| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ZRANB1 |
| Uniprot No | Q9UGI0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-708aa |
| 氨基酸序列 | MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSVCTYENWAKAKRCVVCDHPRPNNIEAIELAETEEASSIINEQDRARWRGSCSSGNSQRRSPPATKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE |
| 预测分子量 | 88.4 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3-4条关于ZRANB1重组蛋白的模拟参考文献(内容基于领域知识模拟，非真实文献)：
1. **文献名称**: "Structural and functional characterization of recombinant ZRANB1 in DNA repair"
**作者**: Chen L, et al.
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组ZRANB1蛋白，通过晶体学分析揭示其锌指结构域与核酸结合的关键位点，并证明其在DNA损伤修复中通过促进同源重组修复通路发挥作用。
2. **文献名称**: "ZRANB1 regulates mRNA splicing via its interaction with the spliceosome"
**作者**: Park S, et al.
**摘要**: 利用哺乳动物细胞系表达重组ZRANB1蛋白，结合免疫共沉淀实验发现其与剪接体核心组分(如U2 snRNP)相互作用，调控前体mRNA的可变剪接，提示ZRANB1在转录后调控中的新功能。
3. **文献名称**: "Recombinant ZRANB1 exhibits endoribonuclease activity dependent on its conserved PIN domain"
**作者**: Gupta R, et al.
**摘要**: 通过体外酶活实验证实重组ZRANB1蛋白的PIN结构域具有位点特异性内切核糖核酸酶活性，可切割特定RNA底物，为解析其在RNA代谢和病毒防御中的机制提供依据。
4. **文献名称**: "ZRANB1 recruits USP9X to stabilize BRCA1 in genomic stability maintenance"
**作者**: Wang Y, et al.
**摘要**: 研究利用重组ZRANB1蛋白进行体外泛素化实验，证明其通过结合去泛素化酶USP9X调控BRCA1蛋白稳定性，从而维持基因组完整性，为癌症治疗提供潜在靶点。
(注：以上文献为模拟生成，实际研究中请以真实数据库检索结果为准。)
ZRANB1 (Zinc Finger RANBP2-Type Containing 1), also known as TRABID, is a ubiquitin-binding protein implicated in regulating cellular processes such as DNA damage response, cell cycle progression, and transcriptional regulation. It belongs to the ovarian tumor (OTU) domain-containing deubiquitinase family, characterized by its ability to cleave ubiquitin chains with distinct linkage specificities. Structurally, ZRANB1 contains an N-terminal OTU domain responsible for its deubiquitinating activity, followed by three zinc finger motifs (RanBP2-type) that mediate protein-protein interactions and subcellular localization. Additionally, it harbors a nuclear localization signal, aligning with its role in nuclear processes.
ZRANB1 interacts with key regulatory proteins, including RAN (a GTPase involved in nucleocytoplasmic transport), components of the DNA repair machinery, and transcription factors. Its deubiquitinase activity targets K29- and K33-linked polyubiquitin chains, modulating substrate stability or signaling pathways. Studies suggest ZRANB1 influences Wnt/β-catenin signaling by deubiquitinating β-catenin, impacting cell proliferation and differentiation. It also participates in resolving DNA replication stress by regulating the Fanconi anemia pathway. Dysregulation of ZRANB1 has been linked to cancers, neurodegenerative disorders, and immune responses, highlighting its therapeutic potential.
Recombinant ZRANB1 protein, typically produced in bacterial or mammalian expression systems with affinity tags (e.g., His or GST), retains enzymatic activity and is widely used in biochemical assays, structural studies, and drug discovery. Its applications include elucidating ubiquitin-dependent signaling mechanisms, screening deubiquitinase inhibitors, and exploring its role in disease pathogenesis.
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