| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TDP43 |
| Uniprot No | Q13148 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-260aa |
| 氨基酸序列 | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSEY IRVTEDENDE PIEIPSEDDG TVLLSTVTAQ FPGACGLRYR NPVSQCMRGV RLVEGILHAP DAGWGNLVYV VNYPKDNKRK MDETDASSAV KVKRAVQKTS DLIVLGLPWK TTEQDLKEYF STFGEVLMVQ VKKDLKTGHS KGFGFVRFTE YETQVKVMSQ RHMIDGRWCD CKLPNSKQSQ DEPLRSRKVF VGRCTEDMTE DELREFFSQY GDVMDVFIPK PFRAFAFVTF ADDQIAQSLC GEDLIIKGIS VHISNA |
| 预测分子量 | 34 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3篇关于TDP-43重组蛋白的文献示例(注：以下为假设性文献，仅用于示例格式)：
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1. **文献名称**：*"Purification and aggregation properties of recombinant human TDP-43"*
**作者**：Smith A. et al.
**摘要**：研究报道了在大肠杆菌中高效表达并纯化重组人源TDP-43蛋白的方法，发现其在体外易形成淀粉样纤维聚集体，模拟了神经退行性疾病中的病理特征。
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2. **文献名称**：*"Structural insights into TDP-43 RNA-binding domain misfolding"*
**作者**：Chen L. et al.
**摘要**：通过核磁共振(NMR)解析重组TDP-43的RNA结合域结构，揭示其病理性突变(如A315T)导致蛋白错误折叠并促进细胞毒性聚集的分子机制。
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3. **文献名称**：*"TDP-43 liquid-liquid phase separation driven by recombinant protein interactions"*
**作者**：Wang Y. et al.
**摘要**：利用重组TDP-43蛋白验证其通过N端低复杂度结构域发生液-液相分离(LLPS)，并证明磷酸化修饰可增强其病理聚集倾向，与ALS疾病相关。
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如需真实文献，建议通过PubMed或Google Scholar搜索关键词："recombinant TDP-43 protein"或"TDP-43 in vitro aggregation"。
TAR DNA-binding protein 43 (TDP-43) is a ubiquitously expressed RNA-binding protein critical for regulating RNA metabolism, including splicing, transport, and stability. Structurally, it contains two conserved RNA-recognition motifs (RRMs) and a C-terminal prion-like domain implicated in protein-protein interactions. Under physiological conditions, TDP-43 resides predominantly in the nucleus, but in neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD), it forms cytoplasmic aggregates characterized by hyperphosphorylation, ubiquitination, and cleavage. These pathological inclusions are hallmarks of disease progression and are linked to neuronal dysfunction and death.
Recombinant TDP-43 proteins are engineered in vitro using expression systems like *E. coli* or mammalian cells to study its normal and pathological functions. These purified proteins retain key domains and biochemical properties, enabling researchers to investigate mechanisms underlying TDP-43 misfolding, aggregation, and interactions with RNA or other proteins. Studies using recombinant TDP-43 have revealed its propensity to undergo liquid-liquid phase separation, a process dysregulated in disease. Additionally, in vitro models have helped identify post-translational modifications (e.g., phosphorylation) and truncation events that promote aggregation.
Current research leverages recombinant TDP-43 to screen therapeutic compounds targeting aggregation or to develop biomarkers. Challenges include replicating disease-specific modifications in vitro and modeling the dynamic shift from soluble to aggregated states. Understanding TDP-43 pathology through recombinant systems remains pivotal for unraveling neurodegenerative mechanisms and designing targeted therapies.
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