| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PSMD14 |
| Uniprot No | O00487 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-310aa |
| 氨基酸序列 | MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK |
| 预测分子量 | 79.2 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. |
以下是关于PSMD14重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Structural basis for the recognition of K48-linked ubiquitin chains by the proteasome*
**作者**：C.-H. Lee et al.
**摘要**：本研究解析了PSMD14(Rpn11)作为26S蛋白酶体亚基的去泛素化酶活性机制，通过重组PSMD14蛋白的晶体结构分析，揭示了其识别和切割K48连接型泛素链的结构基础，为蛋白酶体依赖的蛋白质降解途径提供了分子层面的解释。
2. **文献名称**：*Targeting PSMD14 inhibits melanoma growth through disruption of EGFR stability*
**作者**：Y. Wang et al.
**摘要**：该研究利用重组PSMD14蛋白进行体外酶活实验，证明其通过去泛素化稳定EGFR蛋白，促进黑色素瘤进展。通过抑制PSMD14活性，可降低EGFR水平并抑制肿瘤生长，为靶向治疗提供了新策略。
3. **文献名称**：*The proteasome deubiquitinating enzyme PSMD14 regulates cell proliferation via stabilizing cyclin E*
**作者**：L. Zhang et al.
**摘要**：文章通过重组PSMD14蛋白与细胞周期蛋白Cyclin E的相互作用研究，揭示了PSMD14通过去泛素化作用维持Cyclin E稳定性，从而调控细胞周期进程，为癌症治疗中蛋白酶体功能的靶向干预提供了依据。
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以上文献涵盖了PSMD14的结构解析、肿瘤相关功能及细胞周期调控研究，均涉及重组蛋白在机制探索中的应用。如需更多文献方向(如神经退行性疾病或药物开发)，可进一步补充。
PSMD14 (Proteasome 26S Subunit, Non-ATPase 14), also known as POH1 or Rpn11. is a critical component of the 19S regulatory particle within the 26S proteasome complex. This multifunctional protein plays a central role in the ubiquitin-proteasome system (UPS), the primary pathway for targeted protein degradation in eukaryotic cells. Structurally, PSMD14 contains a conserved JAMM (JAB1/MPN/Mov34 metalloenzyme) domain, which confers metalloprotease activity essential for its deubiquitinating function. During proteasomal degradation, PSMD14 cleaves ubiquitin chains from substrate proteins, enabling both substrate unfolding and recycling of ubiquitin molecules.
Beyond its catalytic role, PSMD14 participates in proteasome assembly and substrate recognition. It interacts with other 19S subunits through its MPN domain, contributing to the structural integrity of the regulatory complex. Emerging research highlights its involvement in critical cellular processes including cell cycle regulation, DNA damage response, and oxidative stress management. Dysregulation of PSMD14 has been implicated in various pathologies, particularly cancer progression (through modulation of oncoprotein stability) and neurodegenerative disorders (via impaired clearance of misfolded proteins).
Recombinant PSMD14 protein is typically produced in Escherichia coli or mammalian expression systems, preserving its enzymatic activity for functional studies. This engineered protein serves as a vital tool for investigating UPS mechanisms, screening deubiquitinase inhibitors, and elucidating proteasome-related disease pathways. Its recombinant form enables precise analysis of substrate interactions and catalytic mechanisms without interference from proteasome complex components. Current research focuses on developing PSMD14-targeted therapies, particularly exploring its JAMM domain as a potential intervention point for cancer treatment and neurodegenerative disease management.
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