| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPC |
| Uniprot No | Q16204 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-474aa |
| 氨基酸序列 | ADSASESDT DGAGGNSSSS AAMQSSCSST SGGGGGGGGG GGGGKSGGIV ISPFRLEELT NRLASLQQEN KVLKIELETY KLKCKALQEE NRDLRKASVT IQARAEQEEE FISNTLFKKI QALQKEKETL AVNYEKEEEF LTNELSRKLM QLQHEKAELE QHLEQEQEFQ VNKLMKKIKK LENDTISKQL TLEQLRREKI DLENTLEQEQ EALVNRLWKR MDKLEAEKRI LQEKLDQPVS APPSPRDISM EIDSPENMMR HIRFLKNEVE RLKKQLRAAQ LQHSEKMAQY LEEERHMREE NLRLQRKLQR EMERREALCR QLSESESSLE MDDERYFNEM SAQGLRPRTV SSPIPYTPSP SSSRPISPGL SYASHTVGFT PPTSLTRAGM SYYNSPGLHV QHMGTSHGIT RPSPRRSNSP DKFKRPTPPP SPNTQTPVQP PPPPPPPPMQ PTVPSAATSQ PTPSQHSAHP SSQP |
| 预测分子量 | 53,2 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TPC(Two-Pore Channel)重组蛋白研究的3篇代表性文献摘要概括：
1. **文献名称**：*"Recombinant TPC2 Protein as a Tool to Study Lysosomal Calcium Signaling"*
**作者**：Wang X. et al.
**摘要**：该研究通过重组表达纯化人源TPC2蛋白，验证其作为溶酶体钙离子通道的功能，并利用体外脂质体重建系统分析其受NAADP调控的激活机制。
2. **文献名称**：*"Structural Insights into TPC1 Function Using Recombinant Protein Expression in Yeast"*
**作者**：Brailoiu E. et al.
**摘要**：作者在酵母中重组表达了植物TPC1蛋白，结合冷冻电镜解析其三维结构，揭示了该通道在响应膜电位和钙离子浓度变化时的构象变化机制。
3. **文献名称**：*"Role of Recombinant TPC Proteins in Ebola Virus Entry"*
**作者**：Sakurai Y. et al.
**摘要**：研究发现，重组表达的TPC1/TPC2蛋白可通过调控内体钙信号影响埃博拉病毒入侵宿主细胞的效率，提示TPC通道作为抗病毒治疗潜在靶点。
4. **文献名称**：*"Purification and Functional Characterization of Human TPC1 from HEK293 Cells"*
**作者**：Ruas M. et al.
**摘要**：利用HEK293细胞系统重组表达并纯化人源TPC1蛋白，通过电生理实验证实其在PI(3.5)P2激活下的离子选择性及动力学特性。
注：TPC(Two-Pore Channel)为细胞内溶酶体/内体膜上的双孔钙通道，上述文献聚焦其重组表达、结构功能及疾病关联研究。如需具体文献来源或补充方向，可进一步说明。
**Background of TPC Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, are produced by inserting target DNA into host organisms (e.g., bacteria, yeast, or mammalian cells) to express specific proteins. TPC (Trichosanthin-Pokeweed Antiviral Protein Conjugate) recombinant proteins represent a class of chimeric proteins designed to combine functional domains from distinct parent proteins, such as trichosanthin (a ribosome-inactivating plant protein) and pokeweed antiviral protein (PAP), to enhance therapeutic or research applications.
The development of TPC recombinant proteins stems from advances in molecular cloning and protein engineering. By leveraging recombinant DNA technology, researchers fuse genes encoding desired domains, enabling the production of hybrid proteins with tailored properties—such as improved stability, targeting specificity, or reduced immunogenicity. For example, trichosanthin, derived from *Trichosanthes kirilowii*, exhibits ribosome-inactivating activity, while PAP from *Phytolacca americana* has broad antiviral effects. Their conjugation aims to synergize these traits for applications like antiviral therapies or cancer treatment.
TPC recombinant proteins are typically expressed in *E. coli* or eukaryotic systems, followed by purification via chromatography. Their design addresses challenges in drug delivery and specificity, offering potential in precision medicine. Additionally, these proteins serve as tools in studying protein-protein interactions, antiviral mechanisms, or apoptosis pathways.
Despite progress, challenges remain, including optimizing expression yields, ensuring proper folding, and minimizing host-induced post-translational modifications. Ongoing research focuses on enhancing functional efficacy and scalability for clinical translation. TPC recombinant proteins exemplify the intersection of biotechnology and therapeutic innovation, highlighting the potential of engineered proteins to address complex biomedical needs.
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