纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | DDC |
Uniprot No | P20711 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-480aa |
氨基酸序列 | MNASEFRRRG KEMVDYMANY MEGIEGRQVY PDVEPGYLRP LIPAAAPQEP DTFEDIINDV EKIIMPGVTH WHSPYFFAYF PTASSYPAML ADMLCGAIGC IGFSWAASPA CTELETVMMD WLGKMLELPK AFLNEKAGEG GGVIQGSASE ATLVALLAAR TKVIHRLQAA SPELTQAAIM EKLVAYSSDQ AHSSVERAGL IGGVKLKAIP SDGNFAMRAS ALQEALERDK AAGLIPFFMV ATLGTTTCCS FDNLLEVGPI CNKEDIWLHV DAAYAGSAFI CPEFRHLLNG VEFADSFNFN PHKWLLVNFD CSAMWVKKRT DLTGAFRLDP TYLKHSHQDS GLITDYRHWQ IPLGRRFRSL KMWFVFRMYG VKGLQAYIRK HVQLSHEFES LVRQDPRFEI CVEVILGLVC FRLKGSNKVN EALLQRINSA KKIHLVPCHL RDKFVLRFAI CSRTVESAHV QRAWEHIKEL AADVLRAERE |
预测分子量 | 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DDC(多巴脱羧酶)重组蛋白研究的示例参考文献(内容为模拟概括,非真实文献):
1. **《Cloning and Prokaryotic Expression of Human DDC Gene》**
- 作者:Smith A, et al.
- 摘要:研究成功克隆了人源DDC基因,并在大肠杆菌中实现重组表达,通过亲和层析纯化获得高纯度蛋白,酶活性实验证实其催化多巴转化为多巴胺的能力。
2. **《Optimization of DDC Expression in Pichia pastoris for Functional Studies》**
- 作者:Zhang L, et al.
- 摘要:探讨了毕赤酵母系统中DDC重组蛋白的表达条件优化,包括诱导时间和温度调控,获得的蛋白具备与天然酶相似的动力学特性,适用于体外药物筛选。
3. **《Structural Insights into DDC via X-ray Crystallography》**
- 作者:Tanaka K, et al.
- 摘要:首次解析了重组DDC蛋白的晶体结构,揭示了其底物结合位点和辅酶相互作用机制,为设计特异性抑制剂提供了结构基础。
4. **《Recombinant DDC in Parkinson’s Disease Models》**
- 作者:Johnson R, et al.
- 摘要:利用重组DDC蛋白在小鼠模型中恢复多巴胺合成,证明其潜在治疗帕金森病的应用价值,并评估了血脑屏障穿透策略。
**注**:以上文献信息为示例,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
**Background of DDC Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. DDC (Dopa Decarboxylase), also known as aromatic L-amino acid decarboxylase (AADC), is a pyridoxal phosphate-dependent enzyme that catalyzes the decarboxylation of L-DOPA to dopamine and 5-hydroxytryptophan to serotonin. These neurotransmitters play critical roles in regulating mood, cognition, and motor functions. Dysregulation of DDC activity is linked to neurological disorders (e.g., Parkinson’s disease), metabolic diseases, and certain cancers.
The production of DDC as a recombinant protein enables precise study of its structure, function, and interactions. Using expression systems like *E. coli*, yeast, or mammalian cells, researchers generate high-purity, active DDC for *in vitro* assays, drug screening, and structural studies (e.g., X-ray crystallography). Recombinant DDC also serves as a tool to investigate enzyme kinetics, inhibitor development, and mechanisms underlying DDC-related pathologies. For instance, mutations in the *DDC* gene cause AADC deficiency, a rare neurometabolic disorder, and recombinant protein studies aid in developing enzyme replacement therapies or gene therapies.
Additionally, recombinant DDC is vital in biomanufacturing. It can be engineered for enhanced stability or altered substrate specificity, expanding its applications in synthetic biology or industrial biocatalysis. In diagnostics, DDC-based assays help quantify neurotransmitter levels or detect autoantibodies in autoimmune conditions.
Overall, DDC recombinant proteins bridge basic science and translational medicine, offering insights into neurobiology, disease mechanisms, and therapeutic innovation. Their scalability and versatility underscore their importance in both academic and industrial settings.
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