| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD32 |
| Uniprot No | P12318 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-216aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMQAAPP KAVLKLEPPW INVLQEDSVT LTCQGARSPE SDSIQWFHNG NLIPTHTQPS YRFKANNNDS GEYTCQTGQT SLSDPVHLTV LSEWLVLQTP HLEFQEGETI MLRCHSWKDK PLVKVTFFQN GKSQKFSRLD PTFSIPQANH SHSGDYHCTG NIGYTLFSSK PVTITVQVPS MGSSSPMG |
| 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. |
以下是关于CD32(FcγRII)重组蛋白的3篇参考文献，涵盖其功能、应用及表达研究：
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1. **文献名称**：*"Human IgG Fc receptor heterogeneity: molecular aspects and clinical implications"*
**作者**：van de Winkel, J.G., Capel, P.J.
**摘要**：该综述总结了FcγRII(CD32)的分子结构、亚型及其在免疫调节中的作用，重点讨论了重组CD32蛋白在解析IgG抗体结合机制中的应用，为治疗性抗体研发提供理论基础。
2. **文献名称**：*"Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses"*
**作者**：Bruhns, P., et al.
**摘要**：本研究利用重组CD32蛋白进行体外结合实验，系统分析了不同FcγRII亚型(如CD32A、CD32B)与IgG亚类的亲和力差异，揭示了其在自身免疫疾病和抗体治疗中的潜在调控机制。
3. **文献名称**：*"Fcγ receptors as potential targets for therapeutic antibodies"*
**作者**：Bakema, J.E., van Egmond, M.
**摘要**：文章探讨了重组CD32B蛋白在肿瘤免疫治疗中的作用，通过体外实验证明其抑制性信号可调节B细胞活性，为靶向FcγR的抗体药物开发提供了新思路。
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**备注**：以上文献信息为示例性质，实际引用时建议通过PubMed或Web of Science核对完整信息。如需实验方法类文献，可进一步补充重组CD32表达纯化的具体研究。
**Background of CD32 Recombinant Protein**
CD32. also known as Fcγ receptor II (FcγRII), is a transmembrane glycoprotein belonging to the immunoglobulin superfamily. It plays a critical role in immune regulation by binding to the Fc region of IgG antibodies, facilitating processes such as phagocytosis, immune complex clearance, and modulation of antibody-dependent cellular responses. CD32 exists in multiple isoforms (CD32A, CD32B, CD32C) with distinct cellular distributions and functions. CD32A and CD32C are activating receptors expressed on myeloid cells, while CD32B, widely found on B cells and macrophages, acts as an inhibitory receptor to dampen immune activation.
Recombinant CD32 proteins are engineered in vitro using expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, functional forms of the protein for research and therapeutic applications. These proteins retain key structural domains, including extracellular IgG-binding regions, transmembrane segments, and intracellular signaling motifs, enabling studies on receptor-ligand interactions, immune signaling pathways, and drug development.
CD32’s involvement in autoimmune diseases, infections, and cancer has driven interest in its recombinant forms. For example, CD32B is a therapeutic target in autoimmune disorders due to its role in suppressing overactive immune responses, while CD32A is explored in cancer immunotherapy to enhance antibody-dependent cellular cytotoxicity (ADCC). Recombinant CD32 proteins are also used in diagnostic assays, antibody-drug conjugate validation, and mechanistic studies of immune evasion by pathogens.
Overall, CD32 recombinant proteins serve as essential tools for understanding IgG-mediated immunity and developing targeted therapies, bridging basic immunology and clinical innovation.
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