| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ZNF2 |
| Uniprot No | Q9BSG1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-426aa |
| 氨基酸序列 | MAAVSPTTRC QESVTFEDVA VVFTDEEWSR LVPIQRDLYK EVMLENYNSI VSLGLPVPQP DVIFQLKRGD KPWMVDLHGS EEREWPESVS LDWETKPEIH DASDKKSEGS LRECLGRQSP LCPKFEVHTP NGRMGTEKQS PSGETRKKSL SRDKGLRRRR SALSREILTK ERHQECSDCG KTFFDHSSLT RHQRTHTGEK PYDCRECGKA FSHRSSLSRH LMSHTGESPY ECSVCSKAFF DRSSLTVHQR IHTGEKPFQC NECGKAFFDR SSLTRHQRIH TGESPYECHQ CGKAFSQKSI LTRHQLIHTG RKPYECNECG KAFYGVSSLN RHQKAHAGDP RYQCNECGKA FFDRSSLTQH QKIHTGDKPY ECSECGKAFS QRCRLTRHQR VHTGEKPFEC TVCGKVFSSK SSVIQHQRRY AKQGID |
| 预测分子量 | 48,7 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ZNF2重组蛋白的示例参考文献(内容为虚构，仅供格式参考，建议通过学术数据库获取真实文献)：
---
1. **文献名称**: *Cloning and Functional Characterization of Recombinant ZNF2 Protein in E. coli*
**作者**: Zhang L, et al.
**摘要**: 本研究成功构建了ZNF2基因的原核表达载体，并在大肠杆菌中高效表达可溶性重组ZNF2蛋白。通过亲和层析纯化后，证实该蛋白具有结合特定DNA序列的能力，为后续功能研究奠定基础。
2. **文献名称**: *ZNF2 Recombinant Protein Promotes Neural Stem Cell Differentiation via Epigenetic Regulation*
**作者**: Chen Y, Wang X.
**摘要**: 通过体外实验发现，纯化的重组ZNF2蛋白能够通过调控组蛋白修饰(如H3K9me3)，激活神经分化相关基因表达，提示其在神经干细胞定向分化中的潜在应用价值。
3. **文献名称**: *Structural Insights into the Zinc Finger Domains of ZNF2 by Cryo-EM*
**作者**: Gupta R, et al.
**摘要**: 本研究利用冷冻电镜解析了ZNF2重组蛋白的三维结构，揭示了其锌指结构域与DNA结合的分子机制，为设计基于ZNF2的基因编辑工具提供结构基础。
---
**建议**：通过PubMed、Google Scholar等平台，以“ZNF2 recombinant protein”“Zinc Finger Protein 2 expression”为关键词检索最新文献，或查阅《Journal of Molecular Biology》《Protein Expression and Purification》等期刊获取真实数据。
The ZNF2 recombinant protein is derived from the zinc finger protein 2 (ZNF2), a member of the zinc finger protein family characterized by conserved Cys2-His2 (C2H2) zinc finger domains. These domains enable sequence-specific DNA binding, positioning ZNF2 as a potential transcriptional regulator involved in diverse cellular processes, including gene expression modulation, cell differentiation, and development. The ZNF2 gene is evolutionarily conserved across species, underscoring its functional significance in maintaining genomic stability and cellular homeostasis.
Recombinant ZNF2 is typically produced using prokaryotic or eukaryotic expression systems, such as E. coli or mammalian cell lines, to ensure proper folding and post-translational modifications. Its production often involves codon optimization, affinity tags (e.g., His-tag), and purification techniques like immobilized metal ion chromatography. This engineered protein retains the DNA-binding capacity and structural integrity of the native protein, making it valuable for functional studies.
Research on ZNF2 has linked it to roles in neurodevelopment, cancer progression, and epigenetic regulation. For instance, studies suggest its involvement in neural stem cell differentiation and tumor suppression, potentially through interactions with chromatin-modifying enzymes or specific gene promoters. Dysregulation of ZNF2 has been observed in certain cancers, hinting at its dual role as an oncogene or tumor suppressor depending on cellular context.
The recombinant ZNF2 protein serves as a critical tool for in vitro assays, including electrophoretic mobility shift assays (EMSA), chromatin immunoprecipitation (ChIP), and high-throughput screening for drug discovery. Its applications extend to gene therapy and synthetic biology, where engineered zinc finger domains are leveraged for targeted genome editing. Ongoing studies aim to elucidate its precise molecular mechanisms and therapeutic potential in diseases associated with transcriptional dysregulation.
×
