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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 Tupaia chinensis CD223/LAG3 Protein, C-Fc
- 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 Tupaia chinensis CD223/LAG3 Protein, C-Fc |
| 货号 | EWD30401 |
| 别名 | FDC, LAG3, Lymphocyte activation gene 3 protein, CD223, sLAG-3, LAG-3, |
| 表达系统 | Mammalian cells |
| Accession号 | XP_014440631.1 |
| 种属 | Tupaia chinensis (Chinese tree shrew) |
| 蛋白长度 | Ala20-Thr447 |
| 预测分子量 | 74.25 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
Protein Microarrays for Identification of Novel Extracellular Protein‐Protein Interactions
representing Cy5‐labeled IgG (red) and unlabeled Fc‐fusion bait proteins (blue) co‐captured on the protein A microbeads. (C ) Results from a test of different molar ratios of Fc‐fusion bait (CD200‐Fc) protein to IgG‐Cy5 mixed and complexed with protein
Recombinant fusion proteins incorporating experimental protein domains fused to immunoglobulin Fc regions have become widely utilized in studies of protein–ligand interactions. The advantages of these systems include an inherent increase
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