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- AntibodySystem
- France
- YVV14701
- 2025年07月09日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
- 保质期：
1 year
- 英文名：
Recombinant BVDV Glycoprotein E2 Protein, N-His
- 库存：
999
- 供应商：
AntibodySystem
- 规格：
100ug
| 状态 | Liquid |
| 保存溶液 | 0.01M PBS, pH 7.4. |
| 纯度 | >90% as determined by SDS-PAGE. |
| 应用 | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| 内毒素水平 | Please contact with the lab for this information. |
| 表达系统 | E. coli |
| Accession号 | P19711 |
| 蛋白长度 | His693-Ser851 |
| 性质 | Recombinant |
| 预测分子量 | 20.34 kDa |
| 稳定性和存储 | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| 重悬 | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| 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 |
| 种属 | Bovine viral diarrhea virus (isolate NADL) (BVDV) (Mucosal disease virus) |
| 运输 | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 备注 | For research use only. |
Currently, AntibodySystem's product lines cover multiple research areas, including 48 types of viruses and superbugs, parasites, tumors, Alzheimer's disease, Parkinson's disease, hypersensitivity and allergic reactions, immune suppression, and immune activation.
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文献和实验Monitoring Recombinant Glycoprotein Heterogeneity
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
N-Linked Protein Glycosylation in a Bacterial System
and permethylation followed by mass spectrometry. We also describe the expression and immunodetection of the model N -glycoprotein, AcrA, fused to a hexa-histidine tag to follow protein glycosylation in C. jejuni . This chapter concludes with the recent demonstration
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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