| WB | 咨询技术 | Human,Mouse,Rat |
| IF | 咨询技术 | Human,Mouse,Rat |
| IHC | 咨询技术 | Human,Mouse,Rat |
| ICC | 技术咨询 | Human,Mouse,Rat |
| FCM | 咨询技术 | Human,Mouse,Rat |
| Elisa | 1/20000 | Human,Mouse,Rat |
| Aliases | UBB; Polyubiquitin-B; UBC; Polyubiquitin-C; RPS27A; UBA80; UBCEP1; Ubiquitin-40S ribosomal protein S27a; Ubiquitin carboxyl extension protein 80; UBA52; UBCEP2; Ubiquitin-60S ribosomal protein L40; CEP52; Ubiquitin A-52 residue ribosomal protein fusion pr |
| Entrez GeneID | 7311; |
| WB Predicted band size | 80 50kDa |
| Host/Isotype | Rabbit IgG |
| Antibody Type | Primary antibody |
| Storage | Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles. |
| Species Reactivity | Human,Mouse,Rat |
| Immunogen | Synthesized peptide derived from the human Ub around the acetylation site of K27. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide,0.5%BSA and 50% glycerol. |
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以下是关于Ub (Acetyl-Lys27)抗体的3篇参考文献示例(注：由于该修饰较为特殊，以下文献为假设性示例，实际文献需通过数据库验证)：
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1. **文献名称**：*Site-specific acetylation of ubiquitin regulates proteasome function*
**作者**：Smith A, et al.
**摘要**：本研究揭示了泛素K27位点乙酰化修饰(Acetyl-Lys27)在调控蛋白酶体降解途径中的关键作用。作者开发了一种特异性识别K27乙酰化泛素的抗体，并通过免疫沉淀和质谱分析证明该修饰通过干扰泛素链的延伸抑制底物降解。
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2. **文献名称**：*A novel antibody-based approach to detect ubiquitin acetylation in cellular stress responses*
**作者**：Chen L, et al.
**摘要**：研究团队报道了一种高特异性的Acetyl-Lys27泛素抗体，并验证其在多种细胞应激模型中的应用。实验表明，DNA损伤可诱导泛素K27乙酰化，该抗体成功用于免疫荧光和Western blot检测，揭示了该修饰与基因组稳定性间的关联。
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3. **文献名称**：*Ubiquitin acetylation at Lys27 modulates autophagy-lysosomal pathway*
**作者**：Wang Y, et al.
**摘要**：本文利用Acetyl-Lys27泛素抗体，首次发现该修饰通过促进特定底物的自噬性降解调控细胞代谢。抗体特异性经肽段竞争实验验证，并通过敲除乙酰转移酶实验证实修饰的功能依赖性。
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**提示**：实际研究中，建议通过 **PubMed** 或 **Google Scholar** 以关键词“Ubiquitin K27 acetylation antibody”或“Acetyl-K27 ubiquitin antibody”检索最新文献，并优先选择包含抗体验证细节(如特异性检测、应用场景)的研究。部分抗体厂商(如Cell Signaling Technology)的技术文档也可能提供相关参考文献。
Ubiquitin (Ub) is a highly conserved regulatory protein involved in diverse cellular processes, including protein degradation, DNA repair, and signal transduction. Post-translational modifications (PTMs) of ubiquitin, such as acetylation, fine-tune its functions and interactions. Acetylation at lysine 27 (K27) is a relatively understudied PTM that modulates Ub’s role in cellular pathways. Unlike ubiquitination, which typically tags proteins for degradation, acetylation at K27 may alter Ub’s ability to form polyubiquitin chains or interact with downstream effectors, potentially influencing substrate specificity or signaling outcomes. This modification has been implicated in regulating immune responses, transcriptional activity, and stress adaptation, though its precise mechanisms remain an active area of research.
The Ub (Acetyl-Lys27) antibody is a critical tool for detecting this specific acetylated form of ubiquitin in experimental settings. It enables researchers to investigate the spatial and temporal dynamics of K27 acetylation under various physiological or pathological conditions, such as inflammation, cancer, or neurodegenerative diseases. By using techniques like immunoprecipitation, Western blotting, or immunofluorescence, this antibody helps elucidate how acetylation crosstalks with other Ub PTMs (e.g., phosphorylation, ubiquitination) to regulate cellular homeostasis. Its development reflects growing interest in the "ubiquitin code" and the functional complexity added by acetylation, offering insights into novel therapeutic targets for diseases linked to Ub signaling dysregulation.
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