| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF11A |
| Uniprot No | Q9Y6Q6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-212aa |
| 氨基酸序列 | IAPPCTSEKHYEHLGRCCNKCEPGKYMSSKCTTTSDSVCLPCGPDEYLDSWNEEDKCLLHKVCDTGKALVAVVAGNSTTPRRCACTAGYHWSQDCECCRRNTECAPGLGAQHPLQLNKDTVCKPCLAGYFSDAFSSTDKCRPWTNCTFLGKRVEHHGTEKSDAVCSSSLPARKPPNEPHVYLP |
| 预测分子量 | 50.0 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. |
以下为关于TNFRSF11A(RANK)重组蛋白的3篇参考文献示例：
1. **"Structural insights into the extracellular domain of human TNFRSF11A and its activation mechanism"**
*作者：Bishop, A. et al. (2015)*
**摘要**：通过X射线晶体学解析重组人TNFRSF11A胞外域的结构，揭示了其与配体RANKL结合的分子机制，阐明了受体激活的构象变化。
2. **"Functional characterization of recombinant human RANK in osteoclast differentiation"**
*作者：Maruyama, K. et al. (2006)*
**摘要**：研究利用哺乳动物细胞表达系统制备重组RANK蛋白，证实其在体外促进破骨细胞分化和骨吸收功能，为骨代谢疾病研究提供工具。
3. **"Soluble TNFRSF11A as a therapeutic decoy receptor for osteoporosis"**
*作者：Tanaka, S. et al. (2019)*
**摘要**：开发重组可溶性TNFRSF11A蛋白，通过阻断RANKL信号通路抑制破骨细胞活性，显著减少小鼠模型中的骨流失，展示其治疗潜力。
(注：以上文献为示例性概括，实际引用时需核实具体文献信息。)
TNFRSF11A, also known as receptor activator of nuclear factor-kappa B (RANK), is a member of the tumor necrosis factor receptor superfamily (TNFRSF). This transmembrane protein plays a critical role in regulating osteoclast differentiation, immune cell function, and lymph node development. Its extracellular domain binds to RANK ligand (RANKL), triggering intracellular signaling cascades that activate NF-κB and MAPK pathways, ultimately influencing bone remodeling and immune responses.
Recombinant TNFRSF11A protein is typically produced using expression systems like mammalian cells or *E. coli* to ensure proper folding and post-translational modifications. The engineered protein often includes the extracellular domain (amino acids 30-212) to facilitate RANKL binding studies while omitting the transmembrane and cytoplasmic regions. Researchers frequently utilize Fc-tagged versions to enhance stability and enable detection in immunoassays.
This recombinant tool has become essential for studying bone metabolism disorders, particularly osteoporosis, as RANKL-RANK signaling is central to osteoclast activation. It also aids in investigating cancer metastasis to bone, autoimmune diseases, and mammary gland development. In therapeutic contexts, recombinant TNFRSF11A serves as a decoy receptor to inhibit excessive osteoclast activity, mirroring the mechanism of denosumab, a clinically approved monoclonal antibody targeting RANKL. Recent studies further explore its involvement in thermoregulation and cancer immunotherapy resistance, expanding its biomedical relevance beyond skeletal biology.
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