| 纯度 | >80%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP7 |
| Uniprot No | Q93009 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-1102aa |
| 氨基酸序列 | MHHHHHHDYKDDDDKNHQQQQQQQKAGEQQLSEPEDMEMEAGDTDDPPRI TQNPVINGNVALSDGHNTAEEDMEDDTSWRSEATFQFTVERFSRLSESVL SPPCFVRNLPWKIMVMPRFYPDRPHQKSVGFFLQCNAESDSTSWSCHAQA VLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDD DKVTFEVFVQADAPHGVAWDSKKHTGYVGLKNQGATCYMNSLLQTLFFTN QLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWE TLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKE VDYRSDRREDYYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGL QEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEF LQKTDPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVS RCTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEVLQAVTDHDI PQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYDE EKVKYTVFKVLKNSSLAEFVQSLSQTMGFPQDQIRLWPMQARSNGTKRPA MLDNEADGNKTMIELSDNENPWTIFLETVDPELAASGATLPKFDKDHDVM LFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYE EVKPNLTERIQDYDVSLDKALDELMDGDIIVFQKDDPENDNSELPTAKEY FRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPML LQFFKSQGYRDGPGNPLRHNYEGTLRDLLQFFKPRQPKKLYYQQLKMKIT DFENRRSFKCIWLNSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKAS GKLRLLEIVSYKIIGVHQEDELLECLSPATSRTFRIEEIPLDQVDIDKEN EMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFE KFKFAIVMMGRHQYINEDEYEVNLKDFEPQPGNMSHPRPWLGLDHFNKAP KRSRYTYLEKAIKIHN |
| 预测分子量 | 130 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USP7重组蛋白的3篇参考文献概览：
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1. **文献名称**：*Structural Basis of Ubiquitin Recognition by the Deubiquitinating Enzyme USP7*
**作者**：Hu, M. et al.
**摘要**：本研究解析了重组人源USP7催化结构域与泛素的复合物晶体结构，揭示了USP7特异性识别泛素的分子机制，并发现其C末端结构域对酶活性的调控作用，为靶向USP7的药物设计提供了结构基础。
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2. **文献名称**：*USP7 Regulates the Stability and Function of HDM2 via Deubiquitination*
**作者**：Li, M. et al.
**摘要**：通过体外重组USP7蛋白实验，作者证明USP7通过去泛素化稳定HDM2(p53的E3连接酶)，从而间接调控p53蛋白水平。研究阐明了USP7在肿瘤发生中的双重角色，并验证了其重组蛋白的酶活功能。
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3. **文献名称**：*Development of a High-Throughput Screening Assay for USP7 Inhibitors Using Recombinant Protein*
**作者**：Chauhan, D. et al.
**摘要**：该研究报道了一种基于重组USP7蛋白的高通量抑制剂筛选平台，鉴定了多个小分子化合物可特异性抑制USP7的去泛素化活性，为癌症治疗提供了潜在先导化合物。
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以上文献均涉及重组USP7蛋白在结构解析、功能研究及药物开发中的应用，覆盖了基础机制探索和转化研究方向。
**Background of USP7 Recombinant Protein**
Ubiquitin-specific protease 7 (USP7), also known as herpesvirus-associated ubiquitin-specific protease (HAUSP), is a member of the deubiquitinating enzyme (DUB) family that regulates protein stability and function by removing ubiquitin chains from target substrates. It plays a pivotal role in cellular processes such as DNA repair, epigenetic regulation, immune response, and tumor suppression. USP7 is particularly noted for its interaction with key regulatory proteins, including p53. PTEN, and MDM2. thereby influencing cell cycle control, apoptosis, and oncogenic signaling pathways. Dysregulation of USP7 has been implicated in cancers, neurodegenerative disorders, and viral infections, making it a therapeutic target of interest.
Recombinant USP7 protein is engineered through molecular cloning and expression systems (e.g., *E. coli* or mammalian cells) to produce a highly purified, functional form of the enzyme for research and drug discovery. Its recombinant form retains the catalytic triad (Cys, His, Asp) within the conserved USP domain, enabling deubiquitinase activity in vitro. Researchers utilize USP7 recombinant protein to study substrate specificity, enzymatic kinetics, and inhibition mechanisms. It is also critical for high-throughput screening of small-molecule inhibitors or modulators aimed at correcting USP7-associated pathologies.
Additionally, USP7’s role in stabilizing oncoproteins (e.g., MDM2) or tumor suppressors (e.g., p53) highlights its dual context-dependent functions, necessitating precise biochemical tools like recombinant proteins to dissect its regulatory networks. Structural studies using recombinant USP7 have further elucidated its interaction with ubiquitin and co-factors, advancing the design of targeted therapies. Overall, USP7 recombinant protein serves as a vital resource for understanding ubiquitin-dependent signaling and developing precision medicine strategies.
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