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Recombinant Human UBC5A protein

  • 中文名: 水稻亚种粳稻泛素结合酶E2 5A(UBC5A)重组蛋白
  • 别    名: UBC5A;SFT;UBC5A;UBCH5;Ubiquitin-conjugating enzyme E2 D1
货号: PA2000-3318
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点UBC5A
Uniprot NoQ8S920
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-147aa
氨基酸序列MASKRIQKELKDLQKDPPTSCSAGPVGEDMFHWQATIMGPSDSPYAGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKDQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRHKYENTARTWTQRYAM
预测分子量16,5 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

关于UBC5A重组蛋白的研究文献相对较少,可能存在名称拼写或亚型标注差异(如UBC5、UBE2A等)。以下是基于泛素结合酶相关重组蛋白的推测性参考(建议核实名称准确性):

1. **标题**: "Functional Characterization of Recombinant UBC5A in Ubiquitin Chain Assembly"

**作者**: Smith J, et al.

**摘要**: 研究报道了人源UBC5A重组蛋白在大肠杆菌中的高效表达及纯化,证实其在体外泛素链组装中的催化活性,并揭示了其与E3连接酶的协同作用机制。

2. **标题**: "Structural Insights into UBC5A Substrate Specificity by Crystallography"

**作者**: Lee H, et al.

**摘要**: 通过X射线晶体学解析了UBC5A重组蛋白的三维结构,发现其独特的泛素结合域构象,解释了其对特定赖氨酸残基(如K48/K63)的选择性泛素链形成能力。

3. **标题**: "UBC5A Recombinant Protein Enhances Protein Degradation in Cancer Cell Models"

**作者**: Zhang R, et al.

**摘要**: 利用哺乳动物细胞表达的UBC5A重组蛋白,证明其在癌细胞中通过调控p53泛素化水平促进蛋白酶体依赖性降解,提示其作为肿瘤治疗靶点的潜力。

4. **标题**: "Optimization of UBC5A Expression in Pichia pastoris for High-Throughput Screening"

**作者**: Müller S, et al.

**摘要**: 开发了毕赤酵母系统中UBC5A重组蛋白的高效分泌表达工艺,并应用于高通量药物筛选平台,评估小分子抑制剂对其酶活性的影响。

**注意**:以上为模拟文献,实际研究中请通过PubMed或Web of Science以“UBC5A recombinant”、“UBC5A expression”等关键词检索,并注意区分不同物种(如酵母Ubc5与哺乳动物同源物可能存在命名差异)。若需具体文献,请提供更明确的蛋白背景或功能方向。

背景信息

**Background of UBC5A Recombinant Protein**

Ubiquitin-conjugating enzyme E2 A (UBC5A), also known as UBCH7. is a member of the E2 ubiquitin-conjugating enzyme family. It plays a critical role in the ubiquitin-proteasome system (UPS), a major pathway for targeted protein degradation in eukaryotic cells. UBC5A facilitates the transfer of ubiquitin molecules to substrate proteins, a process essential for regulating protein stability, cellular homeostasis, and signal transduction. This enzyme operates in tandem with E3 ubiquitin ligases, which confer substrate specificity, enabling selective tagging of proteins for proteasomal degradation or functional modification.

UBC5A is particularly notable for its involvement in diverse physiological processes, including cell cycle regulation, DNA repair, and stress response. Dysregulation of UBC5A has been implicated in several pathologies, such as neurodegenerative diseases (e.g., Parkinson’s disease) and cancers, where altered ubiquitination contributes to abnormal protein accumulation or oncogenic signaling.

Recombinant UBC5A protein is engineered through molecular cloning and expression in heterologous systems like *E. coli* or mammalian cell cultures. This allows large-scale production of the enzyme with high purity and activity for *in vitro* studies. Researchers utilize recombinant UBC5A to investigate ubiquitination mechanisms, screen for modulators of UPS activity, or develop therapeutic strategies targeting ubiquitination pathways.

Structurally, UBC5A contains a conserved catalytic core domain characteristic of E2 enzymes but lacks intrinsic substrate specificity, relying on E3 ligases for target recognition. Its recombinant form often includes affinity tags (e.g., His-tag) for simplified purification. Studies have also explored its isoforms, such as UBC5B, highlighting functional redundancy and tissue-specific expression patterns.

Overall, UBC5A recombinant protein serves as a vital tool for dissecting the molecular intricacies of ubiquitination and advancing drug discovery efforts aimed at UPS-related disorders.

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