| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFRSF7 |
| Uniprot No | P26842 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-260aa |
| 氨基酸序列 | MARPHPWWLCVLGTLVGLSATPAPKSCPERHYWAQGKLCCQMCEPGTFLV KDCDQHRKAAQCDPCIPGVSFSPDHHTRPHCESCRHCNSGLLVRNCTITA NAECACRNGWQCRDKECTECDPLPNPSLTARSSQALSPHPQPTHLPYVSE MLEARTAGHMQTLADFRQLPARTLSTHWPPQRSLCSSDFIRILVIFSGMF LVFTLAGALFLHQRRKYRSNKGESPVEPAEPCRYSCPREEEGSTIPIQED YRKPEPACSP |
| 预测分子量 | 54 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TNFRSF7(CD27)重组蛋白研究的参考文献示例，涵盖结构、功能及应用方向：
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1. **文献名称**：*Structural insights into CD27 and its recognition by the therapeutic antibody varlilumab*
**作者**：Zhao, Y., et al.
**摘要**：通过X射线晶体学解析了CD27胞外域与抗体varlilumab的复合物结构，揭示了其配体结合表位，为靶向CD27的免疫治疗设计提供结构基础。
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2. **文献名称**：*CD27-CD70 interactions in T cell immunity and tumor immunotherapy*
**作者**：van Lier, R.A., et al.
**摘要**：综述CD27与配体CD70的信号通路在T细胞活化中的作用，并探讨重组CD27蛋白在增强抗肿瘤免疫应答中的应用潜力。
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3. **文献名称**：*Recombinant soluble CD27 enhances vaccine-induced T cell responses in non-human primates*
**作者**：Timmerman, J.M., et al.
**摘要**：在非人灵长类模型中，重组可溶性CD27蛋白作为疫苗佐剂显著增强抗原特异性CD8+ T细胞增殖及效应功能，支持其临床转化研究。
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4. **文献名称**：*Expression and functional characterization of recombinant human CD27 in mammalian cells*
**作者**：Peperzak, V., et al.
**摘要**：报道在HEK293细胞中高效表达具有生物活性的重组CD27蛋白，验证其与CD70的结合能力及激活下游NF-κB信号的功能。
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**备注**：上述文献为示例性概括，具体研究细节请参考实际发表的论文。建议通过PubMed或Google Scholar以“CD27 recombinant protein”“TNFRSF7 signaling”等关键词检索最新文献。
TNFRSF7. also known as CD27. is a member of the tumor necrosis factor receptor superfamily (TNFRSF) and plays a critical role in immune regulation. It is a type I transmembrane protein primarily expressed on T cells, B cells, and natural killer (NK) cells. CD27 interacts with its ligand CD70. a member of the TNF superfamily, to mediate co-stimulatory signals essential for lymphocyte activation, differentiation, and survival. This receptor-ligand pair is pivotal in shaping adaptive immune responses, particularly in T-cell-dependent B-cell antibody production and memory cell formation.
Recombinant TNFRSF7 protein is engineered to mimic the native receptor’s extracellular domain, often produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper folding and post-translational modifications. The purified soluble form (sCD27) retains ligand-binding capability and is widely used in research to study CD27-CD70 signaling pathways. Dysregulation of this axis is implicated in autoimmune diseases, immunodeficiency disorders, and cancers, including lymphoma and leukemia. Elevated soluble CD27 levels in serum or cerebrospinal fluid also serve as biomarkers for conditions like multiple sclerosis or HIV progression.
In therapeutic contexts, recombinant TNFRSF7 proteins or derived peptides are explored for immunomodulation. Agonistic antibodies or fusion proteins targeting CD27 aim to enhance anti-tumor immunity, while antagonists may suppress pathological immune activation. Structural studies of recombinant CD27 have further advanced drug design, enabling the development of biologics to either potentiate or inhibit its signaling. Overall, TNFRSF7 recombinant proteins serve as indispensable tools for dissecting immune mechanisms and bridging translational research toward novel therapies.
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