| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GREM2 |
| Uniprot No | Q9H772 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22 to 168 |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSRKNRPAG AIPSPYKDGS SNNSERWQHQ IKEVLASSQE ALVVTERKYL KSDWCKTQPL RQTVSEEGCR SRTILNRFCY GQCNSFYIPR HVKKEEESFQ SCAFCKPQRV TSVLVELECP GLDPPFRLKK IQKVKQCRCM SVNLSDSDKQ |
| 预测分子量 | 19 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 GREM2 重组蛋白的 3 条虚构参考文献示例(实际文献需根据具体数据库检索)：
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1. **文献名称**: "Recombinant GREM2 Protein Inhibits BMP Signaling and Attenuates Fibrosis in a Mouse Model"
**作者**: Zhang Y, et al.
**摘要**: 本研究通过大肠杆菌表达系统纯化重组 GREM2 蛋白，验证其与骨形态发生蛋白(BMP)的结合能力。动物实验表明，重组 GREM2 显著抑制 TGF-β/BMP 信号通路，减轻小鼠肺纤维化模型的病理损伤，提示其潜在治疗纤维化疾病的价值。
2. **文献名称**: "Structural Characterization and Functional Analysis of GREM2 as a BMP Antagonist"
**作者**: Lee S, Kim JH.
**摘要**: 通过 X 射线晶体学解析重组 GREM2 蛋白的三维结构，揭示其与 BMP2/4 相互作用的特异性表位。体外实验证实，重组 GREM2 可剂量依赖性地抑制 BMP 介导的成骨分化，为靶向调控 BMP 信号提供了分子基础。
3. **文献名称**: "High-Yield Production of Bioactive GREM2 in Mammalian Cells and Its Role in Cancer Metastasis"
**作者**: Patel R, et al.
**摘要**: 利用哺乳动物 HEK293 细胞系统高效表达具有糖基化修饰的重组 GREM2 蛋白，证明其抑制 BMP 信号的能力优于原核表达产物。进一步实验发现，高浓度 GREM2 通过调控上皮-间质转化(EMT)促进乳腺癌细胞迁移，提示其在肿瘤微环境中的双重作用。
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如需真实文献，建议通过 **PubMed** 或 **Web of Science** 检索关键词 "GREM2 recombinant protein" 或结合具体研究领域筛选。
**Background of GREM2 Recombinant Protein**
GREM2 (Gremlin-2), a member of the CAN family of cysteine knot-secreted proteins, is a critical regulator of developmental and pathological processes. It functions as a bone morphogenetic protein (BMP) antagonist, binding to BMP ligands to inhibit their interaction with receptors, thereby modulating signaling pathways essential for tissue patterning, organogenesis, and homeostasis. GREM2 is structurally characterized by a conserved N-terminal propeptide domain and a C-terminal cystine-knot motif, which stabilizes its interaction with BMPs. Dysregulation of GREM2 has been implicated in diverse conditions, including fibrosis, cancer progression, and skeletal disorders, highlighting its therapeutic and diagnostic potential.
Recombinant GREM2 protein is engineered using expression systems (e.g., mammalian or bacterial cells) to produce purified, biologically active forms for research and clinical applications. The recombinant protein retains functional domains necessary for BMP binding, enabling studies on its inhibitory mechanisms and downstream effects. Its production often involves tagging (e.g., His-tag) for simplified purification and detection. Researchers utilize GREM2 recombinant protein to investigate BMP signaling dynamics, tissue repair mechanisms, and disease pathways, particularly in contexts like renal fibrosis, osteogenesis, and tumor microenvironments.
Recent studies emphasize GREM2's dual role—acting as both a BMP antagonist and a potential mediator of crosstalk with other signaling pathways (e.g., TGF-β, Wnt). This complexity underscores its value in regenerative medicine and targeted therapies. However, challenges remain in optimizing its stability and delivery *in vivo*. Overall, GREM2 recombinant protein serves as a vital tool for unraveling BMP-related biology and advancing therapeutic strategies for diseases linked to signaling pathway imbalances.
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