| 纯度 | >97%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF17 |
| Uniprot No | Q02223 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 5-54aa |
| 氨基酸序列 | AGQCSQNEYFDSLLHACIPCQLRCSSNTPPLTCQRYCNASVTNSVKGTNA |
| 预测分子量 | 5 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. |
以下为3-4条关于TNFRSF17(BCMA)重组蛋白的模拟参考文献示例，供参考：
1. **文献名称**：*Structural and functional characterization of recombinant TNFRSF17/BCMA for therapeutic targeting*
**作者**：Smith A, et al.
**摘要**：解析了重组TNFRSF17蛋白的晶体结构，探讨其与配体APRIL/BAFF的结合机制，为多发性骨髓瘤靶向药物设计提供依据。
2. **文献名称**：*Production and immunogenicity evaluation of soluble BCMA-Fc fusion protein in myeloma models*
**作者**：Lee JH, et al.
**摘要**：报道了重组BCMA-Fc融合蛋白的哺乳动物细胞表达系统构建，验证其在小鼠模型中阻断肿瘤生长及增强T细胞活性的作用。
3. **文献名称**：*BCMA-specific CAR-T cell activation relies on recombinant BCMA extracellular domain protein screening*
**作者**：Zhang Q, et al.
**摘要**：利用重组TNFRSF17胞外域蛋白筛选高亲和力抗体，优化CAR-T细胞疗法，显著提升对多发性骨髓瘤细胞的杀伤效果。
4. **文献名称**：*Recombinant BCMA as a serum biomarker for monitoring minimal residual disease in multiple myeloma*
**作者**：Garcia M, et al.
**摘要**：开发基于重组BCMA蛋白的ELISA检测法，证实其在患者血清中的定量检测价值，与疾病进展呈正相关。
**注**：以上文献为示例，实际引用请通过PubMed或专业数据库(如Nature、Blood期刊)检索最新研究。
**Background of TNFRSF17 Recombinant Protein**
TNFRSF17. also known as B-cell maturation antigen (BCMA), is a member of the tumor necrosis factor receptor superfamily (TNFRSF). This transmembrane protein is primarily expressed on the surface of mature B lymphocytes and plasma cells, playing a critical role in B-cell development, survival, and immune regulation. Structurally, TNFRSF17 contains a cysteine-rich extracellular domain that binds to its ligands, APRIL (a proliferation-inducing ligand) and BAFF (B-cell activating factor), facilitating downstream signaling pathways such as NF-κB and MAPK, which are essential for B-cell homeostasis.
Dysregulation of TNFRSF17 is closely associated with hematologic malignancies, particularly multiple myeloma, where its overexpression promotes tumor cell proliferation and evasion of apoptosis. This has positioned TNFRSF17 as a key therapeutic target. Recombinant TNFRSF17 protein is engineered to mimic the extracellular domain of the native receptor, often produced in mammalian or insect expression systems to ensure proper post-translational modifications. It is typically fused with tags (e.g., Fc or His tags) for enhanced stability and purification efficiency.
In research, TNFRSF17 recombinant protein is widely used to study ligand-receptor interactions, screen therapeutic antibodies, and validate drug candidates. It also serves as a critical tool in developing CAR-T cell therapies and bispecific antibodies targeting BCMA for treating multiple myeloma. Additionally, soluble TNFRSF17 variants are explored as decoy receptors to neutralize excess APRIL/BAFF in autoimmune diseases. Its versatility in both basic and applied research underscores its significance in advancing immunology and oncology therapeutics.
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