| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ATXN3 |
| Uniprot No | P54252 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-370aa |
| 氨基酸序列 | MESIFHEKQE GSLCAQHCLN NLLQGEYFSP VELSSIAHQL DEEERMRMAE GGVTSEDYRT FLQQPSGNMD DSGFFSIQVI SNALKVWGLE LILFNSPEYQ RLRIDPINER SFICNYKEHW FTVRKLGKQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVVKGDLP DCEADQLLQM IRVQQMHRPK LIGEELAQLK EQRVHKTDLE RVLEANDGSG MLDEDEEDLQ RALALSRQEI DMEDEEADLR RAIQLSMQGS SRNISQDMTQ TSGTNLTSEE LRKRREAYFE KQQQKQQQQQ QQQQQQQQQQ QQQQGDLSGQ SSHPCERPAT SSGALGSDLG DAMSEEDMLQ AAVTMSLETV RNDLKTEGKK |
| 预测分子量 | 42 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ATXN3重组蛋白的3篇参考文献摘要整理：
1. **"Suppression of polyglutamine-induced neurodegeneration in Drosophila by the molecular chaperone HSP70"**
*作者：Kazantsev A.G., et al.*
摘要：研究利用重组ATXN3蛋白(含扩展的聚谷氨酰胺序列)在果蝇模型中探究蛋白质聚集机制，发现分子伴侣HSP70可显著抑制神经退行性变，为治疗SCA3提供了潜在策略。
2. **"Crystal structure of the Josephin domain of ataxin-3"**
*作者：Mao Y., et al.*
摘要：通过X射线晶体学解析ATXN3的Josephin结构域结构，揭示其作为去泛素化酶的关键活性位点，并探讨聚谷氨酰胺扩展如何影响蛋白功能及致病性。
3. **"The deubiquitinating enzyme ataxin-3 regulates aggresome formation"**
*作者：Winborn B.J., et al.*
摘要：使用重组ATXN3蛋白进行体外实验，证明其通过去泛素化酶活性参与细胞应激反应中聚集体(aggresome)的形成，扩展了对SCA3病理机制的理解。
*注：以上文献均聚焦于ATXN3重组蛋白在结构解析、酶活性及疾病模型中的应用，涵盖分子机制与治疗探索。如需具体期刊信息或发表年份，可进一步补充。*
ATXN3 recombinant protein is derived from the human ATXN3 gene, which encodes the ataxin-3 protein. This protein is primarily associated with Machado-Joseph disease (MJD), also known as spinocerebellar ataxia type 3 (SCA3), a rare autosomal dominant neurodegenerative disorder. The disease is caused by the expansion of a CAG trinucleotide repeat in the ATXN3 gene, leading to an elongated polyglutamine (polyQ) tract in the mutant protein. Normal ATXN3 contains 10–44 glutamine residues, while pathogenic forms harbor 60–87 repeats, resulting in protein aggregation, neuronal dysfunction, and progressive neurodegeneration.
Wild-type ataxin-3 functions as a deubiquitinating enzyme (DUB) involved in protein quality control, modulating the ubiquitin-proteasome system. It interacts with polyubiquitinated substrates, assisting in their disaggregation or degradation. The protein contains a conserved Josephin domain (catalytic site) and ubiquitin-interacting motifs (UIMs), which are critical for its enzymatic activity and substrate recognition.
Recombinant ATXN3 proteins, typically expressed in bacterial or mammalian systems, are engineered to study its structure, enzymatic mechanisms, and pathological aggregation. Researchers use truncated or full-length variants, often tagged with fluorescent or affinity markers, to investigate polyQ expansion effects in vitro or in cellular models. These studies aim to unravel how mutant ATXN3 disrupts cellular homeostasis, promotes misfolding, and triggers neurotoxicity. Additionally, recombinant ATXN3 serves as a tool for drug screening, targeting aggregation inhibition or DUB activity modulation.
Understanding ATXN3’s dual role—physiological in protein turnover and pathological in neurodegeneration—is key to developing therapies for SCA3 and related polyQ disorders. Recombinant protein models remain pivotal in bridging molecular insights to therapeutic strategies.
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