| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGFBP3 |
| Uniprot No | P17936 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 28-291aa |
| 氨基酸序列 | GGASSAGLGP VVRCEPCDAR ALAQCAPPPA VCAELVREPG CGCCLTCALS EGQPCGIYTE RCGSGLRCQP SPDEARPLQA LLDGRGLCVN ASAVSRLRAY LLPAPPAPGN ASESEEDRSA GSVESPSVSS THRVSDPKFH PLHSKIIIIK KGHAKDSQRY KVDYESQSTD TQNFSSESKR ETEYGPCRRE MEDTLNHLKF LNVLSPRGVH IPNCDKKGFY KKKQCRPSKG RKRGFCWCVD KYGQPLPGYT TKGKEDVHCY SMQSK |
| 预测分子量 | 29 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IGFBP3重组蛋白的3篇代表性文献概览(格式简化，非完整引用)：
1. **文献名称**：*"Crystal structure of recombinant human insulin-like growth factor-binding protein 3"*
**作者**：Kirstein MN, et al.
**摘要**：解析了重组人IGFBP3的晶体结构，揭示其与IGF-1结合的结构域及可能的生物学功能调控机制。
2. **文献名称**：*"Recombinant human insulin-like growth factor-binding protein-3 inhibits growth of human epidermoid carcinoma cells in vitro"*
**作者**：Oh Y, et al.
**摘要**：研究发现重组IGFBP3通过阻断IGF信号通路，抑制表皮癌细胞增殖，提示其潜在抗肿瘤应用价值。
3. **文献名称**：*"Recombinant IGFBP-3 sensitizes cancer cells to chemotherapeutic agents by IGF-independent mechanisms"*
**作者**：Lee HY, et al.
**摘要**：证明重组IGFBP3通过非依赖IGF的途径(如激活凋亡通路)增强癌细胞对化疗药物的敏感性。
4. **文献名称**：*"Production and characterization of recombinant human IGFBP-3 in mammalian cells"*
**作者**：Baxter RC.
**摘要**：描述哺乳动物细胞表达系统生产重组IGFBP3的工艺优化及其生物学活性验证，为临床级生产奠定基础。
(注：以上为示例性内容，实际文献请通过PubMed/Google Scholar等平台检索验证。)
**Background of Recombinant IGFBP3 Protein**
Insulin-like Growth Factor Binding Protein 3 (IGFBP3) is a key component of the insulin-like growth factor (IGF) system, which regulates cellular growth, metabolism, and survival. As the most abundant IGF-binding protein in circulation, IGFBP3 modulates the bioavailability and activity of IGF-1 and IGF-2 by forming ternary complexes with them and the acid-labile subunit (ALS), prolonging their half-life and controlling their interaction with cell surface receptors. Beyond its IGF-dependent roles, IGFBP3 exhibits IGF-independent functions, including direct effects on apoptosis, cell adhesion, and transcriptional regulation, often mediated through interactions with nuclear receptors or cell membrane proteins.
Structurally, IGFBP3 contains conserved N- and C-terminal domains critical for IGF binding, alongside a central linker region susceptible to proteolytic cleavage, which fine-tunes its bioactivity. Post-translational modifications, such as phosphorylation and glycosylation, further influence its stability and function.
Recombinant IGFBP3 protein, produced via molecular cloning in systems like *E. coli*, mammalian cells, or yeast, offers a standardized tool for studying IGFBP3's mechanisms and therapeutic potential. Its applications span *in vitro* and *in vivo* research, particularly in cancer, where IGFBP3’s dual role as a tumor suppressor or promoter (context-dependent) is under investigation. In metabolic disorders, recombinant IGFBP3 helps dissect IGF-axis dysregulation linked to diabetes or obesity. Clinically, it is explored as a biomarker for diseases like acromegaly or as a therapeutic agent to inhibit IGF-driven tumor growth. Emerging studies also highlight its utility in drug delivery, leveraging its ability to bind small molecules or target specific tissues.
Overall, recombinant IGFBP3 serves as a vital reagent for unraveling the IGF system's complexity and advancing translational research across diverse pathologies.
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