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Recombinant Human DCAF16 protein

  • 中文名: DDB1和CUL4相关因子16(DCAF16)重组蛋白
  • 别    名: DCAF16;C4orf30;DDB1- and CUL4-associated factor 16
货号: PA2000-3397
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点DCAF16
Uniprot No C4orf30
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-216aa
氨基酸序列MGPRNPSPDHLSESESEEEENISYLNESSGEEWDSSEEEDSMVPNLSPLESLAWQVKCLLKYSTTWKPLNPNSWLYHAKLLDPSTPVHILREIGLRLSHCSHCVPKLEPIPEWPPLASCGVPPFQKPLTSPSRLSRDHATLNGALQFATKQLSRTLSRATPIPEYLKQIPNSCVSGCCCGWLTKTVKETTRTEPINTTYSYTDFQKAVNKLLTASL
预测分子量 55.3 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

以下是基于学术领域相关主题模拟生成的关于DCAF16重组蛋白的参考文献示例。由于无法访问实时数据库,建议通过PubMed或Google Scholar验证最新研究:

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1. **文献名称**: *Structural and Functional Analysis of DCAF16 in the CRL4 Ubiquitin Ligase Complex*

**作者**: Zhang L, et al.

**摘要**: 本研究利用重组DCAF16蛋白解析了其与DDB1-CUL4复合物的相互作用机制,通过X射线晶体学揭示了DCAF16的WD40结构域对底物识别的关键作用,并证明其在DNA损伤应答中的泛素化功能。

2. **文献名称**: *Recombinant DCAF16 Expression and Its Role in Protein Degradation Pathways*

**作者**: Gupta R, et al.

**摘要**: 作者在大肠杆菌中成功表达并纯化重组DCAF16蛋白,结合体外泛素化实验,发现DCAF16特异性招募某些核蛋白作为CRL4泛素连接酶的降解靶标,为靶向治疗提供新思路。

3. **文献名称**: *DCAF16-Mediated Substrate Recognition in Leukemia Cell Lines*

**作者**: Tanaka K, et al.

**摘要**: 通过重组DCAF16与白血病细胞裂解物的互作组学分析,鉴定出多个潜在底物蛋白,揭示DCAF16通过调控细胞周期蛋白稳定性影响癌细胞增殖的分子机制。

4. **文献名称**: *Development of a DCAF16 Knockout Model Using CRISPR-Cas9 and Recombinant Rescue*

**作者**: Wang Y, et al.

**摘要**: 研究构建了DCAF16基因敲除细胞系,并通过重组DCAF16蛋白回补实验证实其对于维持基因组稳定性及修复UV诱导DNA损伤的必要性。

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**注意**:以上文献为示例性质,实际引用请查询具体数据库获取准确信息。研究DCAF16时可关注其与泛素-蛋白酶体系统、癌症或遗传疾病的相关性。

背景信息

**Background of DCAF16 Recombinant Protein**

DCAF16 (DDB1- and CUL4-associated factor 16) is a substrate-recognition component of the CUL4-DDB1 E3 ubiquitin ligase complex, which plays a critical role in the ubiquitin-proteasome system (UPS). This system regulates protein degradation, a fundamental process for maintaining cellular homeostasis, DNA repair, and signal transduction. DCAF16 is part of the DCAF protein family, known for binding to the DDB1 adaptor to recruit specific substrates for ubiquitination and subsequent proteasomal degradation.

Recombinant DCAF16 proteins are engineered in vitro using expression systems (e.g., *E. coli*, mammalian, or insect cells*) to study its structural and functional properties. These proteins retain the ability to interact with DDB1 and participate in substrate recognition, making them valuable tools for dissecting molecular mechanisms of ubiquitination, substrate specificity, and protein turnover. Research has linked DCAF16 to diverse cellular processes, including chromatin remodeling, cell cycle regulation, and responses to DNA damage. For instance, DCAF16 may mediate degradation of proteins involved in histone modification, impacting epigenetic regulation.

Recent studies highlight its potential therapeutic relevance. DCAF16 is implicated in targeted protein degradation (TPD) strategies, such as PROTACs (Proteolysis-Targeting Chimeras), where small molecules redirect E3 ligases to degrade disease-related proteins. Its role in specific cancers and neurodegenerative disorders is under investigation, with recombinant DCAF16 enabling *in vitro* assays to identify binding partners or screen for modulators.

Structural studies using recombinant DCAF16 have also advanced understanding of its WD40 repeat domains, which facilitate protein-protein interactions. Challenges remain in fully elucidating its physiological substrates and regulatory networks. Nonetheless, DCAF16 recombinant proteins serve as pivotal reagents for exploring UPS-driven pathways and developing novel therapies targeting protein degradation.

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