| WB | 1/500 - 1/2000 | 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 | 1/10000 | Human,Mouse,Rat |
| Aliases | TEF1; HAUSP; USP7 |
| Entrez GeneID | 7874 |
| clone | 5F11 |
| WB Predicted band size | 128kDa |
| Host/Isotype | Mouse IgG1 |
| 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 |
| Immunogen | Purified recombinant fragment of human HAUSP expressed in E. Coli. |
| Formulation | Purified antibody in PBS with 0.05% sodium azide. |
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以下是关于HAUSP抗体的3篇经典文献及其摘要：
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1. **文献名称**：*Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization*
**作者**：Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A.Y., Qin, J., Gu, W.
**摘要**：该研究揭示了HAUSP通过去泛素化p53和其E3泛素连接酶MDM2.调控p53蛋白稳定性。实验中使用HAUSP抗体进行免疫沉淀和Western blot，证明HAUSP在DNA损伤应答中通过拮抗MDM2介导的p53降解，维持p53的肿瘤抑制功能。
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2. **文献名称**：*Herpesvirus-associated ubiquitin-specific protease (HAUSP) regulates viral replication through stabilizing viral immediate-early protein ICP0*
**作者**：Everett, R.D., Meredith, M., Orr, A.
**摘要**：本文发现HAUSP与单纯疱疹病毒1型(HSV-1)蛋白ICP0相互作用，并通过去泛素化增强ICP0的稳定性。研究中利用HAUSP特异性抗体进行免疫荧光和共定位分析，揭示了HAUSP在病毒复制周期中的关键作用。
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3. **文献名称**：*USP7 as a therapeutic target in acute myeloid leukemia: inhibition of HAUSP deubiquitinase activity induces p53-dependent apoptosis*
**作者**：Song, M.S., Salmena, L., Pandolfi, P.P.
**摘要**：该研究证明HAUSP(USP7)在急性髓系白血病(AML)中通过稳定MDM2抑制p53功能。使用HAUSP抗体进行免疫组化和基因敲除实验，发现靶向HAUSP可激活p53依赖性凋亡通路，提示其作为AML治疗靶点的潜力。
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这些文献均涉及HAUSP抗体的应用(如免疫沉淀、Western blot、免疫荧光等)，并聚焦于HAUSP在肿瘤调控、病毒感染及靶向治疗中的功能机制。如需扩展，可进一步查阅相关药物开发研究(如HAUSP抑制剂筛选)。
**Background of HAUSP Antibody**
HAUSP (Herpesvirus-Associated Ubiquitin-Specific Protease), also known as USP7. is a deubiquitinating enzyme belonging to the ubiquitin-specific protease (USP) family. It plays a critical role in regulating protein stability by removing ubiquitin chains from substrate proteins, thereby preventing their degradation via the proteasome. HAUSP gained prominence for its interaction with the tumor suppressor p53. where it stabilizes p53 by deubiquitinating and counteracting the E3 ligase MDM2. a key negative regulator of p53. This interplay highlights HAUSP's dual role in both promoting and suppressing tumorigenesis, depending on cellular context.
Beyond p53. HAUSP targets diverse substrates, including PTEN, FOXO4. and viral proteins, linking it to cancer, neurodegenerative diseases, and viral infections. Its structural domains, such as the N-terminal tumor suppressor–binding region and the C-terminal catalytic domain, enable substrate recognition and enzymatic activity.
HAUSP-specific antibodies are essential tools for studying its expression, localization, and interactions in cellular pathways. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence. Research on HAUSP inhibitors, aimed at modulating pathways like p53-MDM2 for cancer therapy, underscores its therapeutic relevance. However, challenges remain in understanding its substrate-specific effects and balancing therapeutic benefits with off-target risks. HAUSP antibodies thus serve as critical reagents in both basic research and drug development.
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