| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Trim2 |
| Uniprot No | D3ZQG6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-744aa |
| 氨基酸序列 | MASEGASIPSPVVRQIDKQFLICSICLERYKNPKVLPCLHTFCERCLQNYIPAHSLTLSCPVCRQTSILPEKGVAALQNNFFITNLMDVLQRTPGSNGEDPSILQTVTAVAAGKPLSCPNHDGNVMEFYCQSCETAMCRECTEGEHAEHPTVPLKDVVEQHKASLQVQLDAVNKRLPEIDSALQFISEIIHQLTNQKASIVDDIHSTFDELQKTLNVRKSVLLMELEVNYGLKHKVLQSQLDTLLQGQESIKSCSNFTAQALNHGTETEVLLVKKQMSEKLNELADQDFPLHPRENDQLDFIVETEGLKKSIHNLGTILTTNAVASETVATGEGLRQTIIGQPMSVTITTKDKDGELCKTGNAYLTAELSTPDGSVADGEILDNKNGTYEFLYTVQKEGDFTLSLRLYDQHIRGSPFKLKVIRSADVSPTTEGVKRRVKSPGSGHVKQKAVKRPASMYSTGKRKENPIEDDLIFRVGTKGRNKGEFTNLQGVAASTSGKILIADSNNQCVQIFSNDGQFKSRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSNDGKFKTKIGSGKLMGPKGVSVDRNGHIIVVDNKACCVFIFQPNGKIVTRFGSRGNGDRQFAGPHFAAVNSSNEIIITDFHNHSVKVFNQEGEFMLKFGSNGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDGSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ |
| 预测分子量 | 85.5 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 **Trim2重组蛋白** 的3-4篇参考文献示例(部分为模拟文献，实际文献需根据具体数据库检索)：
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1. **文献名称**: *Structural and Functional Analysis of TRIM2 Reveals Its Ubiquitin Ligase Activity*
**作者**: Smith J, et al.
**摘要**: 本研究解析了Trim2重组蛋白的晶体结构，发现其通过RING结构域介导泛素化反应，并证实其在神经细胞中参与错误折叠蛋白的降解通路。
2. **文献名称**: *TRIM2 Regulates Axonal Transport and Neurodegeneration in Charcot-Marie-Tooth Disease*
**作者**: Johnson L, et al.
**摘要**: 通过体外重组Trim2蛋白实验和基因敲除模型，证明Trim2通过调控微管稳定性维持轴突运输功能，其缺失可导致周围神经病变(如CMT疾病)。
3. **文献名称**: *Recombinant TRIM2 Protein Attenuates Tau Aggregation in Alzheimer’s Disease Models*
**作者**: Lee S, et al.
**摘要**: 利用重组Trim2蛋白处理阿尔茨海默病小鼠模型，发现其通过促进Tau蛋白的泛素化-蛋白酶体降解途径，显著减少神经纤维缠结。
4. **文献名称**: *TRIM Family Proteins in Cellular Quality Control: Focus on TRIM2 Applications*
**作者**: García-Sánchez M, et al.
**摘要**: 综述TRIM家族蛋白(包括Trim2)在细胞质量控制中的作用，强调重组Trim2在治疗神经退行性疾病和癌症中的潜在应用价值。
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如需真实文献，建议在 **PubMed** 或 **Web of Science** 中检索关键词：*"Trim2 recombinant protein"、"TRIM2 ubiquitination"、"TRIM2 neurodegeneration"*。
Trim2 (Tripartite Motif-containing protein 2) is a member of the TRIM protein family, characterized by a conserved tripartite motif comprising a RING domain, one or two B-box domains, and a coiled-coil region. Primarily expressed in the nervous system, Trim2 functions as an E3 ubiquitin ligase, mediating protein ubiquitination—a critical post-translational modification regulating protein degradation, trafficking, and signaling. It plays a key role in maintaining neuronal health, particularly in axonal homeostasis and vesicle transport. Trim2 interacts with microtubule-associated proteins, such as neurofilaments, to regulate their turnover and prevent abnormal aggregation, a process vital for preventing neurodegeneration.
Studies link Trim2 mutations to Charcot-Marie-Tooth disease type 2R (CMT2R), a peripheral neuropathy characterized by axonal degeneration. Loss-of-function mutations disrupt Trim2's ability to ubiquitinate misfolded proteins, leading to toxic accumulations that impair axonal integrity. Additionally, Trim2 is implicated in other neurodegenerative conditions, including amyotrophic lateral sclerosis (ALS) and traumatic brain injury, where its dysfunction exacerbates protein aggregation and neuronal damage.
Recombinant Trim2 proteins are engineered for *in vitro* and *in vivo* studies to dissect its molecular mechanisms, substrate specificity, and therapeutic potential. These tools enable researchers to explore Trim2's role in ubiquitination cascades, screen for modulators of its E3 ligase activity, and develop targeted therapies for neurodegenerative diseases. The protein’s structural domains, particularly the RING domain, are also studied for designing inhibitors or stabilizers to fine-tune its function in disease contexts. Overall, Trim2 represents a critical target for understanding and treating disorders rooted in protein homeostasis imbalances.
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