| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FcgBP |
| Uniprot No | Q9Y6R7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 471-690aa |
| 氨基酸序列 | VCRAQGDPHYTTFDGRRYDMMGTCSYTMVELCSEDDTLPAFSVEAKNEHRGSRRVSYVGLVTVRAYSHSVSLTRGEVGFVLVDNQRSRLPVSLSEGRLRVYQSGPRAVVELVFGLVVTYDWDCQLALSLPARFQDQVCGLCGNYNGDPADDFLTPDGALAPDAVEFASSWKLDDGDYLCEDGCQNNCPACTPGQAQHYEGDRLCGMLTKLDGPFAVCHDT |
| 预测分子量 | 31.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于FcgBP(假设为Fc gamma结合蛋白)重组蛋白的模拟参考文献示例，供参考。建议通过学术数据库(如PubMed、Google Scholar)核实最新研究：
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1. **文献名称**: *"Recombinant expression and functional characterization of FcγBP in mammalian cells"*
**作者**: Smith A, et al.
**摘要**: 本研究报道了在CHO细胞中成功表达并纯化重组FcγBP蛋白，验证了其与IgG抗体的Fc区域特异性结合能力，为免疫治疗研究提供了工具。
2. **文献名称**: *"FcγBP modulates inflammatory responses in a murine sepsis model"*
**作者**: Johnson B, et al.
**摘要**: 通过重组Fcγ蛋白阻断实验，证明其可抑制Fcγ受体介导的炎症信号通路，显著降低小鼠败血症模型的炎症损伤，提示其治疗潜力。
3. **文献名称**: *"Structural insights into FcγBP-IgG interaction by cryo-EM"*
**作者**: Chen L, et al.
**摘要**: 利用冷冻电镜解析重组FcγBP与IgG复合物的三维结构，揭示了关键结合位点，为设计靶向Fcγ通路的药物提供结构基础。
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**注**：以上文献为示例性内容，实际研究需根据具体缩写定义(如FcgBP是否指Ficolin-γ等)调整检索策略。建议结合具体研究背景进一步筛选文献。
Fc gamma-binding protein (FcγBP) is a secreted glycoprotein that interacts with the Fc region of immunoglobulin G (IgG), playing a role in immune regulation. It was first identified in mammalian biological fluids, including serum and mucosal secretions, and is structurally characterized by multiple repeating domains resembling those in von Willebrand factor. These domains enable FcγBP to form multimeric structures, enhancing its binding avidity to IgG antibodies.
Recombinant FcγBP is engineered through genetic modification, typically expressed in mammalian cell systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation, which are critical for its functional integrity. The production involves cloning the FcγBP gene into expression vectors, followed by purification using affinity chromatography.
Functionally, FcγBP modulates immune responses by competing with cellular Fc gamma receptors (FcγRs) for IgG binding. This interaction can influence antibody-dependent effector functions, including phagocytosis, complement activation, and cytokine release. Its ability to sequester IgG complexes suggests a role in maintaining immune homeostasis, potentially dampening excessive inflammation or autoimmunity.
Research applications of recombinant FcγBP include studying IgG-Fc interactions, developing therapeutic strategies for autoimmune diseases (e.g., rheumatoid arthritis), and optimizing antibody-based therapies. In biopharmaceuticals, it serves as a tool to engineer antibodies with tailored Fc-mediated activities. Further studies explore its diagnostic potential in immune-complex-related disorders.
In summary, recombinant FcγBP is a versatile molecule bridging basic immunology and translational research, offering insights into antibody regulation and therapeutic innovation.
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