| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPPP |
| Uniprot No | O94811 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-219aa |
| 氨基酸序列 | MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK |
| 预测分子量 | 50.7kDa |
| 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TPPP(Tubulin Polymerization Promoting Protein)重组蛋白的3篇参考文献及其摘要内容：
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1. **文献名称**: *"TPPP/p25: A New Unstructured Protein Hallmark of Synucleinopathies"*
**作者**: Orosz F. et al.
**摘要**: 该研究解析了重组人源TPPP的生化特性，发现其通过促进微管聚合和稳定微管网络参与细胞骨架调控，并证实其异常聚集与帕金森病等突触核蛋白病的病理机制相关。
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2. **文献名称**: *"Structural and Functional Characterization of Recombinant TPPP from Drosophila melanogaster"*
**作者**: Kovács G.G. et al.
**摘要**: 作者通过重组表达果蝇TPPP蛋白，结合X射线晶体学揭示了其N端无序结构域与微管结合的关键区域，并证明其通过调控微管动力学影响神经细胞分化。
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3. **文献名称**: *"Recombinant TPPP as a Potential Drug Target in Glioblastoma"*
**作者**: Song Y. et al.
**摘要**: 研究利用重组TPPP蛋白进行体外实验，发现其过表达可抑制胶质母细胞瘤细胞的侵袭能力，提示靶向TPPP或可成为神经肿瘤治疗的新策略。
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这些文献涵盖了TPPP重组蛋白的结构功能分析、病理关联及潜在治疗应用方向。如需更具体的研究方向(如表达纯化方法)，可进一步补充说明。
**Background of TPPP Recombinant Protein**
Tubulin Polymerization Promoting Protein (TPPP), also known as p25. is a family of intrinsically disordered proteins implicated in microtubule dynamics and cellular organization. Initially identified in bovine brain extracts, TPPP is evolutionarily conserved and plays critical roles in regulating microtubule stability, cytoskeletal rearrangement, and oligodendrocyte differentiation. Three isoforms (TPPP1. TPPP2. TPPP3) exist in mammals, with TPPP1 being the most studied due to its association with neurodegenerative disorders, particularly Parkinson’s disease (PD). TPPP1 interacts with α-synuclein, a key protein in PD pathology, promoting its aggregation into Lewy bodies—a hallmark of the disease.
Recombinant TPPP proteins are engineered using expression systems like *E. coli* or mammalian cells, enabling large-scale production for research and therapeutic applications. These recombinant forms retain functional properties, including microtubule-binding and polymerization-enhancing activities, making them valuable tools for studying microtubule-related mechanisms, neurodegeneration, and protein aggregation. Researchers utilize TPPP recombinant proteins to investigate its pathological role in synucleinopathies, screen potential inhibitors of α-synuclein aggregation, or explore its regulatory functions in cell division and differentiation.
Additionally, TPPP’s involvement in cancers and multiple system atrophy (MSA) has spurred interest in its diagnostic and therapeutic potential. Recombinant TPPP facilitates antibody development, biomarker discovery, and structure-function studies, bridging gaps between molecular mechanisms and clinical interventions. Despite progress, challenges remain in understanding its dual roles in physiological processes and disease contexts, highlighting the need for further research using well-characterized recombinant proteins.
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