| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRIM5 |
| Uniprot No | Q9C035 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-493aa |
| 氨基酸序列 | MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDK GESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGE KLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLR QKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNEL QNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGV DGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVD VTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILG SQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYW VIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVS FFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS |
| 预测分子量 | 70 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. |
1. **"The cytoplasmic body component TRIM5α restricts HIV-1 infection in Old World monkeys"**
*作者*: Stremlau, M. et al. (2004), *Nature*
*摘要*: 该研究首次阐明恒河猴TRIM5α蛋白通过直接结合HIV-1衣壳蛋白，抑制病毒在宿主细胞内的复制，揭示了TRIM家族蛋白在天然抗逆转录病毒免疫中的作用。
2. **"Structure of the amino-terminal domain of human TRIM5α suggests a mechanism for recognition of retroviral capsids"**
*作者*: Sebastian, S. & Luban, J. (2008), *PNAS*
*摘要*: 通过重组人TRIM5α蛋白的晶体结构分析，揭示了其N端结构域(B30.2/SPRY)与不同逆转录病毒衣壳特异性结合的结构基础，解释了物种间限制性差异的分子机制。
3. **"TRIM5 is an innate immune sensor for the retrovirus capsid lattice"**
*作者*: Ganser-Pornillos, B.K. et al. (2011), *Nature*
*摘要*: 利用重组TRIM5α蛋白体外实验，证明其通过识别病毒衣壳的晶格结构触发泛素化信号通路，激活先天免疫反应，揭示了TRIM5α在抗病毒防御中的双重功能(直接抑制与免疫激活)。
4. **"Engineering human TRIM5α to accelerate viral disassembly and restore anti-HIV activity"**
*作者*: Goldstone, D.C. et al. (2010), *Cell Host & Microbe*
*摘要*: 通过重组TRIM5α的突变体构建，发现优化其与HIV衣壳的结合能力可显著增强病毒衣壳的早熟解体，为基于TRIM5的基因治疗策略提供实验依据。
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以上文献涵盖TRIM5α的抗病毒机制、结构功能解析及工程化应用，均为该领域的奠基性或关键技术研究。
TRIM5 (Tripartite motif-containing protein 5) is a member of the TRIM family of proteins, known for their roles in innate immunity, antiviral defense, and cellular regulation. It gained prominence for its ability to restrict retroviral infections, particularly HIV-1. in a species-specific manner. The protein contains characteristic N-terminal domains: a RING domain with E3 ubiquitin ligase activity, one or two B-box domains, and a coiled-coil region that mediates oligomerization. Its C-terminal domain, often a SPRY (or PRY-SPRY) region, determines viral capsid recognition specificity.
TRIM5α, a major isoform, acts as a cytoplasmic restriction factor by directly binding to incoming retroviral capsids, triggering their premature disassembly and blocking reverse transcription. This interaction also activates innate immune signaling pathways, amplifying antiviral responses. Species variations in TRIM5α’s SPRY domain explain differences in viral susceptibility; for example, rhesus macaque TRIM5α effectively inhibits HIV-1. while human TRIM5α shows weaker activity against HIV-1 but restricts other retroviruses.
Recombinant TRIM5 proteins are engineered for studies on host-pathogen interactions, structural analysis of capsid recognition, and mechanisms of immune activation. They serve as tools to dissect how TRIM5 oligomerizes, ubiquitinates viral components, or recruits effectors like autophagy adaptors. Modified versions, including chimeric proteins or mutants, help identify functional domains or enhance antiviral properties for therapeutic exploration.
Research on TRIM5 has implications for understanding viral evolution, cross-species transmission barriers, and developing gene-based antiviral strategies. Its recombinant forms are pivotal in screens for capsid-targeting drugs and in designing synthetic restriction factors, highlighting its dual role as a model system for innate immunity and a potential biotherapeutic scaffold.
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