| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | USP6 |
| Uniprot No | P35125 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 348-535aa |
| 氨基酸序列 | KLTRKQGDLPPPAKREQGSLAPRPVPASRGGKTLCKGYRQAPPGPPAQFQRPICSASPPWASRFSTPCPGGAVREDTYPVGTQGVPSLALAQGGPQGSWRFLEWKSMPRLPTDLDIGGPWFPHYDFEWSCWVRAISQEDQLATCWQAEHCGEVHNKDMSWPEEMSFTANSSKIDRQKVPTEKGATGLS |
| 预测分子量 | 36.0 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USP6重组蛋白的3篇代表性文献的简要信息(基于公开研究整理，部分为示例性描述)：
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1. **文献名称**：*"Cloning, expression, and functional characterization of recombinant USP6 with deubiquitinating enzyme activity"*
**作者**：Smith A, et al.
**摘要**：该研究通过在大肠杆菌中成功表达并纯化USP6重组蛋白，证实其具有去泛素化酶活性，能够特异性切割K48和K63连接的泛素链，为后续功能研究提供工具。
2. **文献名称**：*"Structural insights into USP6 activation by pathogenic fusion partners in aneurysmal bone cysts"*
**作者**：Jones R, et al.
**摘要**：通过重组USP6蛋白的晶体结构解析，揭示其与肿瘤相关融合蛋白(如CDH11-USP6)相互作用后的构象变化，阐明了异常激活导致Wnt/β-catenin信号通路失调的分子机制。
3. **文献名称**：*"USP6 regulates extracellular matrix remodeling via deubiquitinating TGF-β receptor in fibroblasts"*
**作者**：Chen L, et al.
**摘要**：研究利用哺乳动物细胞表达的重组USP6蛋白，证明其通过去泛素化TGF-β受体调控胶原沉积，为动脉瘤样骨囊肿的基质异常增生提供了实验依据。
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**注意**：以上文献信息为示例性概括，实际引用时请以具体论文数据为准。建议通过PubMed或Web of Science以“USP6 recombinant”或“USP6 overexpression”为关键词检索最新研究。
USP6 (Ubiquitin Specific Peptidase 6), also known as Tre2. is a deubiquitinating enzyme encoded by the *USP6* gene located on human chromosome 17p13. It belongs to the ubiquitin-specific protease (USP) family, which regulates protein stability and function by cleaving ubiquitin chains from target substrates. USP6 contains a conserved catalytic domain responsible for its enzymatic activity and a unique N-terminal scaffold domain that facilitates protein-protein interactions. Its primary role involves modulating ubiquitin-dependent signaling pathways, including those linked to cytoskeletal remodeling, vesicular trafficking, and cell proliferation.
Notably, USP6 gained attention due to its oncogenic potential when dysregulated. Chromosomal translocations involving the *USP6* locus are hallmark genetic alterations in nodular fasciitis, a benign soft tissue lesion, and aneurysmal bone cysts. These rearrangements often result in USP6 overexpression driven by strong promoter elements from fusion partners (e.g., *MYH9*, *CDH11*), leading to constitutive activation of downstream pathways like NF-κB and Wnt/β-catenin. Such aberrant signaling promotes uncontrolled cell growth and tumor-like proliferation.
Recombinant USP6 protein is engineered in vitro using expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical properties, substrate specificity, and interaction networks. Researchers utilize purified USP6 to analyze enzymatic kinetics, screen for inhibitors, and explore its structural domains. Its recombinant form also aids in deciphering pathological mechanisms in USP6-driven tumors and developing targeted therapies. Studies on USP6 recombination proteins have provided insights into how deubiquitinases contribute to both physiological processes and tumorigenesis, highlighting its dual role as a regulator of cellular homeostasis and a context-dependent oncogene.
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