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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IGF2 |
| Uniprot No | P01344 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 25-91aa |
| 氨基酸序列 | AYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRS CDLALLETYCATPAKSE |
| 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. |
以下是关于IGF2重组蛋白的3篇参考文献示例(信息基于公开文献概括，非真实引用)：
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1. **文献名称**：*Production and characterization of recombinant human IGF2 in E. coli for therapeutic applications*
**作者**：Smith A, et al.
**摘要**：该研究报道了在大肠杆菌中高效表达重组人IGF2蛋白的工艺，通过优化密码子和纯化步骤获得高纯度蛋白，并验证其促进细胞增殖的生物活性，为糖尿病治疗研究提供材料基础。
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2. **文献名称**：*Recombinant IGF2 enhances placental development in a murine intrauterine growth restriction model*
**作者**：Chen L, et al.
**摘要**：研究利用哺乳动物细胞表达系统生产重组IGF2.通过小鼠模型证明其能通过激活PI3K/Akt通路改善胎盘血管生成，缓解胎儿生长受限，提示其在产科疾病的潜在治疗价值。
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3. **文献名称**：*Structural and functional analysis of glycosylated versus non-glycosylated IGF2 isoforms*
**作者**：Wang Y, et al.
**摘要**：通过昆虫细胞(糖基化)和大肠杆菌(非糖基化)系统分别制备重组IGF2.比较两者结构差异及对IGF1R受体的亲和力，揭示糖基化修饰对蛋白稳定性和信号调控的影响。
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**注**：以上为模拟摘要，实际文献需通过PubMed或Web of Science检索关键词“recombinant IGF2”获取。如需真实文献，可提供具体研究方向(如疾病机制、纯化工艺等)进一步筛选。
**Background of Recombinant IGF2 Protein**
Recombinant insulin-like growth factor 2 (IGF2) is a synthetic version of the naturally occurring IGF2 protein, a key member of the insulin-like growth factor family. IGF2. encoded by the *IGF2* gene in humans, is a 67-amino acid polypeptide hormone structurally similar to insulin and IGF1. It plays critical roles in fetal development, tissue growth, and metabolism by binding to receptors such as the IGF1 receptor (IGF1R) and insulin receptor (IR), activating downstream signaling pathways like PI3K/AKT and MAPK. Unlike IGF1. IGF2 expression is predominantly regulated by genomic imprinting, with the paternal allele being primarily active.
Recombinant IGF2 is produced using biotechnological platforms like *E. coli*, yeast, or mammalian cell systems. These systems enable scalable production of high-purity, bioactive IGF2 for research and therapeutic applications. In research, recombinant IGF2 is used to study its role in development, cancer (where IGF2 overexpression is linked to tumor progression), and metabolic disorders. It also serves as a tool to explore imprinting disorders like Beckwith-Wiedemann syndrome. Therapeutically, recombinant IGF2 has potential in treating growth deficiencies, muscle wasting, or wound healing, though clinical applications remain experimental.
Challenges in recombinant IGF2 production include ensuring proper post-translational modifications (e.g., glycosylation) for full bioactivity, which often requires mammalian expression systems. Additionally, its dual receptor-binding behavior and complex regulatory mechanisms necessitate careful functional characterization. Despite these hurdles, recombinant IGF2 remains a vital reagent for advancing both basic science and translational medicine.
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