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Recombinant Human ZNF507 Protein

  • 中文名: 重组人(ZNF507)蛋白
  • 别    名: KIAA1084; Zinc finger Protein 507; ZN507_HUMAN; ZNF 507; ZNF507
货号: PAX2000-12899
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ZNF507
Uniprot NoQ8TCN5
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-953 aa
活性数据MEESSSVAMLVPDIGEQEAILTAESIISPSLEIDEQRKTKPDPLIHVIQKLSKIVENEKSQKCLLIGKKRPRSSAATHSLETQELCEIPAKVIQSPAADTRRAEMSQTNFTPDTLAQNEGKAMSYQCSLCKFLSSSFSVLKDHIKQHGQQNEVILMCSECHITSRSQEELEAHVVNDHDNDANIHTQSKAQQCVSPSSSLCRKTTERNETIPDIPVSVDNLQTHTVQTASVAEMGRRKWYAYEQYGMYRCLFCSYTCGQQRMLKTHAWKHAGEVDCSYPIFENENEPLGLLDSSAAAAPGGVDAVVIAIGESELSIHNGPSVQVQICSSEQLSSSSPLEQSAERGVHLSQSVTLDPNEEEMLEVISDAEENLIPDSLLTSAQKIISSSPNKKGHVNVIVERLPSAEETLSQKRFLMNTEMEEGKDLSLTEAQIGREGMDDVYRADKCTVDIGGLIIGWSSSEKKDELMNKGLATDENAPPGRRRTNSESLRLHSLAAEALVTMPIRAAELTRANLGHYGDINLLDPDTSQRQVDSTLAAYSKMMSPLKNSSDGLTSLNQSNSTLVALPEGRQELSDGQVKTGISMSLLTVIEKLRERTDQNASDDDILKELQDNAQCQPNSDTSLSGNNVVEYIPNAERPYRCRLCHYTSGNKGYIKQHLRVHRQRQPYQCPICEHIADNSKDLESHMIHHCKTRIYQCKQCEESFHYKSQLRNHEREQHSLPDTLSIATSNEPRISSDTADGKCVQEGNKSSVQKQYRCDVCDYTSTTYVGVRNHRRIHNSDKPYRCSLCGYVCSHPPSLKSHMWKHASDQNYNYEQVNKAINDAISQSGRVLGKSPGKTQLKSSEESADPVTGSSENAVSSSELMSQTPSEVLGTNENEKLSPTSNTSYSLEKISSLAPPSMEYCVLLFCCCICGFESTSKENLLDHMKEHEGEIVNIILNKDHNTALNTN
分子量132.2 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.


参考文献

以下是针对重组人ZNF507蛋白的模拟参考文献示例(仅供参考,实际文献需结合具体数据库检索):

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1. **文献名称**: *"Recombinant expression and functional characterization of human ZNF507 as a transcriptional repressor"*

**作者**: Zhang L et al.

**摘要**: 本研究成功在大肠杆菌系统中重组表达了人ZNF507蛋白,并通过电泳迁移率实验(EMSA)证实其能特异性结合DNA的GC富集区。进一步细胞实验表明,ZNF507可抑制下游基因的转录活性,提示其可能通过调控靶基因参与肿瘤发生。

2. **文献名称**: *"ZNF507 interacts with HDAC1 to regulate Wnt signaling in colorectal cancer"*

**作者**: Tanaka K et al.

**摘要**: 通过免疫共沉淀(Co-IP)和质谱分析,作者发现重组ZNF507蛋白与组蛋白去乙酰化酶HDAC1存在直接相互作用。敲低ZNF507可激活Wnt通路相关基因表达,表明其在结直肠癌中可能通过表观遗传修饰影响信号通路。

3. **文献名称**: *"Structural analysis of recombinant ZNF507 zinc finger domain reveals DNA-binding motifs"*

**作者**: Smith R et al.

**摘要**: 采用X射线晶体学解析了重组ZNF507锌指结构域的三维结构(分辨率2.1Å),揭示了其独特的氨基酸排列与DNA结合位点特异性,为设计靶向ZNF507的小分子抑制剂提供了结构基础。

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**注意事项**:

- 以上为基于锌指蛋白研究范式的假设性文献,真实研究需通过PubMed、Google Scholar等平台以“ZNF507”、“recombinant protein”等关键词检索。

- 若文献稀缺,建议扩展至ZNF家族(如ZNF替罪因子或癌症相关锌指蛋白)的研究作为背景参考。


背景信息

Zinc finger protein 507 (ZNF507), encoded by the ZNF507 gene in humans, belongs to the large family of C2H2-type zinc finger proteins, which are characterized by conserved zinc-binding motifs involved in DNA binding and protein interactions. These proteins play pivotal roles in transcriptional regulation, chromatin remodeling, and cellular differentiation. ZNF507 contains multiple tandem zinc finger domains, suggesting its potential function as a sequence-specific DNA-binding protein that modulates gene expression. Though its precise biological mechanisms remain understudied, emerging evidence links ZNF507 to cellular processes such as cell cycle control, apoptosis, and nervous system development.

Recent studies have implicated ZNF507 in cancer progression and neurological disorders. For example, altered ZNF507 expression has been observed in certain tumors, possibly influencing oncogenic pathways or epigenetic regulation. In neurodevelopment, ZNF507 may interact with signaling molecules critical for neural differentiation. Recombinant human ZNF507 protein is commonly produced via bacterial or mammalian expression systems, enabling in vitro studies to dissect its molecular interactions, post-translational modifications, and functional roles. While research on ZNF507 is still evolving, its structural features and preliminary associations with disease underscore its potential as a therapeutic target or biomarker. Further investigations are needed to elucidate its precise molecular networks and physiological relevance.


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