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| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VEGF121 |
| Uniprot No | P15692-9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-147aa |
| 氨基酸序列 | APMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPS CVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHN KCECRPKKDRARQEKCDKPRR |
| 预测分子量 | 14 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VEGF121重组蛋白的3篇参考文献的简要总结：
1. **标题**：*Production and characterization of recombinant human VEGF121 in insect cells*
**作者**：Ferrara, N. et al.
**摘要**：该研究利用杆状病毒表达系统在昆虫细胞中高效表达并纯化重组人VEGF121蛋白，证实其具有促进内皮细胞增殖和迁移的活性，且与VEGF165相比缺乏肝素结合能力。
2. **标题**：*VEGF121 regulates endothelial cell survival through PI3K/Akt signaling pathway*
**作者**：Soker, S. et al.
**摘要**：研究证明重组VEGF121通过激活PI3K/Akt信号通路抑制内皮细胞凋亡，并揭示了其与VEGF受体2(VEGFR2)的特异性结合在缺血性疾病治疗中的潜在应用。
3. **标题**：*Comparative analysis of VEGF121 and VEGF165 in tumor angiogenesis models*
**作者**：Dvorak, H.F. et al.
**摘要**：通过小鼠肿瘤模型比较发现，重组VEGF121因缺乏细胞外基质结合域，表现出更广泛的扩散性，但其促血管生成活性持续时间短于VEGF165.提示亚型选择对治疗策略的影响。
注：以上文献信息为基于领域知识的示例，实际引用需以具体论文内容为准。建议通过PubMed或Web of Science以关键词“VEGF121 recombinant”进一步检索最新研究。
Vascular endothelial growth factor 121 (VEGF₁₂₁) is a splice variant of the VEGF-A gene, a key regulator of angiogenesis. VEGF-A undergoes alternative mRNA splicing to generate multiple isoforms, with VEGF₁₂₁ being the shortest and most soluble form due to the absence of heparin-binding domains present in longer isoforms like VEGF₁₆₅. This 121-amino-acid protein retains the receptor-binding regions essential for activating VEGF receptors (VEGFR-1 and VEGFR-2), triggering downstream signaling pathways (e.g., PI3K-Akt and MAPK) that promote endothelial cell proliferation, migration, and vascular permeability.
Recombinant VEGF₁₂₁ is typically produced using expression systems like *E. coli* or mammalian cells. Its lack of heparin-binding motifs simplifies purification compared to other isoforms, while maintaining biological activity. This makes it a valuable tool for studying angiogenesis mechanisms *in vitro* and *in vivo*. In research, VEGF₁₂₁ is used to stimulate endothelial cell responses, model vascular development, and investigate pathological conditions such as cancer and ischemic diseases. Its therapeutic potential has been explored for promoting collateral blood vessel formation in ischemic tissues (e.g., myocardial infarction, peripheral artery disease) and enhancing wound healing. However, its short half-life and unregulated pro-angiogenic effects limit clinical applications, necessitating delivery systems or combination therapies.
Notably, VEGF₁₂₁’s inability to bind extracellular matrix components distinguishes it from heparin-binding isoforms, resulting in broader tissue diffusion but reduced local retention. This property influences its functional outcomes in different experimental or therapeutic contexts. While VEGF-targeted drugs (e.g., bevacizumab) primarily focus on inhibiting pathological angiogenesis, recombinant VEGF₁₂₁ remains pivotal in both basic research and emerging regenerative medicine strategies, despite mixed results in clinical trials for cardiovascular repair. Its role in balancing pro- and anti-angiogenic therapies continues to drive interdisciplinary studies.
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