| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP8 |
| Uniprot No | P40818 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-1118aa |
| 氨基酸序列 | PAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECR LDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEE AERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAK GSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLII MDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRG NVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGY ENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQT PPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSI KNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVF SPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQ KAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGV KRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGK PFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGL PSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQ IPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPK AEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHL ADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFK ITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHL DDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMY LSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIW KLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKY NLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAA YILFYTSLGPRVTDVAT |
| 预测分子量 | 128 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USP8重组蛋白的3篇代表性参考文献示例(注：文献信息为示例性虚构，实际研究中请以真实文献为准)：
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1. **文献名称**：*Purification and Functional Characterization of Recombinant USP8 Deubiquitinase*
**作者**：Smith J. et al.
**摘要**：本研究通过原核表达系统成功纯化USP8重组蛋白，并验证其去泛素化酶活性。实验表明，USP8特异性切割K63-linked泛素链，且其催化活性依赖于保守的半胱氨酸结构域。
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2. **文献名称**：*USP8 Regulates EGFR Recycling via Recombinant Protein-Mediated Ubiquitin Editing*
**作者**：Almeida C. et al.
**摘要**：通过体外重组USP8蛋白实验，揭示其通过去泛素化作用调控表皮生长因子受体(EGFR)的内吞与溶酶体降解途径，为靶向EGFR的癌症治疗提供新机制。
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3. **文献名称**：*Crystal Structure of Recombinant USP8 Catalytic Domain and Its Implication in Substrate Recognition*
**作者**：Kumar R. et al.
**摘要**：解析了重组USP8催化结构域的晶体结构，发现其独特的锌指结构域对底物结合至关重要，为设计特异性USP8抑制剂奠定结构基础。
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如需真实文献，建议在PubMed或Web of Science中检索关键词“USP8 recombinant protein”或“USP8 deubiquitinase”。
USP8 (Ubiquitin-Specific Protease 8) is a deubiquitinating enzyme (DUB) that plays a critical role in regulating cellular processes by removing ubiquitin chains from target proteins, thereby influencing their stability, localization, or activity. As a member of the ubiquitin-specific protease family, USP8 is involved in maintaining protein homeostasis, particularly in endosomal sorting and receptor tyrosine kinase signaling, such as EGFR trafficking. It directly interacts with the endosomal sorting complex required for transport (ESCRT) machinery to modulate the fate of ubiquitinated membrane proteins, determining whether they are recycled or degraded in lysosomes.
Recombinant USP8 protein is engineered for in vitro studies to explore its enzymatic mechanisms, substrate specificity, and regulatory roles. Produced using expression systems like *E. coli* or mammalian cells, the purified protein often includes tags (e.g., GST, His-tag) for ease of isolation. Researchers utilize it to investigate USP8's involvement in diseases, including cancer and neurodegenerative disorders. For example, USP8 dysfunction is linked to impaired protein degradation pathways in Parkinson’s disease, where aberrant α-synuclein aggregation occurs. In cancer, USP8 can either promote or suppress tumor growth depending on context, making it a nuanced therapeutic target.
Structural studies of recombinant USP8 have revealed insights into its catalytic domain and regulatory regions, which are essential for designing inhibitors. Its activity is modulated by phosphorylation and protein interactions, such as binding to 14-3-3 proteins. Current research focuses on developing USP8-targeted therapies, leveraging recombinant protein tools for high-throughput drug screening and mechanistic validation. Overall, USP8 recombinant protein serves as a vital resource for deciphering ubiquitin-dependent pathways and their implications in health and disease.
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