| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD97 |
| Uniprot No | P48960-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-742aa |
| 氨基酸序列 | MGGRVFLAFCVWLTLPGAETQDSRGCARWCPQNSSCVNATACRCNPGFSS FSEIITTPTETCDDINECATPSKVSCGKFSDCWNTEGSYDCVCSPGYEPV SGAKTFKNESENTCQDVDECSSGRHQCDSSTVCFNTVGSYSCRCRPGWKP RHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDSKTSS AEVTIQNVIKLVDELMEAPGDVEALAPPVRHLIATQLLSNLEDIMRILAK SLPKGPFTYISPSNTELTLMIQERGDKNVTMGQSSARMKLNWAVAAGAED PGPAVAGILSIQNMTTLLANASLNLHSKKQAELEEIYESSIRGVQLRRLS AVNSIFLSHNNTKELNSPILFAFSHLESSDGEAGRDPPAKDVMPGPRQEL LCAFWKSDSDRGGHWATEGCQVLGSKNGSTTCQCSHLSSFAILMAHYDVE DWKLTLITRVGLALSLFCLLLCILTFLLVRPIQGSRTTIHLHLCICLFVG STIFLAGIENEGGQVGLRCRLVAGLLHYCFLAAFCWMSLEGLELYFLVVR VFQGQGLSTRWLCLIGYGVPLLIVGVSAAIYSKGYGRPRYCWLDFEQGFL WSFLGPVTFIILCNAVIFVTTVWKLTQKFSEINPDMKKLKKARALTITAI AQLFLLGCTWVFGLFIFDDRSLVLTYVFTILNCLQGAFLYLLHCLLNKKV REEYRKWACLVAGGSKYSEFTSTTSGTGHNQTRALRASESGI |
| 预测分子量 | 107 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篇关于CD97重组蛋白的参考文献摘要：
1. **《CD97 is a processed, seven-transmembrane, heterodimeric receptor associated with inflammation》**
- 作者：Hamann J, et al.
- 摘要：研究利用重组CD97蛋白揭示其作为七次跨膜异源二聚体受体的结构特征，并证明其在白细胞迁移和炎症反应中的调控作用。
2. **《CD97 promotes tumor cell proliferation and invasion through adhesion molecule interactions》**
- 作者：Wu Y, et al.
- 摘要：通过重组CD97蛋白实验，发现其通过结合整合素等黏附分子激活下游信号通路，促进多种癌症(如胃癌、胶质瘤)的增殖和转移。
3. **《Recombinant CD97/ADGRE5 ectodomain fragment inhibits angiogenesis in vitro》**
- 作者：Gray JX, et al.
- 摘要：研究构建CD97重组胞外域蛋白片段，证明其可通过竞争性结合血管内皮细胞表面配体CD55.抑制肿瘤微环境中的血管生成。
注：以上内容为文献核心结论的简化概括，实际引用需核对原文(建议通过PubMed或Web of Science检索具体文献)。
CD97 is a cell-surface glycoprotein belonging to the adhesion-class G protein-coupled receptor (GPCR) family, specifically categorized within the EGF-TM7 subgroup. It plays pivotal roles in immune regulation, inflammation, and cancer progression by mediating cell-cell interactions through its ligands, including CD55 (a complement regulatory protein). Structurally, CD97 features an extended N-terminal extracellular region containing multiple epidermal growth factor (EGF)-like domains, followed by a seven-transmembrane helix characteristic of GPCRs. Alternative splicing generates isoforms with varying numbers of EGF domains (typically 3-5), influencing ligand-binding specificity and cellular responses.
Recombinant CD97 protein is engineered to study its biological functions and therapeutic potential. It is commonly produced in mammalian expression systems (e.g., HEK293 cells) to ensure proper post-translational modifications, including glycosylation critical for receptor-ligand interactions. The recombinant form often includes truncated extracellular domains (e.g., EGF modules) fused to Fc tags (human IgG1) or His tags for purification and detection. This design preserves functional epitopes while enhancing solubility and stability for in vitro assays.
Research applications include investigating CD97-CD55 signaling in leukocyte trafficking, tumor immune evasion, and angiogenesis. Its overexpression in malignancies like glioblastoma and thyroid carcinoma correlates with metastasis, making recombinant CD97 valuable for developing diagnostic tools or inhibitory antibodies. Additionally, structural studies using recombinant protein help map binding interfaces for drug design. Challenges remain in fully recapitulating native conformational dynamics due to the receptor's complex multi-domain architecture and membrane-associated nature. Current efforts focus on optimizing recombinant variants to mirror physiological interactions while enabling high-throughput screening platforms for therapeutic discovery.
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