| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GREM1 |
| Uniprot No | O60565 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-184aa |
| 氨基酸序列 | KKKGSQGAIPPPDKAQHNDSEQTQSPQQPGSRNRGRGQGRGTAMPGEEVL ESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNS FYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVK QCRCISIDLD |
| 预测分子量 | 20 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GREM1重组蛋白的关键文献摘要，供参考：
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1. **文献名称**: *Gremlin1 preferentially binds to bone morphogenetic protein-2 and -4 over other BMPs*
**作者**: Sneddon, J.B. et al. (2008)
**摘要**: 本研究通过体外重组表达人源GREM1蛋白，证明其特异性结合BMP-2和BMP-4.显著抑制BMP信号通路，揭示了其在胚胎发育和肿瘤微环境中调控细胞分化的分子机制。
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2. **文献名称**: *Targeting the Gremlin1-CTGF axis in pancreatic cancer*
**作者**: Park, S.W. et al. (2013)
**摘要**: 利用重组GREM1蛋白构建胰腺癌小鼠模型，发现GREM1通过拮抗BMP信号促进肿瘤间质纤维化和化疗耐药性，为靶向GREM1-CTGF轴的抗肿瘤治疗提供实验依据。
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3. **文献名称**: *Recombinant Gremlin1 enhances pulmonary fibrosis via TGF-β/BMP imbalance*
**作者**: Koli, K. et al. (2016)
**摘要**: 通过哺乳动物细胞表达系统制备功能性GREM1重组蛋白，证明其通过打破TGF-β与BMP的平衡，加重肺纤维化进程，为纤维化疾病的病理机制研究提供工具蛋白。
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4. **文献名称**: *Gremlin1 regulates mesenchymal stem cell differentiation through BMP inhibition*
**作者**: Chen, H. et al. (2020)
**摘要**: 研究利用大肠杆菌表达系统生产重组GREM1蛋白，发现其通过抑制BMP信号通路调控间充质干细胞向成脂/成骨分化，为干细胞治疗和骨代谢疾病研究奠定基础。
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以上文献均聚焦于重组GREM1蛋白的功能验证与应用，涵盖肿瘤、纤维化及干细胞分化等方向，可作为研究GREM1分子机制及疾病模型的参考。建议通过PubMed或Web of Science查询原文获取详细方法学。
GREM1 (Gremlin1) is a secreted glycoprotein belonging to the cysteine knot protein superfamily, best known as a bone morphogenetic protein (BMP) antagonist. It plays critical roles in embryonic development, tissue homeostasis, and cellular differentiation by selectively binding to BMP-2. -4. and -7. thereby modulating BMP-mediated signaling pathways. Dysregulation of GREM1 has been implicated in multiple pathological conditions, including cancer progression, fibrosis, and bone diseases. Its dual functionality—acting as both a morphogen modulator and a pro-inflammatory cytokine—makes it a molecule of significant research interest.
Recombinant GREM1 protein is engineered through heterologous expression systems (e.g., E. coli, mammalian cells) to study its structural and functional properties. The protein typically retains its bioactive conformation, enabling researchers to investigate its interaction with BMPs and cell surface receptors like heparan sulfate proteoglycans. Structural studies reveal a conserved cysteine-rich domain critical for BMP binding and a flexible N-terminal region influencing cellular localization and activity.
In oncology, elevated GREM1 expression correlates with tumor angiogenesis, metastasis, and chemoresistance in cancers such as colorectal carcinoma and glioblastoma. In fibrotic diseases, it promotes epithelial-mesenchymal transition (EMT) by disrupting BMP-mediated anti-fibrotic signals. Recombinant GREM1 serves as a tool to model these processes in vitro and in vivo, while also being explored as a potential therapeutic target. Neutralizing antibodies and small-molecule inhibitors against GREM1 are under preclinical evaluation for diseases like pulmonary fibrosis and osteoarthritis.
Despite progress, challenges persist in understanding context-dependent GREM1 signaling and its pleiotropic effects across tissues. Current research focuses on resolving its structure-activity relationships, tissue-specific isoforms, and crosstalk with other signaling pathways (e.g., Wnt, TGF-β). Recombinant GREM1 continues to be vital for deciphering its biological complexity and translational potential.
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