| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FcaR |
| Uniprot No | P24071 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-227aa |
| 氨基酸序列 | QEGDFPMPFISAKSSPVIPLDGSVKIQCQAIREAYLTQLMIIKNSTYREI GRRLKFWNETDPEFVIDHMDANKAGRYQCQYRIGHYRFRYSDTLELVVTG LYGKPFLSADRGLVLMPGENISLTCSSAHIPFDRFSLAKEGELSLPQHQS GEHPANFSLGPVDLNVSGIYRCYGWYNRSPYLWSFPSNALELVVTDSIHQ DYTTQNVDHHHHHH |
| 预测分子量 | 25 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FcαR(假设为IgA Fc受体相关重组蛋白)的参考文献示例(仅供格式参考，建议通过学术数据库核实最新文献)：
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1. **标题**：*Structural insights into IgA recognition by FcαRI (CD89) through crystallography*
**作者**：Herr AB, et al.
**摘要**：该研究通过X射线晶体学解析了重组FcαR蛋白与IgA-Fc的复合物结构，揭示了受体与配体结合的关键位点，为免疫调节药物设计提供了结构基础。
2. **标题**：*Recombinant FcαRI extracellular domain production in mammalian cells for functional studies*
**作者**：van Egmond M, et al.
**摘要**：报道了在哺乳动物细胞中高效表达可溶性重组FcαR胞外域的方法，并验证其与IgA的结合活性及在炎症反应中的功能。
3. **标题**：*Targeted drug delivery via FcαR-mediated nanoparticles*
**作者**：Leusen JHW, et al.
**摘要**：利用重组FcαR蛋白修饰纳米颗粒，实现IgA介导的靶向递送系统，展示了其在肿瘤治疗中的潜在应用。
4. **标题**：*FcαR polymorphisms and ligand binding affinity in autoimmune disorders*
**作者**：Smith P, et al.
**摘要**：通过重组FcαR突变体分析，发现特定基因多态性影响受体与IgA的结合能力，可能与自身免疫疾病易感性相关。
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**注意**：以上为示例性内容，实际文献请通过PubMed、Google Scholar等平台以关键词“FcαR recombinant protein”、“CD89 IgA receptor”检索近年发表的研究。
FcaR, or Fc alpha receptor (also known as CD89), is a transmembrane protein that plays a central role in mediating immune responses involving immunoglobulin A (IgA). As the primary receptor for IgA, FcaR is predominantly expressed on myeloid cells, including neutrophils, monocytes, and macrophages. Its interaction with IgA antibodies bridges innate and adaptive immunity by facilitating processes such as pathogen phagocytosis, cytokine release, and antigen presentation. Dysregulation of FcaR signaling has been implicated in inflammatory diseases, autoimmune disorders, and IgA-related pathologies like IgA nephropathy.
Recombinant FcaR proteins are engineered versions of this receptor, typically produced in heterologous expression systems (e.g., mammalian or insect cells) to study its structure-function relationships or develop therapeutic interventions. These recombinant constructs often include the extracellular domain of FcaR, which contains the IgA-binding region, and may be fused with tags (e.g., Fc or His-tags) for purification and detection. Researchers utilize recombinant FcaR to investigate IgA-mediated immune activation, map binding epitopes, and screen for inhibitors that block pathogenic IgA-FcaR interactions.
In therapeutic development, recombinant FcaR has become a valuable tool for designing biologics that modulate IgA-driven inflammation. For instance, soluble FcaR variants are being explored as decoy receptors to neutralize excess IgA in autoimmune conditions. Additionally, structural insights from recombinant FcaR studies aid in optimizing monoclonal antibodies targeting this receptor for cancer immunotherapy or anti-inflammatory therapies. The protein's versatility in both basic research and clinical applications continues to make it a focus of immunology and drug discovery studies.
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