| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TSG101 |
| Uniprot No | Q99816 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-145aa |
| 氨基酸序列 | MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFSRP |
| 预测分子量 | 20.7 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TSG101重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**：*HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 for particle release*
**作者**：Demirov, D.G., et al.
**摘要**：该研究揭示了HIV-1通过其Gag蛋白的"late domain"与TSG101重组蛋白直接相互作用，促进病毒粒子从宿主细胞膜出芽释放。实验表明，TSG101是病毒出芽的关键宿主因子。
2. **文献名称**：*Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding*
**作者**：Garrus, J.E., et al.
**摘要**：本文证实TSG101作为ESCRT-I复合体的核心组分，通过重组蛋白实验证明其与HIV-1 Gag蛋白的结合对病毒出芽至关重要，并揭示了ESCRT通路在病毒释放中的保守作用。
3. **文献名称**：*Structural and functional studies of the TSG101-ESCRT-I complex*
**作者**：Kostelansky, M.S., et al.
**摘要**：通过重组表达和纯化TSG101蛋白，结合X射线晶体学解析了ESCRT-I复合体的三维结构，阐明了TSG101与泛素化底物及下游ESCRT组分的分子互作机制。
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这些研究利用重组TSG101蛋白，分别在病毒学、细胞生物学和结构生物学领域揭示了其功能机制。如需扩展，可进一步检索涉及TSG101重组蛋白在癌症或膜重塑中的文献。
TSG101 (tumor susceptibility gene 101) is a multifunctional protein involved in key cellular processes, including endosomal sorting, vesicle trafficking, and membrane remodeling. It is a critical component of the ESCRT (Endosomal Sorting Complex Required for Transport) machinery, particularly ESCRT-I, which regulates the sorting of ubiquitinated cargo proteins into multivesicular bodies (MVBs) and facilitates membrane scission during processes like cytokinesis, viral budding, and exosome formation. The protein contains an N-terminal ubiquitin-enhancing variant (UEV) domain that binds ubiquitin, a proline-rich region, and a coiled-coil domain mediating interactions with other ESCRT components. Dysregulation of TSG101 is linked to cancer progression, neurodegenerative disorders, and viral pathogenesis (e.g., HIV-1 budding).
Recombinant TSG101 protein is produced using expression systems like *E. coli* or mammalian cells, enabling controlled studies of its structure and function. Purification typically involves affinity chromatography (e.g., His-tag) followed by size-exclusion chromatography to ensure homogeneity. Researchers use recombinant TSG101 to investigate its role in ubiquitin-dependent cargo sorting, ESCRT assembly, and interactions with viral proteins (e.g., HIV-1 Gag). It also serves as a tool for exploring disease mechanisms, such as disrupted MVB formation in cancer metastasis or impaired autophagy in neurodegeneration. Additionally, recombinant TSG101 supports drug discovery efforts targeting ESCRT-dependent pathways, offering potential therapeutic strategies against viral infections or ESCRT-related pathologies. Its versatility in biochemical assays, structural studies, and cell-based models underscores its importance in both basic and applied biomedical research.
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