| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Fcgr3 |
| Uniprot No | P08508 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-215aa |
| 氨基酸序列 | ALPKAVVKLDPPWIQVLKEDMVTLMCEGTHNPGNSSTQWFHNGRSIRSQVQASYTFKATVNDSGEYRCQMEQTRLSDPVDLGVISDWLLLQTPQRVFLEGETITLRCHSWRNKLLNRISFFHNEKSVRYHHYKSNFSIPKANHSHSGDYYCKGSLGSTQHQSKPVTITVQDPATTSSISLVWYHT |
| 预测分子量 | 37.2 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Fcgr3重组蛋白的3篇代表性文献示例(注：文献信息为模拟示例，实际引用需核实)：
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1. **文献名称**: "Expression and functional characterization of recombinant human FcγRIII in NK cells"
**作者**: Smith A, et al.
**摘要**: 研究通过哺乳动物表达系统成功重组表达人源FcγRIII蛋白，并验证其在自然杀伤细胞(NK细胞)中的功能。结果表明，重组FcγRIII可增强抗体依赖性细胞毒性(ADCC)，为癌症免疫治疗提供实验依据。
2. **文献名称**: "Structural insights into Fcgr3 receptor-antibody interactions using recombinant protein mutants"
**作者**: Lee J, et al.
**摘要**: 通过重组Fcgr3蛋白的定点突变和晶体结构分析，揭示了FcγRIII与IgG抗体的结合机制，发现特定氨基酸残基对亲和力调节的关键作用，为设计优化抗体药物提供结构基础。
3. **文献名称**: "Recombinant Fcgr3 as a biomarker for autoimmune disease progression"
**作者**: Chen L, et al.
**摘要**: 开发了基于重组Fcgr3蛋白的血清检测方法，发现其在系统性红斑狼疮(SLE)患者中的异常表达水平与疾病活动度显著相关，提示其作为临床生物标志物的潜力。
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**说明**：以上文献为示例性质，实际研究中需通过PubMed或Web of Science等平台检索具体文献(关键词：Fcgr3 recombinant protein、FcγRIII expression)。建议关注领域内权威期刊如*Journal of Immunology*或*Nature Biotechnology*。
FcγRIII (Fc gamma receptor III), also known as CD16. is a cell-surface glycoprotein belonging to the immunoglobulin superfamily. It plays a critical role in immune responses by binding the Fc region of IgG antibodies, facilitating antibody-dependent cellular cytotoxicity (ADCC), phagocytosis, and cytokine release. Two isoforms exist in humans: FcγRIIIa (CD16a), expressed on natural killer (NK) cells and macrophages, and FcγRIIIb (CD16b), a glycosylphosphatidylinositol (GPI)-anchored protein found on neutrophils. Dysregulation of FcγRIII signaling is linked to autoimmune diseases, infections, and cancer progression.
Recombinant FcγRIII proteins are engineered versions produced via expression systems like mammalian cells (e.g., HEK293 or CHO) or insect cells to ensure proper glycosylation and functionality. These proteins typically include the extracellular domain (ECD) responsible for IgG binding. Researchers use them to study receptor-ligand interactions, screen therapeutic antibodies, or develop biologics that modulate immune activity. For instance, FcγRIIIa is a target for cancer immunotherapies aiming to enhance NK cell-mediated tumor cell killing. Conversely, blocking FcγRIII may mitigate inflammation in autoimmune disorders.
In drug development, recombinant FcγRIII proteins serve as tools for characterizing monoclonal antibodies' Fc-mediated effector functions. They help optimize antibody engineering strategies, such as glycoengineering or Fc mutagenesis, to fine-tune ADCC potency. Recent applications include bispecific antibodies and checkpoint inhibitors designed to engage FcγRIII for improved therapeutic efficacy. Overall, recombinant FcγRIII proteins are indispensable for advancing both basic immunology research and clinical therapies targeting immune regulation.
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