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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GDF3 |
| Uniprot No | Q9NR23 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 251-364aa |
| 氨基酸序列 | AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDE CGCG |
| 预测分子量 | 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GDF3重组蛋白的3篇参考文献示例(文献信息为示例性概括，具体内容需根据实际文献调整)：
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1. **文献名称**: "Recombinant GDF3 Protein Induces Adipogenesis in Mesenchymal Stem Cells"
**作者**: Li Y, et al.
**摘要**: 研究通过大肠杆菌表达系统制备重组GDF3蛋白，并验证其诱导间充质干细胞向脂肪细胞分化的功能，揭示GDF3在脂肪代谢调控中的潜在作用。
2. **文献名称**: "Structural Characterization and Functional Analysis of GDF3 in Early Embryonic Development"
**作者**: Wang J, et al.
**摘要**: 利用哺乳动物细胞表达纯化重组GDF3蛋白，结合晶体结构解析和斑马鱼模型实验，证明GDF3通过BMP信号通路调控胚胎发育中的细胞命运决定。
3. **文献名称**: "GDF3 as a Novel Biomarker in Osteoporosis: Production and Therapeutic Potential of Recombinant Protein"
**作者**: Kumar S, et al.
**摘要**: 开发CHO细胞表达的高纯度重组GDF3蛋白，通过体外成骨细胞实验和小鼠模型验证其促进骨形成的能力，提示其在骨质疏松症治疗中的应用前景。
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建议通过PubMed、Web of Science等数据库以“recombinant GDF3 protein”“GDF3 expression”“GDF3 functional study”为关键词进一步检索最新文献。
Growth differentiation factor 3 (GDF3), a member of the transforming growth factor-beta (TGF-β) superfamily, is a secreted signaling protein involved in embryonic development, cell differentiation, and tissue homeostasis. Initially identified through genomic studies, GDF3 shares structural homology with other TGF-β proteins but exhibits distinct functional characteristics. It is synthesized as a precursor protein that undergoes proteolytic cleavage to release a mature, biologically active dimer. GDF3 signals primarily through SMAD-dependent pathways, though its specific receptor interactions remain less defined compared to other family members like BMPs (bone morphogenetic proteins).
Research highlights GDF3's dual regulatory roles, acting as both a BMP antagonist and an activator in context-dependent manners. In mammals, it plays critical roles in early embryogenesis, particularly in maintaining the pluripotency of embryonic stem cells and regulating left-right asymmetry. Notably, GDF3 is highly expressed in human pluripotent stem cells, where it suppresses spontaneous differentiation and supports self-renewal. Its expression decreases during differentiation, suggesting a stage-specific function. In adult tissues, GDF3 shows limited expression but has been implicated in adipose tissue regulation and skeletal development.
Recombinant GDF3 protein, produced via bacterial or mammalian expression systems, enables functional studies and therapeutic exploration. Challenges in production include maintaining proper protein folding and post-translational modifications essential for bioactivity. Current applications focus on regenerative medicine, particularly in stem cell-based therapies and tissue engineering. Emerging evidence also links GDF3 to cancer progression, where it may act as either a tumor suppressor or promoter depending on cellular context. Despite advances, its precise mechanisms, receptor partnerships, and therapeutic potential require further investigation to address inconsistencies across experimental models and species-specific functional variations.
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