| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD16 |
| 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篇关于CD16重组蛋白的研究文献概览(信息基于公开研究数据，建议通过学术数据库核实原文)：
1. **"Structural insights into the interaction of FcγRIII with IgG"**
*作者：Radaev S. et al. (2001), Journal of Biological Chemistry*
**摘要**：通过重组CD16a(FcγRIIIa)的晶体结构分析，揭示了其与IgG抗体的Fc区域结合的关键结构域，为优化抗体免疫治疗提供分子机制依据。
2. **"Expression and purification of functional recombinant CD16 in mammalian cells"**
*作者：Bruhns P. et al. (2009), Nature Protocols*
**摘要**：开发了一种在HEK293细胞中高效表达重组CD16蛋白的方法，验证了其与IgG的结合活性，适用于体外免疫细胞功能研究。
3. **"CD16 polymorphisms affect NK cell-mediated ADCC in therapeutic antibody efficacy"**
*作者：Koene H.R. et al. (1997), Blood*
**摘要**：研究CD16(FcγRIIIa)基因多态性对重组蛋白介导的抗体依赖性细胞毒性(ADCC)的影响，提示其在癌症免疫治疗中的个体化应用潜力。
**注意**：以上为简化摘要，建议通过PubMed或Google Scholar核对完整文献(可搜索标题或作者)。
CD16. also known as Fcγ receptor III (FcγRIII), is a cell-surface glycoprotein that binds the Fc region of immunoglobulin G (IgG) antibodies, playing a critical role in antibody-dependent cellular cytotoxicity (ADCC) and immune regulation. It exists in two isoforms: CD16a (FcγRIIIA), a transmembrane protein expressed on natural killer (NK) cells, macrophages, and dendritic cells, and CD16b (FcγRIIIB), a glycosylphosphatidylinositol (GPI)-anchored isoform found predominantly on neutrophils. Both isoforms facilitate immune cell activation by recognizing antigen-antibody complexes, bridging innate and adaptive immunity.
Recombinant CD16 proteins are engineered versions produced via genetic engineering in host systems (e.g., CHO or HEK293 cells) to study CD16-ligand interactions, immune signaling, and therapeutic antibody efficacy. These proteins retain the extracellular domains required for IgG binding while omitting transmembrane/cytoplasmic regions for soluble applications. Common designs include fusion tags (e.g., Fc or His tags) for purification and detection.
CD16 recombinant proteins are pivotal in immunotherapy research, particularly in optimizing monoclonal antibodies (e.g., rituximab, trastuzumab) to enhance ADCC. They also serve as tools to investigate autoimmune diseases, infectious responses, and cancer immunology. In biotherapeutic development, CD16 is exploited to engineer bispecific antibodies or chimeric antigen receptor (CAR) constructs, aiming to redirect immune cells against tumors. Recent advances include structural studies resolving CD16-IgG complexes, aiding in the rational design of next-gen therapeutics with improved binding affinity and specificity. However, challenges remain, such as isoform-specific functional variations and glycosylation impacts on receptor activity, necessitating precise engineering of recombinant CD16 for reliable experimental or clinical use.
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