| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FcgR3A |
| Uniprot No | P08637 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-208aa |
| 氨基酸序列 | GMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESL ISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRW VFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKD SGSYFCRGLVGSKNVSSETVNITITQGLAVSTISSFFPPGYQHHHHHH |
| 预测分子量 | 23 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3篇与FcgR3A重组蛋白相关的文献示例(注：文献信息为模拟示例，非真实存在)：
1. **文献名称**：*Structural and functional characterization of recombinant human FcgR3A*
**作者**：Bruhns P, et al.
**摘要**：该研究通过哺乳动物表达系统成功制备重组FcgR3A蛋白，并解析其与IgG1抗体的Fc结构域结合机制，揭示了受体多态性(如V158F)对抗体结合的亲和力差异，为优化治疗性抗体设计提供依据。
2. **文献名称**：*FcgR3A polymorphism impacts monoclonal antibody therapy efficacy in cancer patients*
**作者**：Weng WK, et al.
**摘要**：通过分析FcgR3A基因多态性(V/F 158)与临床疗效的关联，发现携带高亲和力V等位基因的患者在接受利妥昔单抗治疗时，抗体依赖性细胞毒性(ADCC)增强，提示重组FcgR3A蛋白可作为体外药效评估工具。
3. **文献名称**：*Recombinant FcgR3A as a critical reagent for antibody-drug conjugate development*
**作者**：Sondermann P, et al.
**摘要**：研究利用昆虫细胞表达系统纯化功能性FcgR3A蛋白，并建立基于表面等离子体共振(SPR)的检测平台，定量评估抗体药物偶联物(ADC)与受体的结合动力学，支持ADC药物的临床前开发。
4. **文献名称**：*Engineering soluble FcgR3A variants for high-throughput screening*
**作者**：Zhao Y, et al.
**摘要**：通过基因工程改造获得可溶性FcgR3A重组蛋白，优化其稳定性与IgG结合能力，开发适用于高通量筛选的体外检测体系，用于筛选增强ADCC活性的下一代治疗性抗体。
(注：以上文献为假设性示例，实际引用需核实真实论文信息。)
FcγRIIIa (CD16a) is a low-affinity immunoglobulin G (IgG) Fc receptor primarily expressed on natural killer (NK) cells, macrophages, and monocytes. It plays a critical role in antibody-dependent cellular cytotoxicity (ADCC), a key mechanism by which immune cells recognize and eliminate antibody-coated pathogens or malignant cells. Structurally, it belongs to the Fcγ receptor family, which bridges innate and adaptive immunity by linking IgG antibodies to effector cell functions. The receptor binds the Fc region of IgG1 and IgG3 subclasses, triggering cytotoxic signaling pathways upon immune complex formation.
Recombinant FcγRIIIa proteins are engineered versions of this receptor, often produced in mammalian expression systems (e.g., CHO or HEK293 cells) to ensure proper glycosylation and functionality. These proteins typically include the extracellular domain (ECD) containing two immunoglobulin-like domains critical for IgG binding. Variants exist due to a genetic polymorphism (F158V) that significantly impacts IgG binding affinity, influencing clinical responses to therapeutic antibodies.
In research and drug development, recombinant FcγRIIIa serves as a vital tool for characterizing antibody-receptor interactions, optimizing therapeutic monoclonal antibodies (e.g., rituximab, trastuzumab), and screening compounds that modulate ADCC activity. It's also used in biophysical assays (SPR, ELISA) to quantify binding kinetics and assess biosimilarity. Clinically, FcγRIIIa polymorphisms are studied as biomarkers for predicting patient responses to antibody-based therapies. Recent applications extend to engineered NK cell therapies and bispecific antibodies designed to enhance tumor targeting through FcγRIIIa engagement.
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