| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BAFFR |
| Uniprot No | Q96RJ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-71aa |
| 氨基酸序列 | RRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAGASSP APRTALQPQESVGAGAGEAA |
| 预测分子量 | 40 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条与BAFFR重组蛋白相关的参考文献示例(内容基于领域内典型研究方向概括，非真实文献)：
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1. **标题**: *"A recombinant soluble BAFFR-Fc fusion protein attenuates autoimmune pathology in murine lupus models"*
**作者**: Li, X. et al.
**摘要**: 该研究构建了BAFFR胞外段与IgG Fc的融合蛋白，通过阻断BAFF/BAFFR信号通路抑制B细胞过度活化。在狼疮小鼠模型中，该重组蛋白显著降低自身抗体水平并缓解肾脏损伤，提示其作为自身免疫疾病治疗剂的潜力。
2. **标题**: *"Structural and functional characterization of human BAFF receptor binding to BAFF using recombinant protein technology"*
**作者**: Patel, R.K. & Schneider, P.
**摘要**: 作者通过重组表达并纯化BAFFR胞外域，结合表面等离子体共振(SPR)技术分析其与BAFF蛋白的相互作用动力学。研究发现BAFFR以高亲和力结合BAFF三聚体，为靶向该通路的抑制剂设计提供了结构基础。
3. **标题**: *"Soluble BAFFR as a decoy receptor effectively inhibits B-cell proliferation in chronic lymphocytic leukemia"*
**作者**: Müller, G. et al.
**摘要**: 研究利用重组可溶性BAFFR蛋白阻断BAFF介导的B细胞存活信号，在慢性淋巴细胞白血病(CLL)模型中诱导恶性B细胞凋亡，证实其在B细胞恶性肿瘤治疗中的应用价值。
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**注**：以上文献为示例性概括，实际引用需查询PubMed、Web of Science等数据库获取真实发表信息。
**Background of BAFFR Recombinant Protein**
BAFFR (B-cell Activating Factor Receptor), also known as TNFRSF13C, is a member of the tumor necrosis factor receptor superfamily (TNFRSF). It plays a critical role in B-cell development, survival, and homeostasis by binding to its ligand BAFF (B-cell Activating Factor, or BLyS). The BAFF-BAFFR interaction is essential for the maturation of transitional B cells into functional mature B cells and for maintaining peripheral B-cell populations. Dysregulation of this signaling axis is implicated in autoimmune diseases (e.g., systemic lupus erythematosus, rheumatoid arthritis) and B-cell malignancies, making BAFFR a therapeutic target.
Recombinant BAFFR proteins are engineered to mimic the native receptor’s extracellular domain, often fused with Fc tags (e.g., human IgG Fc) or other solubility-enhancing tags to improve stability and enable detection. These proteins are typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications and ligand-binding activity.
In research, BAFFR recombinant proteins are used to study BAFF-BAFFR signaling mechanisms, screen inhibitors for therapeutic development, or neutralize excessive BAFF in vitro. They also serve as tools in diagnostic assays to measure BAFF levels in clinical samples. Therapeutically, BAFFR-Fc fusion proteins (e.g., analogs of the drug belimumab) have been explored as decoy receptors to block pathogenic BAFF signaling.
Overall, BAFFR recombinant proteins provide a versatile platform for understanding B-cell biology and advancing treatments for immune disorders and cancers linked to BAFF/BAFFR dysregulation.
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