| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ZRANB2 |
| Uniprot No | O95218 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-320aa |
| 氨基酸序列 | MSTKNFRVSDGDWICPDKKCGNVNFARRTSCNRCGREKTTEAKMMKAGGTEIGKTLAEKSRGLFSANDWQCKTCSNVNWARRSECNMCNTPKYAKLEERTGYGGGFNERENVEYIEREESDGEYDEFGRKKKKYRGKAVGPASILKEVEDKESEGEEEDEDEDLSKYKLDEDEDEDDADLSKYNLDASEEEDSNKKKSNRRSRSKSRSSHSRSSSRSSSPSSSRSRSRSRSRSSSSSQSRSRSSSRERSRSRGSKSRSSSRSHRGSSSPRKRSYSSSSSSPERNRKRSRSRSSSSGDRKKRRTRSRSPESQVIGENTKQP |
| 预测分子量 | 52.3 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ZRANB2重组蛋白的3篇参考文献的简要总结：
1. **文献名称**：*Structural and functional analysis of the ZRANB2 splicing factor*
**作者**：Smith A, Jones B, et al.
**摘要**：该研究解析了重组ZRANB2蛋白的晶体结构，揭示了其RNA结合结构域的关键氨基酸残基，并通过体外剪接实验证明其在选择性剪接中的调控作用。
2. **文献名称**：*ZRANB2 interacts with spliceosomal components via recombinant protein pull-down assays*
**作者**：Chen L, Wang H, et al.
**摘要**：通过重组ZRANB2蛋白的亲和层析实验，发现其与U2AF35等剪接体蛋白直接互作，提示其在pre-mRNA加工中的协同调控机制。
3. **文献名称**：*Recombinant ZRANB2 expression in E. coli and its role in cellular stress response*
**作者**：Kim S, Park J, et al.
**摘要**：报道了在大肠杆菌中高效表达可溶性重组ZRANB2蛋白的方法，并证明其在氧化应激条件下通过调控靶基因可变剪接影响细胞存活。
注：以上文献信息为模拟示例，实际引用需查询具体数据库(如PubMed)获取真实文献。
ZRANB2 (Zinc Finger RanBP2-Type Containing 2), also known as ZIS2 or ZNF462. is a protein-coding gene implicated in RNA processing and cellular regulation. It belongs to the zinc finger protein family, characterized by conserved RanBP2-type zinc finger domains that mediate RNA binding and protein-protein interactions. Structurally, ZRANB2 contains an N-terminal arginine/serine-rich (RS) domain, which is common in splicing factors, and two tandem RanBP2-type zinc finger motifs. These domains suggest roles in RNA metabolism, including splicing, stability, or transport.
Recombinant ZRANB2 protein is engineered for in vitro studies to dissect its molecular functions. Produced via bacterial or mammalian expression systems, it retains key functional domains for experimental analyses. Research highlights its involvement in alternative splicing regulation by interacting with components of the spliceosome. It may act as a scaffold or modulator, linking RNA targets to splicing machinery. Additionally, ZRANB2 interacts with proteins involved in transcription (e.g., PPARγ) and DNA damage response pathways, hinting at broader regulatory roles.
Dysregulation of ZRANB2 is associated with diseases, including cancers and neurological disorders. Recombinant ZRANB2 facilitates mechanistic studies—such as RNA-binding assays, protein interaction mapping, or structural analyses—to explore its pathological relevance. Its role in RNA processing also makes it a potential target for therapeutic interventions. Current research focuses on elucidating its precise molecular targets, post-translational modifications, and crosstalk with signaling pathways. Overall, recombinant ZRANB2 serves as a critical tool for unraveling its biological significance in health and disease.
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