| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF13C |
| Uniprot No | Q96RJ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-76aa |
| 氨基酸序列 | MRRGPRSLRG RDAPAPTPCV PAECFDLLVR HCVACGLLRT PRPKPAGASS PAPRTALQPQ ESVGAGAGEA ALPLPG |
| 预测分子量 | 7.8 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TNFRSF13C(BAFF-R)重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：**"BAFF-R, a newly identified TNF receptor that specifically interacts with BAFF"**
**作者**：Thompson, J.S., et al.
**摘要**：该研究首次鉴定了BAFF-R(TNFRSF13C)作为BAFF的专一受体，通过重组蛋白技术证实其在B细胞存活信号传导中的作用，并解析了其与BAFF结合的分子机制。
2. **文献名称**：**"Crystal structure of recombinant human BAFF-R bound to BAFF"**
**作者**：Xiao, Y., et al.
**摘要**：通过X射线晶体学解析了重组人源BAFF-R蛋白与BAFF的复合物结构，揭示了受体-配体特异性结合的关键氨基酸残基，为靶向药物设计提供了结构基础。
3. **文献名称**：**"Soluble recombinant TNFRSF13C suppresses autoimmune responses by neutralizing BAFF in murine models"**
**作者**：Zhang, Z., et al.
**摘要**：研究利用重组可溶性TNFRSF13C蛋白在小鼠模型中中和BAFF，显著抑制自身免疫反应，证明其在治疗BAFF依赖性自身免疫疾病中的潜在应用价值。
4. **文献名称**：**"Recombinant TNF receptor superfamily 13C (TNFRSF13C) enhances B cell maturation and antibody production in vitro"**
**作者**：Li, H., et al.
**摘要**：通过体外实验证明，重组TNFRSF13C蛋白能够促进B细胞成熟并增强抗体分泌，为疫苗佐剂或免疫缺陷疾病的治疗提供了新思路。
(注：以上文献信息为示例，实际引用需根据具体论文调整。)
TNFRSF13C, also known as BAFF receptor (BR3) or CD268. is a member of the tumor necrosis factor receptor superfamily (TNFRSF). It plays a critical role in B-cell development, survival, and immune regulation by binding to its ligand BAFF (B-cell activating factor, BLyS). This interaction activates downstream signaling pathways, including NF-κB and MAPK, which are essential for maintaining B-cell homeostasis. Dysregulation of the BAFF-BR3 axis is implicated in autoimmune diseases like systemic lupus erythematosus (SLE) and rheumatoid arthritis, where excessive BAFF promotes autoreactive B-cell survival.
Recombinant TNFRSF13C protein is engineered for research and therapeutic applications. Typically produced in mammalian expression systems (e.g., HEK293 or CHO cells), it retains the extracellular domain of BR3 to enable ligand binding while excluding transmembrane and intracellular regions. This soluble form can act as a decoy receptor, neutralizing excess BAFF to suppress pathological B-cell activity. Structurally, it often includes an Fc fusion (e.g., human IgG1 Fc) to enhance stability, prolong serum half-life, and facilitate detection in assays.
In research, recombinant TNFRSF13C is used to study BAFF-BR3 interactions, B-cell signaling mechanisms, and autoimmune disease pathogenesis. Therapeutically, it serves as a prototype for biologics targeting BAFF-driven disorders. Similar agents like belimumab (anti-BAFF monoclonal antibody) have been approved for SLE, highlighting the pathway's clinical relevance. Current studies explore its potential in combination therapies or as a biomarker for disease progression. Challenges include optimizing receptor affinity and minimizing off-target effects, but its role in modulating immune responses continues to drive interest in both basic and applied immunology.
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