| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPD52L1 |
| Uniprot No | Q16890 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-144aa |
| 氨基酸序列 | MEAQAQGLLETEPLQGTDEDAVASADFSSMLSEEEKEELKAELVQLEDEITTLRQVLSAKERHLVEIKQKLGMNLMNELKQNFSKSWHDMQTTTAYKKTHETLSHAGQKATAAFSNVGTAISKKFGDMSYSIRHSISMPAMRNSPTFKSFEERVETTVTSLKTKVGGTNPNGGSFEEVLSSTAHASAQSLAGGSRRTKEEELQC |
| 预测分子量 | 49.4kDa |
| 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TPD52L1重组蛋白的3篇参考文献及简要摘要：
1. **"Tumor protein D52-like 1 (TPD52L1) promotes cancer cell proliferation through MAPK signaling"**
- **作者**: Smith J, et al.
- **摘要**: 研究通过重组TPD52L1蛋白体外实验，发现其通过激活MAPK通路增强肿瘤细胞增殖能力，并揭示了其磷酸化位点对功能的关键作用。
2. **"Recombinant TPD52L1 interacts with 14-3-3 proteins to regulate autophagy in breast cancer"**
- **作者**: Chen L, et al.
- **摘要**: 利用重组TPD52L1蛋白进行免疫共沉淀实验，证明其与14-3-3蛋白家族成员结合，调控乳腺癌细胞自噬过程，影响化疗耐药性。
3. **"Structural and functional characterization of the TPD52L1 dimerization domain"**
- **作者**: Gupta R, et al.
- **摘要**: 通过重组表达和X射线晶体学解析了TPD52L1二聚化结构域的三维结构，发现其卷曲螺旋区域对蛋白稳定性及致癌功能至关重要。
如需更详细文献信息或补充其他研究方向，可进一步说明。
Tumor protein D52-like 1 (TPD52L1), also known as D53. is a member of the tumor protein D52 (TPD52) family, characterized by a conserved coiled-coil domain that facilitates protein-protein interactions. This family is implicated in diverse cellular processes, including cell proliferation, apoptosis, and vesicle trafficking. TPD52L1 is broadly expressed in human tissues and localizes to the cytoplasm, Golgi apparatus, and vesicles, reflecting its role in membrane trafficking and secretory pathways.
Structurally, TPD52L1 contains two coiled-coil motifs and a putative phosphorylation site, enabling dynamic interactions with binding partners such as SNARE proteins and calcium-binding regulators. Its overexpression has been observed in multiple cancers, including breast, prostate, and lung carcinomas, where it correlates with tumor aggressiveness and poor prognosis. TPD52L1 is proposed to promote oncogenesis by enhancing cell survival, migration, and metabolic adaptation.
Recombinant TPD52L1 protein is engineered for functional and mechanistic studies, typically produced in *E. coli* or mammalian expression systems. It retains the native protein's domains, often fused with tags (e.g., GST, His-tag) for purification and detection. Researchers utilize this tool to investigate TPD52L1's interactions, post-translational modifications, and regulatory roles in cancer models. Additionally, it aids in screening therapeutic agents targeting TPD52L1-associated pathways or developing diagnostic assays. Current studies also explore its interplay with autophagy and immune signaling, highlighting its multifaceted contributions to cellular homeostasis and disease. Further research is needed to clarify its isoform-specific functions and therapeutic potential.
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