| 纯度 | ＞90% by SDS-PAGE. |
| 种属 | Human |
| 靶点 | YWHAQ |
| Uniprot No | P27348 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-245aa |
| 氨基酸序列 | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN |
| 预测分子量 | 54.8kDa |
| 蛋白标签 | C-his |
| 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. |
以下为YWHAQ(14-3-3τ)重组蛋白相关的文献摘要整理：
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1. **文献名称**：*14-3-3τ phosphorylation at serine 233 modulates interaction with client proteins*
**作者**：Smith A, et al.
**摘要**：本研究利用重组YWHAQ蛋白，探究其Ser233位点磷酸化对结合伴侣蛋白(如BAD和CDC25)的调控作用，揭示了磷酸化依赖性相互作用在细胞凋亡中的机制。
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2. **文献名称**：*Structural basis of 14-3-3τ protein dimerization and ligand recognition*
**作者**：Chen L, et al.
**摘要**：通过X射线晶体学解析重组YWHAQ蛋白的晶体结构，阐明其二聚化界面及与磷酸化靶肽的结合模式，为设计靶向14-3-3τ的小分子抑制剂提供结构基础。
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3. **文献名称**：*Recombinant YWHAQ enhances α-synuclein aggregation in Parkinson’s disease models*
**作者**：Wang X, et al.
**摘要**：体外实验表明，重组YWHAQ蛋白通过结合α-突触核蛋白磷酸化形式，促进其病理性聚集，提示14-3-3τ在神经退行性疾病中的潜在作用。
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4. **文献名称**：*Development of a high-throughput assay for 14-3-3τ-client protein interactions*
**作者**：Johnson R, et al.
**摘要**：基于重组YWHAQ蛋白构建荧光偏振检测平台，筛选出多个调控14-3-3τ与p53相互作用的化合物，为癌症治疗提供新策略。
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**注**：以上文献信息为示例性质，实际文献需通过学术数据库检索。建议使用关键词“YWHAQ recombinant”、“14-3-3 tau expression”或结合具体应用方向(如“cancer”“phosphorylation”)进行精确查找。
**Background of YWHAQ Recombinant Protein**
The YWHAQ protein, also known as 14-3-3 theta, belongs to the highly conserved 14-3-3 protein family, which comprises regulatory molecules involved in diverse cellular processes such as signal transduction, apoptosis, cell cycle control, and stress response. These proteins function as adaptors or scaffolds, modulating interactions between phosphorylated client proteins and other cellular components. YWHAQ specifically interacts with target proteins via phosphoserine/phosphothreonine motifs, influencing their stability, localization, or activity. Dysregulation of 14-3-3 proteins, including YWHAQ, has been implicated in pathologies like cancer, neurodegenerative disorders, and metabolic diseases, underscoring their therapeutic and diagnostic relevance.
Recombinant YWHAQ protein is produced using biotechnological methods, typically through expression in bacterial (e.g., *E. coli*) or eukaryotic (e.g., mammalian, insect) systems. This allows for large-scale, high-purity production of the protein for research and industrial applications. The recombinant form retains the native structure and functional properties of endogenous YWHAQ, enabling studies on its molecular interactions, post-translational modifications, and role in signaling networks.
In research, YWHAQ recombinant protein is utilized to investigate mechanisms underlying diseases linked to 14-3-3 dysfunction. For example, it aids in mapping binding partners in cancer-related pathways (e.g., PI3K/AKT, MAPK) or exploring its neuroprotective effects in models of Alzheimer’s or Parkinson’s disease. Additionally, it serves as a critical reagent in drug discovery, facilitating screens for small molecules that modulate 14-3-3-protein interactions.
Overall, YWHAQ recombinant protein is a vital tool for deciphering cellular regulation and advancing therapeutic strategies targeting 14-3-3-mediated pathways. Its applications span basic research, biomarker development, and preclinical drug evaluation.
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