| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ZNF630 |
| Uniprot No | Q2M218 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-657 aa |
| 活性数据 | MIESQEPVTFEDVAVDFTQEEWQQLNPAQKTLHRDVMLETYNHLVSVGCSGIKPDVIFKLEHGKDPWIIESELSRWIYPDRVKGLESSQQIISGELLFQREILERAPKDNSLYSVLKIWHIDNQMDRYQGNQDRVLRQVTVISRETLTDEMGSKYSAFGKMFNRCTDLAPLSQKFHKFDSCENSLKSNSDLLNYNRSYARKNPTKRFRCGRPPKYNASCSVPEKEGFIHTGMEPYGDSQCEKVLSHKQAHVQYKKFQAREKPNVCSMCGKAFIKKSQLIIHQRIHTGEKPYVCGDCRKAFSEKSHLIVHQRIHTGEKPYECTKYGRAFSRKSPFTVHQRVHTGEKPYECFECPKAFSQKSHLIIHQRVHTREKPFECSECRKAFCEMSHLFIHQITHTGKKPYECTECGKTFPRKTQLIIHQRTHTGEKPYKCGECGKTFCQQSHLIGHQRIHTGEKPYVCTDCGKAFSQKSHLTGHQRLHTGEKPYMCTECGKSFSQKSPLIIHQRIHTGEKPYQCGECGKTFSQKSLLIIHLRVHTGEKPYECTECGRAFSLKSHLILHQRGHTGEKPYECSECGKAFCGKSPLIIHQKTHPREKTPECAESGMTFFWKSQMITYQRRHTGEKPSRCSDCGKAFCQHVYFTGHQNPYRKDTLYIC |
| 分子量 | 72.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 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. |
以下提供的文献为根据ZNF630蛋白研究领域常见方向的假设性示例(实际文献可能需要通过学术数据库确认)：
1. **文献名称**：*Cloning and Functional Analysis of Recombinant Human ZNF630 Protein in DNA Binding*
**作者**：Smith J, et al.
**摘要**：本研究成功在大肠杆菌系统中表达并纯化了重组人ZNF630蛋白，通过电泳迁移率变动实验(EMSA)证实其与特定DNA序列的结合能力，提示其在基因调控中的作用。
2. **文献名称**：*Evolutionary Conservation and Divergence of ZNF630 in Primate Species*
**作者**：Brown K, et al.
**摘要**：作者通过重组ZNF630蛋白的多物种比对实验，揭示了该蛋白在灵长类进化中的结构保守性及功能分化，指出其可能参与物种特异性转录调控通路。
3. **文献名称**：*ZNF630 Overexpression Promotes Tumor Cell Apoptosis via p53 Signaling Pathway*
**作者**：Li X, et al.
**摘要**：利用重组ZNF630蛋白体外处理癌细胞，发现其通过激活p53依赖的凋亡通路抑制肿瘤生长，为癌症靶向治疗提供了潜在靶点。
4. **文献名称**：*Structural Characterization of ZNF630 Zinc Finger Domain by X-ray Crystallography*
**作者**：Wang Y, et al.
**摘要**：本研究解析了重组ZNF630蛋白锌指结构域的晶体结构，阐明了其与DNA相互作用的分子机制，为理性设计基因编辑工具提供理论支持。
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**备注**：
- 以上文献为基于研究领域常见主题的假设示例，实际文献需通过PubMed、Web of Science等平台检索关键词“ZNF630 recombinant”或“ZNF630 protein”确认。
- 若该蛋白研究较少，可扩展至锌指蛋白家族(如ZNF3/ZNF7等)或结合功能相似蛋白的文献。
Zinc finger protein 630 (ZNF630) is a member of the zinc finger protein family, characterized by conserved Cys₂His₂-type zinc finger domains that enable sequence-specific DNA binding. It is encoded by the ZNF630 gene located on human chromosome Xp11.3. As a putative transcription factor, ZNF630 is hypothesized to regulate gene expression by interacting with promoter regions of target genes, though its precise biological functions remain incomparatively understudied relative to other zinc finger proteins. Studies suggest potential roles in cellular processes such as differentiation, development, or tumorigenesis, with dysregulation observed in certain cancers. However, detailed mechanisms and physiological targets are still being elucidated.
Recombinant human ZNF630 protein is typically produced using heterologous expression systems, such as E. coli or mammalian cell lines, to enable functional studies. The recombinant form often includes affinity tags (e.g., His-tag) for purification and detection. Structurally, the protein contains multiple tandem zinc finger motifs, each stabilized by zinc ions, which are critical for DNA-binding activity. Research applications include investigating DNA-protein interactions, mapping binding sites via electrophoretic mobility shift assays (EMSA), and exploring its regulatory networks. Recent efforts have utilized CRISPR-based knockout models and transcriptomic analyses to identify candidate target genes and associated pathways. Despite progress, ZNF630's exact role in human health and disease warrants further exploration, particularly its potential as a biomarker or therapeutic target. Current studies emphasize resolving its three-dimensional structure and context-specific interactions within diverse cellular environments.
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