of recombinant cytochromes c have been made during the last decade. It has been shown that a single gene cluster, ccmA–H , is responsible for cytochrome c maturation in Escherichia
Analysis of Laminin Structure and Function with Recombinant Glycoprotein Expressed in Insect Cells
Recent developments in the application of eukaryotic recombinant protein techniques have provided new tools with which to dissect and map functional activities in basement membrane glycoproteins. This has been particularly valuable
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