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Recombinant Human ZNF592 protein

  • 中文名: 锌指蛋白592(ZNF592)重组蛋白
  • 别    名: ZNF592;KIAA0211;Zinc finger protein 592
货号: PA2000-3591
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ZNF592
Uniprot No Q92610
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-242aa
氨基酸序列MGDMKTPDFDDLLAAFDIPDPTSLDAKEAIQTPSEENESPLKPPGICMDESVSLSHSGSAPDVPAVSVIVKNTSRQESFEAEKDHITPSLLHNGFRGSDLPPDPHNCGKFDSTFMNGDSARSFPGKLEPPKSEPLPTFNQFSPISSPEPEDPIKDNGFGIKPKHSDSYFPPPLGCGAVGGPVLEALAKFPVPELHMFDHFCKKEPKPEPLPLGSQQEHEQSGQNTVEPHKDPDATRFFGEAL
预测分子量 53.2 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.

参考文献

以下是关于ZNF592重组蛋白的示例参考文献(内容为虚构示例,仅供格式参考):

1. **《Cloning and expression of human ZNF592 in E. coli》**

- 作者:Cieply, A. et al.

- 摘要:研究报道了ZNF592基因的克隆策略,通过大肠杆菌系统高效表达重组蛋白,并验证其DNA结合活性。

2. **《ZNF592 mutations disrupt protein stability in neurodevelopmental disorders》**

- 作者:Hahn, Y. & Neubauer, G.

- 摘要:通过重组ZNF592蛋白功能实验,揭示其突变导致蛋白构象异常,与CAGI综合征的致病机制相关。

3. **《Structural analysis of ZNF592 zinc finger domains by X-ray crystallography》**

- 作者:Zhang, Q. et al.

- 摘要:解析了重组ZNF592蛋白的锌指结构域三维结构,阐明其与特定DNA序列结合的分子基础。

4. **《Recombinant ZNF592 as a diagnostic marker for genetic screening》**

- 作者:Johnson, R.L. et al.

- 摘要:开发基于重组ZNF592蛋白的ELISA检测技术,用于快速筛查与智力障碍相关的基因突变。

(注:以上文献为模拟内容,实际研究中请通过PubMed/Google Scholar检索真实文献。)

背景信息

The ZNF592 protein, encoded by the ZNF592 gene, belongs to the zinc finger protein family characterized by conserved C2H2-type zinc finger motifs that mediate sequence-specific DNA or RNA interactions. This nuclear protein is implicated in transcriptional regulation, though its precise biological roles remain under active investigation. It has been linked to developmental processes and neurological functions, with mutations in ZNF592 associated with congenital disorders such as mild intellectual disability and cerebellar hypoplasia. Notably, pathogenic variants are reported in individuals with autosomal recessive spinocerebellar ataxia (SCAR16), suggesting its critical role in neuronal maintenance.

Recombinant ZNF592 protein is typically produced using heterologous expression systems (e.g., E. coli, mammalian cells) to enable functional and structural studies. The recombinant form often includes epitope tags (HA, FLAG, or His-tag) for purification and detection. Structural studies reveal multiple zinc finger domains arranged in tandem, supporting its potential as a nucleic acid-binding protein. Researchers employ this recombinant tool to investigate its interaction partners, DNA/RNA binding specificity, and post-translational modifications.

Current research focuses on elucidating ZNF592's role in gene regulatory networks, particularly in neurodevelopment and chromatin remodeling. Its recombinant version facilitates in vitro assays (EMSA, pull-downs), cellular localization studies, and disease modeling. Pharmaceutical interest emerges from its potential as a biomarker or therapeutic target for ZNF592-related neuropathies. However, challenges persist in fully characterizing its molecular targets and regulatory mechanisms, highlighting the need for continued investigation using recombinant protein-based approaches.

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