- ￥1800 - 17280
- AntibodySystem
- France
- EVV08501
- 2025年12月06日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
-20℃
- 保质期：
12 months
- 英文名：
Recombinant HRSV G/Major surface glycoprotein G 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： | ￥1800.0 |
|---|---|---|---|
| 规格： | 100μg | 产品价格： | ￥2880.0 |
| 规格： | 1mg | 产品价格： | ￥17280.0 |
| 产品名 | Recombinant HRSV G/Major surface glycoprotein G Protein, C-His |
| 货号 | EVV08501 |
| 别名 | Major surface glycoprotein G, Attachment glycoprotein G, Membrane-bound glycoprotein, mG, Mature secreted glycoprotein G, Mature sG, G |
| 表达系统 | Mammalian Cells |
| Accession号 | P20895 |
| 种属 | Human respiratory syncytial virus A (strain Long) |
| 蛋白长度 | Asn66-Gln298 |
| 预测分子量 | 28.35 kDa |
| 性质 | Recombinant |
| 内毒素水平 | Please contact with the lab for this information. |
| 纯度 | >90% as determined by SDS-PAGE. |
| 应用 | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| 状态 | Lyophilized |
| 保存溶液 | Lyophilized from a solution in PBS pH 7.4, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| 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. |
| 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. |
| 说明 | For research use only. |
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文献和实验ANTIBODY BINDING TO PROTEIN A AND PROTEIN G
., Finstad, J., Williams, Jr., R. C. 1970. Phylogenetic insight into evolution of mammalian Fc fragment of g G globulin using staphylococcal protein A. J. Immunol. 104:140-147. Kronvall, G. 1973. A surface component in group A, C, and G streptococci
Combined 3C-ChIP-Cloning (6C) Assay: A Tool to Unravel Protein-Mediated Genome Architecture
to 37°C and 65°C Sonicator Spectrophotometer Thermal cycler, automated Timer Tubes, microcentrifuge, 1.5-mL Tubes, polypropylene, 14-mL (e.g., 17- x 100-mm) for use in high-speed centrifuge Tubes, polypropylene, 50-mL
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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