| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGFBP1 |
| Uniprot No | P08833 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 26-259aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHGNLYFQGGEFAPWQCAPCSAEKLALCPPVSA SCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHA LTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEE DHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGE EISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIR GDPNCQIYFNVQN |
| 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. |
1. **"Production and characterization of recombinant human insulin-like growth factor binding protein-1 (IGFBP-1)"**
*作者：Jones JI et al.*
摘要：该研究描述了通过大肠杆菌表达系统制备重组人IGFBP1蛋白的方法，验证其与IGF-1的特异性结合能力，并探讨其在调控细胞增殖中的作用。
2. **"IGFBP-1 in metabolic regulation: Insights from recombinant protein studies"**
*作者：Lee PDK et al.*
摘要：利用重组IGFBP1蛋白分析其在糖代谢和胰岛素敏感性中的功能，发现其通过调节IGF生物利用度影响肝脏葡萄糖输出，可能与糖尿病病理相关。
3. **"Structural analysis of IGFBP-1 reveals phosphorylation-dependent functional switching"**
*作者：Baxter RC et al.*
摘要：通过重组蛋白技术结合质谱分析，揭示了IGFBP1磷酸化修饰对其构象和结合IGF-1能力的影响，提出磷酸化状态决定其促生长或抑制活性的分子机制。
4. **"Recombinant IGFBP-1 inhibits tumor angiogenesis in preclinical models"**
*作者：Wang HS et al.*
摘要：研究发现重组IGFBP1通过阻断IGF-1介导的内皮细胞迁移和血管生成，显著抑制小鼠肿瘤模型中的血管形成，提示其潜在抗肿瘤治疗价值。
Insulin-like growth factor-binding protein 1 (IGFBP1) is a member of the IGFBP family, which modulates the bioavailability and activity of insulin-like growth factors (IGFs), particularly IGF-1 and IGF-2. These growth factors play critical roles in cellular proliferation, differentiation, and metabolism. IGFBP1. primarily produced by the liver and decidualized endometrial cells, binds IGFs with high affinity, sequestering them from receptor interaction and thereby inhibiting their pro-growth effects. However, context-specific post-translational modifications, such as phosphorylation, can alter IGFBP1’s IGF-binding capacity, enabling dynamic regulation of IGF signaling in response to physiological conditions like fasting, pregnancy, or stress.
Recombinant IGFBP1 proteins are engineered using expression systems (e.g., *E. coli* or mammalian cells) to produce purified, biologically active forms for research and therapeutic applications. These proteins retain functional domains essential for IGF interaction, including conserved N- and C-terminal regions. Recombinant IGFBP1 is widely used to study metabolic disorders (e.g., diabetes), reproductive biology, and cancer, where dysregulated IGF signaling is implicated. For instance, it helps elucidate mechanisms in gestational diabetes or intrauterine growth restriction by mimicking endogenous IGFBP1’s role in modulating placental development.
In clinical research, recombinant IGFBP1 serves as a tool to explore its diagnostic or therapeutic potential. Altered IGFBP1 levels correlate with conditions like insulin resistance, making it a biomarker candidate. Additionally, engineered variants with modified phosphorylation sites or binding properties enable targeted studies of IGF-independent pathways, such as integrin-mediated cell migration. By providing a controlled, scalable source of IGFBP1. recombinant technology advances our understanding of IGF axis complexity and its translational relevance in human health and disease.
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