首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GDN |
| Uniprot No | P07093 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-398aa |
| 氨基酸序列 | SHFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITTGSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP |
| 预测分子量 | 57.9 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GDNF(胶质细胞源性神经营养因子)重组蛋白的模拟参考文献示例，供参考使用。建议通过学术数据库(如PubMed、Google Scholar)检索最新文献以获取具体研究：
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1. **标题**：*High-yield expression and purification of recombinant human GDNF in Escherichia coli*
**作者**：Smith A, et al.
**摘要**：本研究报道了一种利用大肠杆菌表达系统高效生产重组人GDNF的方法，通过优化密码子和纯化步骤，获得了具有生物活性的GDNF蛋白，验证其对神经元细胞的存活促进作用。
2. **标题**：*Therapeutic potential of recombinant GDNF in a Parkinson’s disease mouse model*
**作者**：Johnson R, et al.
**摘要**：通过动物实验证明，重组GDNF蛋白能显著改善帕金森病模型小鼠的运动功能，并促进中脑多巴胺能神经元的存活和突触再生，提示其作为神经保护剂的潜力。
3. **标题**：*Structural characterization of mammalian cell-derived GDNF using cryo-EM*
**作者**：Lee H, et al.
**摘要**：利用哺乳动物表达系统(CHO细胞)生产重组GDNF，并通过冷冻电镜解析其三维结构，揭示其与受体结合的分子机制，为优化蛋白功能提供依据。
4. **标题**：*Comparative analysis of GDNF bioactivity from different recombinant expression systems*
**作者**：Chen X, et al.
**摘要**：对比细菌、昆虫和哺乳动物细胞表达的重组GDNF蛋白，发现哺乳动物来源的GDNF具有更高的糖基化水平和体内稳定性，强调了表达系统选择对临床应用的重要性。
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**注意**：以上为模拟文献，实际研究中请查阅真实发表的论文。检索时可使用关键词“GDNF recombinant protein”“GDNF expression”“GDNF therapeutic application”等。
**Background of Recombinant GDN Protein**
Glial cell line-derived neurotrophic factor (GDNF), a member of the transforming growth factor-β (TGF-β) superfamily, was first identified in 1993 for its critical role in promoting the survival and differentiation of midbrain dopaminergic neurons. This discovery positioned GDNF as a promising therapeutic candidate for neurodegenerative disorders, particularly Parkinson’s disease (PD), where dopaminergic neuron degeneration is a hallmark. Structurally, GDNF functions as a homodimer, binding to the GDNF family receptor α1 (GFRα1) and activating the RET tyrosine kinase receptor to regulate cell survival, proliferation, and synaptic plasticity.
Recombinant GDNF (rGDNF) is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. Its production addresses the need for scalable, pure, and bioactive protein for research and clinical applications. Early preclinical studies demonstrated rGDNF’s efficacy in rescuing dopaminergic neurons in PD models, sparking interest in clinical trials. However, human trials yielded mixed results, partly due to challenges in protein delivery across the blood-brain barrier and optimal dosing regimens.
Beyond PD, rGDNF has shown potential in treating other conditions, including neuropathies, spinal cord injuries, and diabetes. In the peripheral nervous system, it supports sensory and autonomic neurons, while in metabolic contexts, it enhances pancreatic β-cell function. Recent advancements focus on improving rGDNF delivery methods (e.g., viral vectors, encapsulated cell implants) and engineering variants with enhanced stability or tissue specificity.
Despite hurdles, rGDNF remains a cornerstone in neurotrophic factor research, reflecting its unique neuroprotective and regenerative properties. Ongoing studies aim to refine its therapeutic applications, underscoring its enduring relevance in neuroscience and regenerative medicine.
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