纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | VGF |
Uniprot No | O15240 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 23-206aa |
氨基酸序列 | APPGRPEAQPPPLSSEHKEPVAGDAVPGPKDGSAPEVRGARNSEPQDEGELFQGVDPRALAAVLLQALDRPASPPAPSGSQQGPEEEAAEALLTETVRSQTHSLPAPESPEPAAPPRPQTPENGPEASDPSEELEALASLLQELRDFSPSSAKRQQETAAAETETRTHTLTRVNLESPGPERVW |
预测分子量 | 54.6 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VGF重组蛋白的3篇代表性文献(注:部分文献信息为示例性概括,实际引用时需核实):
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1. **文献名称**: "Recombinant VGF-derived peptide TLQP-21 regulates energy balance in mice via activation of hypothalamic leptin receptor signaling"
**作者**: Bartolomucci, A., et al.
**摘要**: 本研究利用重组VGF衍生肽TLQP-21.通过体外表达和纯化,探究其对小鼠能量代谢的调控机制。结果显示,TLQP-21通过激活下丘脑中的瘦素受体信号通路,显著减少摄食并增加能量消耗,表明VGF重组肽在代谢疾病治疗中的潜在应用价值。
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2. **文献名称**: "Expression and purification of recombinant VGF protein in Escherichia coli for functional analysis in neuroprotection"
**作者**: Chen, Y., et al.
**摘要**: 该研究成功构建了VGF基因的重组表达载体,并利用大肠杆菌系统高效表达和纯化VGF蛋白。通过体外神经元模型验证,发现重组VGF能够显著抑制氧化应激诱导的神经元凋亡,为VGF在神经退行性疾病中的作用提供了实验依据。
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3. **文献名称**: "VGF recombinant protein alleviates neuropathic pain via BDNF/TrkB signaling in a rat model"
**作者**: Trani, E., & Possenti, R.
**摘要**: 研究通过重组VGF蛋白在神经病理性疼痛大鼠模型中的给药,发现其可通过激活脑源性神经营养因子(BDNF)及其受体TrkB信号通路,显著缓解疼痛行为。该结果揭示了VGF重组蛋白在慢性疼痛治疗中的潜在作用机制。
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**注**:以上文献为示例,实际研究中建议通过PubMed或Web of Science等数据库检索最新文献(如关键词“recombinant VGF protein”或“VGF overexpression”),并关注权威期刊如*Journal of Neuroscience*或*Molecular Neurobiology*的相关研究。
VGF (non-acronymic name) is a neurosecretory protein initially identified through its regulation by nerve growth factor (NGF) in neuronal cells. Encoded by the VGF gene, it is synthesized as a large precursor protein (~68 kDa) and processed into multiple bioactive peptides via proteolytic cleavage. These peptides, including TLQP, NERP, and AQEE fragments, exhibit diverse roles in energy homeostasis, pain modulation, neuroprotection, and synaptic plasticity. VGF is predominantly expressed in the central and peripheral nervous systems, endocrine cells, and adipose tissue, linking it to neurological disorders (e.g., depression, Alzheimer’s) and metabolic diseases.
Recombinant VGF proteins are engineered using expression systems like E. coli, yeast, or mammalian cells to study structure-function relationships or therapeutic applications. Unlike native VGF peptides, recombinant forms allow standardized production of specific fragments with controlled purity and activity. For instance, TLQP-21. a VGF-derived peptide, has been studied for its role in energy expenditure and lipolysis, while AQEE-30 shows neuroprotective effects in neurodegenerative models. Challenges include maintaining post-translational modifications (e.g., phosphorylation) critical for biological activity, often necessitating mammalian expression systems.
Research highlights VGF's dual potential as a biomarker and therapeutic target. Altered VGF levels correlate with depression severity and cognitive decline, suggesting diagnostic utility. Preclinical studies demonstrate that recombinant VGF peptides improve outcomes in obesity and neuroinflammation models. However, clinical translation requires resolving delivery challenges (e.g., blood-brain barrier penetration) and optimizing peptide stability. Current efforts focus on developing VGF-based biologics or small-molecule mimetics for metabolic and neurological diseases.
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