首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%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重组蛋白的假设性参考文献示例(仅供参考，非真实文献)：
---
1. **《高效表达与纯化重组人IGF2蛋白及其生物活性研究》**
*作者：Zhang L, Wang Y, et al.*
摘要：研究利用大肠杆菌表达系统成功表达重组人IGF2蛋白，通过优化诱导条件和亲和层析纯化获得高纯度蛋白，体外实验证实其能显著促进成肌细胞增殖。
2. **《重组IGF2通过MAPK通路调控肿瘤细胞侵袭的机制》**
*作者：Chen H, Liu X, et al.*
摘要：探讨重组IGF2在乳腺癌细胞中的作用，发现其通过激活MAPK信号通路增强细胞迁移和侵袭能力，为靶向治疗提供潜在靶点。
3. **《重组IGF2在骨骼修复中的应用：动物模型验证》**
*作者：Martinez R, et al.*
摘要：研究在小鼠骨缺损模型中局部应用重组IGF2蛋白，结果显示其显著促进成骨细胞分化和骨组织再生，提示其在骨修复中的临床应用潜力。
4. **《重组IGF2蛋白的糖基化修饰对其功能的影响》**
*作者：Kim S, Park J, et al.*
摘要：比较哺乳动物细胞(CHO)与原核系统表达的IGF2.发现糖基化修饰显著影响其受体结合效率和体内半衰期，为生产优化提供依据。
---
注：以上为示例性内容，实际文献需通过学术数据库(如PubMed、Web of Science)检索。
Insulin-like growth factor 2 (IGF2) is a peptide hormone structurally homologous to proinsulin, playing critical roles in fetal growth, cell proliferation, differentiation, and metabolism regulation. It primarily signals through the IGF1 receptor (IGF1R) and insulin receptor (IR), though it also interacts with the IGF2 receptor (IGF2R), a scavenger receptor with no signaling function. Dysregulation of IGF2 expression is linked to developmental disorders, cancer progression, and metabolic diseases.
Recombinant IGF2 protein is produced using DNA technology, where the *IGF2* gene is cloned into expression systems like *E. coli*, mammalian cells, or yeast. Post-translationally modified forms (e.g., glycosylated) often require mammalian expression to mimic natural isoforms. The protein is purified via chromatography, ensuring high purity and bioactivity for research or therapeutic use. Recombinant production overcomes limitations of tissue-derived IGF2. offering batch consistency and avoiding pathogen risks.
In research, recombinant IGF2 aids studies on growth signaling mechanisms, stem cell differentiation, and disease models such as cancers (e.g., hepatocellular carcinoma) or imprinting disorders like Beckwith-Wiedemann syndrome. Therapeutically, it holds potential for treating muscle wasting, wound healing, or neurodegenerative conditions, though its oncogenic risks necessitate controlled delivery. Current challenges include optimizing receptor specificity and minimizing off-target effects.
Recent advances explore engineered IGF2 variants with improved stability or tissue targeting, as well as its role as a biomarker in prenatal diagnostics and cancer. Despite preclinical progress, clinical applications remain limited, underscoring the need for deeper mechanistic studies and safety evaluations.
×
