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100ul
| 产品编号 | bs-0362P-Cy3 |
| 英文名称 | Recombinant protein A, Cy3 conjugated |
| 中文名称 | Cy3标记蛋白A |
| 英文别名 | reProtein A/Cy3; Recombinant Protein A/Cy3; |
| 性状 | Liquid |
| 浓度 | >1.0 mg/ml |
| 储存液 | 10 mM TBS (pH=7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. |
| 研究领域 | Tags & Cell Markers > Fusion / Marker Proteins > Protein A |
| 亚细胞定位 | Secreted; cell wall. |
| 保存条件 | Stored at -20℃ for one year. |
| 注意事项 | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| 背景资料 | Protein A is a 40-60 kDa surface protein originally found in the cell wall of the bacteria Staphylococcus aureus (SPA). SPA binds proteins from many of mammalian species, most notably IgGs, and helps inhibit phagocytic engulfment and acts as an immunological disguise via this type of interaction, thus the bacteria will disrupts opsonization and phagocytosis. SPA is known to bind with Fc region of immunoglobulins preferentially through interaction with the VH3 variable region of the heavy chain. SPA has been shown to bind with high affinity to human IgG1 and IgG2 as well as mouse IgG2a and IgG2b, whereas bind with moderate affinity to human IgM, IgA and IgE as well as mouse IgG3 and IgG1. SPA is often produced in E. coli and is practically coupled to other molecules such as enzymes, biotin, radioactive iodine for use in immunology and other biological research. SPA is also immobilized onto solid supports such as agarose beads for total IgG purifying or interest protein or protein complex identifying in immunoprecipitation studies. |
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文献和实验Detecting Low‐Affinity Extracellular Protein Interactions Using Protein Microarrays
are produced as soluble recombinant proteins by transiently transfecting a mammalian cell line. The proteins are purified using an oligo‐His tag using a bespoke purification apparatus (the “Protein Press”) and subsequently printed onto glass slides
between crystals of protein?nucleic acid complexes and those containing protein alone is a common problem in structural studies of protein?nucleic acid interactions. Currently, there are several methods available for detecting nucleic acid in crystals, including
2D-DIGE: Comparative Proteomics of Cellular Signalling Pathways
resolutive 2-D electrophoresis allows the separation of heterogeneous protein samples on the basis of isoelectric point (p I ), molecular mass (M r), solubility, and relative abundance ((1) J Biol Chem 250: 4007–4021, 1975; (2) Electrophoresis 14: 1067–1073
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