- ￥1868
- abinScience
- France
- HS925011
- 2026年03月03日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.
- 保质期：
1 year
- 英文名：
Recombinant Human RAGE/AGER Protein, C-Fc
- 库存：
999
- 供应商：
abinScience
- 规格：
100ug
| Product name | Recombinant Human RAGE/AGER Protein, C-Fc |
|---|---|
| Catalog No. | HS925011 |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. |
| Purity | >95% as determined by SDS-PAGE. |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Endotoxin level | Please contact with the lab for this information. |
| Expression system | Mammalian Cells |
| Accession | Q15109 |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Alternative Names | Advanced glycosylation end product-specific receptor, Receptor for advanced glycosylation end products, AGER, RAGE |
| Species | Homo sapiens (Human) |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
abinScience, founded in 2023 in Strasbourg, France, is committed to developing and producing high-quality life science reagents. Rooted in one of Europe’s leading hubs for scientific innovation, abinScience empowers global research through reliable, efficient experimental solutions. Guided by the vision of “Empowering Bioscience Discovery,” we support scientists worldwide in advancing the frontiers of bioscience.
Technology and Innovation
Relying on the global leading position in antibody and protein research and more than 20 years of industry experience of its parent company ProteoGenix since 2003...
Product categories and application fields.
Main products...
Application field: Infectious disease research, Neuroscience, Immunology, Oncology
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文献和实验• Comparison of glucose degradation product and receptor levels in diabetic and normal pregnancy., PMID:32517435
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
Assessing Fc Glycan Heterogeneity of Therapeutic Recombinant Monoclonal Antibodies Using NP-HPLC
Recombinant monoclonal antibodies (rMAbs) are becoming major human therapeutics to treat life-threatening diseases such as cancer. These rMAbs are produced using either in vitro cell culture processes or transgenic technology in animals
human E-cadherin-IgG Fc domain fusion protein (E-cad-Fc) has recently been shown to be extremely efficient in facilitating the culture of human embryonic stem (ES) cells and induced pluripotent stem (iPS) cells under completely defined conditions
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