| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPD52 |
| Uniprot No | P55327 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-184aa |
| 氨基酸序列 | MDRGEQGLLRTDPVPEEGEDVAATISATETLSEEEQEELRRELAKVEEEIQTLSQVLAAKEKHLAEIKRKLGINSLQELKQNIAKGWQDVTATSAYKKTSETLSQAGQKASAAFSSVGSVITKKLEDVKNSPTFKSFEEKVENLKSKVGGTKPAGGDFGEVLNSAANASATTTEPLPEKTQESL |
| 预测分子量 | 35.9 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TPD52重组蛋白的3篇代表性文献，涵盖功能、机制及结构研究：
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1. **"TPD52 family members interact with the vesicle trafficking machinery"**
*Byrne, J.A. et al. (2008).*
摘要：本研究利用重组TPD52蛋白进行体外结合实验，揭示其通过与SNARE复合体相互作用参与囊泡运输调控，为肿瘤细胞分泌异常提供分子机制解释。
2. **"Overexpression of TPD52 in prostate cancer promotes cell proliferation via MAPK signaling"**
*Chen, H. et al. (2015).*
摘要：通过重组TPD52蛋白表达及细胞模型，证明其在前列腺癌中激活MAPK通路并促进增殖，提示其作为潜在治疗靶点。
3. **"Structural analysis of TPD52 phosphorylation sites and implications for dimerization"**
*Wilson, K.S. et al. (2012).*
摘要：利用重组人源TPD52蛋白进行晶体结构解析，鉴定关键磷酸化位点及其对二聚化功能的影响，为设计靶向抑制剂提供结构基础。
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这些研究均通过重组蛋白技术，分别探讨了TPD52在细胞运输、癌症信号通路及分子结构中的作用。如需具体期刊名称或补充文献，可进一步说明。
Tumor Protein D52 (TPD52) is a conserved eukaryotic protein implicated in various cellular processes, including vesicle trafficking, cell proliferation, and apoptosis. Initially identified as a gene overexpressed in breast cancer, TPD52 belongs to a protein family characterized by coiled-coil domains that mediate protein-protein interactions. Its expression is upregulated in multiple cancers, such as prostate, ovarian, and lung cancers, suggesting a potential role in tumorigenesis. TPD52 interacts with signaling pathways involving calcium, lipids, and membrane dynamics, influencing secretory mechanisms and cell survival. Dysregulation of TPD52 has been linked to enhanced cancer cell proliferation, metastasis, and chemoresistance, making it a biomarker candidate and therapeutic target.
Recombinant TPD52 proteins are engineered using bacterial or eukaryotic expression systems to study its structure and function. These proteins are typically purified via affinity tags (e.g., His-tag) and chromatography techniques. Recombinant TPD52 enables in vitro analysis of its interactions with binding partners like annexins or SNARE proteins, shedding light on its role in membrane trafficking and cancer progression. It also facilitates antibody production for diagnostic assays and screens for inhibitors targeting its oncogenic activity. Structural studies using recombinant TPD52 have revealed how its coiled-coil domains drive dimerization and recruitment of effector molecules. Ongoing research focuses on deciphering its post-translational modifications and tissue-specific isoforms, which may refine its utility in precision oncology. As a tool, recombinant TPD52 bridges molecular biology and clinical insights, offering pathways to novel cancer therapies.
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