首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >98%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EG-VEGF |
| Uniprot No | P58294 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-105aa |
| 氨基酸序列 | AVITGACERDVQCGAGTCCAISLWLRGLRMCTPLGREGEECHPGSHKVPF FRKRKHHTCPCLPNLLCSRFPDGRYRCSMDLKNINF |
| 预测分子量 | 10 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EG-VEGF(Endocrine Gland-Derived Vascular Endothelial Growth Factor，也称Prokineticin 1)重组蛋白的3篇代表性文献及其摘要内容：
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1. **文献名称**: *Identification of EG-VEGF as a novel angiogenic factor in endocrine glands*
**作者**: LeCouter, J., et al.
**摘要**: 该研究首次鉴定了EG-VEGF作为内分泌器官(如肾上腺、卵巢)特异性的血管生成因子，利用重组EG-VEGF蛋白证明其能选择性促进这些组织中内皮细胞的增殖和迁移，与VEGF形成互补作用，揭示了其在局部血管调控中的关键功能。
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2. **文献名称**: *Prokineticin 1 signaling and receptor specificity in endothelial cells*
**作者**: Masuda, H., et al.
**摘要**: 本研究通过重组PROK1(即EG-VEGF)蛋白分析其与受体(PKR1/PKR2)的相互作用，发现其通过激活MAPK和PI3K-Akt信号通路诱导内皮细胞趋化性，并证实其在体外和体内模型中促进血管新生的能力，为靶向治疗提供依据。
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3. **文献名称**: *EG-VEGF regulates human follicular development via autocrine mechanisms*
**作者**: Ferrara, S., et al.
**摘要**: 通过重组EG-VEGF蛋白实验，本文揭示了其在人类卵巢卵泡发育中的自分泌作用，证明其通过调控颗粒细胞增殖及激素分泌影响卵母细胞成熟，提示其在不孕症和生殖医学中的潜在应用价值。
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4. **文献名称**: *Prokineticin 1 overexpression drives tumor angiogenesis in colorectal cancer*
**作者**: Furness, F.B., et al.
**摘要**: 该研究利用重组EG-VEGF蛋白及基因沉默技术，证明其在结直肠癌中通过激活肿瘤相关内皮细胞促进血管异常生成，并与患者预后不良相关，提示其作为抗血管生成治疗的新靶点。
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这些文献涵盖了EG-VEGF重组蛋白在基础机制、生殖生物学及肿瘤学中的关键研究，反映了其多方面的生物学功能和应用潜力。
**Background of EG-VEGF Recombinant Protein**
Endocrine gland-derived vascular endothelial growth factor (EG-VEGF), also known as prokineticin-1 (PK1), is a secreted protein identified in 2001 as a tissue-specific angiogenic factor. Unlike classical VEGF family members, EG-VEGF shares no structural homology with VEGF but exerts similar biological effects, primarily regulating angiogenesis and vascular permeability. It is predominantly expressed in steroidogenic tissues, including the adrenal glands, ovaries, testes, and placenta, suggesting a role in endocrine organ development and function.
EG-VEGF binds to two G protein-coupled receptors, PROKR1 and PROKR2. activating intracellular signaling pathways such as MAPK/ERK and PI3K/Akt. These pathways promote endothelial cell proliferation, migration, and survival, contributing to tissue-specific vascularization. Its expression is hormonally regulated, with links to reproductive physiology (e.g., corpus luteum formation) and pathologies like cancer, where it may drive tumor angiogenesis.
Recombinant EG-VEGF is produced via DNA cloning and expression in prokaryotic (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian cells), ensuring post-translational modifications for bioactivity. Purified recombinant protein enables *in vitro* and *in vivo* studies to dissect its roles in angiogenesis, endocrine function, and disease mechanisms. Potential therapeutic applications include promoting tissue regeneration or inhibiting EG-VEGF signaling in cancers. However, challenges remain in understanding its interplay with other angiogenic factors and optimizing targeted delivery.
Research on EG-VEGF highlights its unique niche in vascular biology, bridging endocrine regulation and tissue-specific angiogenesis, offering insights for both physiological studies and clinical translation.
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