| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ZNF599 |
| Uniprot No | Q96NL3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-588 aa |
| 活性数据 | MAAPALALVSFEDVVVTFTGEEWGHLDLAQRTLYQEVMLETCRLLVSLGHPVPKPELIYLLEHGQELWTVKRGLSQSTCAGEKAKPKITEPTASQLAFSEESSFQELLAQRSSRDSRLGQARDEEKLIKIQEGNLRPGTNPHKEICPEKLSYKHDDLEPDDSLGLRVLQERVTPQDALHECDSQGPGKDPMTDARNNPYTCTECGKGFSKKWALVRHQQIHAGVKPYECNECGKACRYMADVIRHMRLHTGEKPYKCIECGKAFKRRFHLTEHQRIHTGDKPYECKECGKAFTHRSSFIQHNMTHTREKPFLCKECGKAFYYSSSFAQHMRIHTGKKLYECGECGKAFTHRSTFIQHNVTHTGEKPFLCKECGKTFCLNSSFTQHMRIHTGEKPYECGECGKAFTHRSTFIRHKRTHTGEKPFECKECGKAFCDSSSLIQHMRIHTGEKPYECSECGKAFTHHSVFIRHNRTHSGQKPLECKECAKAFYYSSSFTRHMRIHTGEKPYVCRECGKAFTQPANFVRHNRIHTGEKPFECKECEKAFCDNFALTQHMRTHTGEKPFECNECGKTFSHSSSFTHHRKIHTRV |
| 分子量 | 93.9 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. |
以下是几篇关于重组人ZNF599蛋白的虚构参考文献(基于领域知识推测，非真实存在，供参考)：
---
1. **文献名称**: *ZNF599 regulates transcriptional networks in cancer cells through KRAB domain-mediated chromatin remodeling*
**作者**: Zhang L, et al.
**摘要**: 本研究首次报道了重组ZNF599蛋白通过其KRAB结构域招募染色质修饰复合物，抑制致癌基因(如MYC)的转录活性。通过CRISPR筛选和ChIP-seq分析，发现ZNF599在抑制肝癌细胞增殖中起关键作用。
---
2. **文献名称**: *Crystal structure of the zinc finger domain of human ZNF599 reveals DNA-binding specificity*
**作者**: Wang Y, et al.
**摘要**: 本研究解析了ZNF599蛋白锌指结构域的X射线晶体结构(分辨率2.1Å)，揭示其通过第2-4指状结构与富含GC的DNA序列结合。体外实验表明重组ZNF599可调控p53信号通路相关基因的启动子活性。
---
3. **文献名称**: *ZNF599 interacts with ubiquitin-specific protease 7 (USP7) and modulates protein stability in neurodegenerative pathways*
**作者**: Liu X, et al.
**摘要**: 通过酵母双杂交筛选，发现重组ZNF599蛋白与去泛素化酶USP7直接相互作用。实验表明，ZNF599通过调控Tau蛋白的泛素化水平影响其稳定性，提示其在阿尔茨海默病中的潜在病理作用。
---
4. **文献名称**: *High-throughput production of recombinant ZNF599 in E. coli and functional analysis of its splice variants*
**作者**: Chen H, et al.
**摘要**: 本研究优化了ZNF599在大肠杆菌中的可溶性表达条件(产率~15 mg/L)，发现其剪切变体Δexon3失去核定位能力。通过RNA干扰证实全长ZNF599对细胞周期G1/S期转换具有抑制作用。
---
**注**：以上文献为模拟示例，真实文献请通过PubMed、Google Scholar等平台以“ZNF599”或“zinc finger protein 599”为关键词检索。如需具体文献协助，建议补充蛋白功能方向(如癌症、神经疾病等)。
Zinc finger protein 599 (ZNF599) is a member of the zinc finger protein family, characterized by conserved Cys₂His₂ (C2H2)-type zinc finger domains that mediate sequence-specific DNA or RNA interactions. As a transcription factor, it is hypothesized to play regulatory roles in gene expression, though its precise biological functions remain under investigation. ZNF599 is encoded in humans by the ZNF599 gene located on chromosome 19 (19q13.43), and its expression has been detected in various tissues, suggesting potential involvement in diverse cellular processes.
Recombinant human ZNF599 protein is typically produced using heterologous expression systems, such as E. coli or mammalian cell lines, enabling in vitro studies of its molecular interactions and functional mechanisms. Structural studies emphasize its modular zinc finger array, which may facilitate binding to specific nucleic acid motifs. Emerging evidence links ZNF599 to cellular differentiation pathways and stress response systems, with preliminary associations to cancer progression and neurological disorders reported in some omics datasets. Its recombinant form is particularly valuable for biochemical assays (e.g., electrophoretic mobility shift assays), protein interaction mapping, and mechanistic studies exploring zinc finger-mediated gene regulation. Current research focuses on elucidating its target genes, post-translational modifications, and potential therapeutic relevance in diseases involving transcriptional dysregulation. However, functional annotations remain incomplete, underscoring the need for further characterization of this understudied protein.
×
