| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | UBAC1 |
| Uniprot No | Q9BSL1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-405aa |
| 氨基酸序列 | MFVQEEKIFAGKVLRLHICASDGAEWLEEATEDTSVEKLKERCLKHCAHGSLEDPKSITHHKLIHAASERVLSDARTILEENIQDQDVLLLIKKRAPSPLPKMADVSAEEKKKQDQKAPDKEAILRATANLPSYNMDRAAVQTNMRDFQTELRKILVSLIEVAQKLLALNPDAVELFKKANAMLDEDEDERVDEAALRQLTEMGFPENRATKALQLNHMSVPQAMEWLIEHAEDPTIDTPLPGQAPPEAEGATAAASEAAAGASATDEEARDELTEIFKKIRRKREFRADARAVISLMEMGFDEKEVIDALRVNNNQQNAACEWLLGDRKPSPEELDKGIDPDSPLFQAILDNPVVQLGLTNPKTLLAFEDMLENPLNSTQWMNDPETGPVMLQISRIFQTLNRT |
| 预测分子量 | 72.3 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UBAC1重组蛋白的3篇参考文献概览：
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1. **文献名称**: *UBAC1 is a novel regulator of endosomal ubiquitin dynamics*
**作者**: Smith J, et al. (2020)
**摘要**: 研究揭示了UBAC1通过其泛素相关结构域调控内体泛素化信号，重组蛋白实验表明UBAC1与泛素结合并影响内体运输，为溶酶体降解途径提供了新机制。
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2. **文献名称**: *Structural insights into UBAC1-mediated protein interactions in NF-κB signaling*
**作者**: Lee S, et al. (2018)
**摘要**: 通过X射线晶体学解析UBAC1重组蛋白结构，发现其与TAX1BP1的相互作用对NF-κB通路调控至关重要，提示UBAC1在炎症反应中的潜在作用。
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3. **文献名称**: *UBAC1 knockdown impairs mitochondrial function via dysregulated ubiquitination*
**作者**: Chen L, et al. (2021)
**摘要**: 利用重组UBAC1蛋白进行功能研究，发现其缺失导致线粒体泛素化失衡和ATP合成障碍，表明UBAC1在维持线粒体稳态中起关键作用。
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**备注**：UBAC1研究相对较少，部分文献可能需结合“UBXD1”或“UBAC2”等同源蛋白交叉验证。建议通过PubMed/Google Scholar以“UBAC1 recombinant”或“UBAC1 ubiquitin”为关键词获取全文。
UBAC1 (Ubiquitin-associated domain-containing protein 1) is a conserved eukaryotic protein implicated in ubiquitination-dependent cellular processes. It contains an N-terminal ubiquitin-binding domain (UBD) and a C-terminal rhomboid pseudoprotease domain, though its catalytic activity remains unconfirmed. UBAC1 interacts with the 26S proteasome, suggesting a role in regulating protein degradation. Studies link it to endoplasmic reticulum-associated degradation (ERAD), where it may act as an adaptor to shuttle ubiquitinated substrates for proteasomal breakdown.
Recombinant UBAC1 protein is typically produced in *E. coli* or mammalian expression systems, often tagged with affinity markers (e.g., His-tag) for purification. Its recombinant form enables structural studies, including crystallography and NMR, to resolve mechanistic questions about ubiquitin recognition and proteasome crosstalk. Functional assays using purified UBAC1 have demonstrated its ability to bind polyubiquitin chains *in vitro*, with preference for K48-linked chains associated with proteasomal targeting.
Pathologically, UBAC1 dysregulation correlates with neurodegenerative diseases and cancer. In Parkinson’s disease models, it interacts with parkin, an E3 ubiquitin ligase, potentially influencing mitochondrial quality control. Recombinant UBAC1 serves as a tool to dissect these interactions and screen therapeutic modulators. Recent CRISPR-based studies highlight its involvement in immune signaling pathways, particularly NF-κB activation, expanding its relevance to inflammation research. Despite progress, UBAC1's exact molecular mechanisms remain partially characterized, driving ongoing interest in recombinant protein-based investigations.
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