| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OTUD7B |
| Uniprot No | Q6GQQ9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-843aa |
| 氨基酸序列 | MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVKLHLLHSYMNVKWIPLSSDAQAPLAQPESPTASAGDEPRSTPESGDSDKESVGSSSTSNEGGRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGSKPGGVGTGLGGSSGTETLEKKKKNSLKSWKGGKEEAAGDGPVSEKPPAESVGNGGSKYSQEVMQSLSILRTAMQGEGKFIFVGTLKMGHRHQYQEEMIQRYLSDAEERFLAEQKQKEAERKIMNGGIGGGPPPAKKPEPDAREEQPTGPPAESRAMAFSTGYPGDFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPPYATFPRQCPPGRPYPHQDSIPSLEPGSHSKDGLHRGALLPPPYRVADSYSNGYREPPEPDGWAGGLRGLPPTQTKCKQPNCSFYGHPETNNFCSCCYREELRRREREPDGELLVHRF |
| 预测分子量 | 92,5 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OTUD7B重组蛋白的3篇代表性文献概览(注：文献为模拟示例，实际研究请查阅具体数据库)：
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1. **标题**: *OTUD7B deubiquitinates KEAP1 to activate NRF2-mediated antioxidant responses*
**作者**: Li Y, et al.
**摘要**: 本研究揭示了OTUD7B通过去泛素化KEAP1.解除其对NRF2的抑制作用，从而激活抗氧化应激通路。重组OTUD7B蛋白的体外实验证实其直接与KEAP1相互作用，并调控氧化损伤下的细胞存活。
2. **标题**: *Structural basis of OTUD7B deubiquitinating enzyme activity in innate immunity*
**作者**: Zhang X, et al.
**摘要**: 通过X射线晶体学解析了OTUD7B重组蛋白的催化结构域，阐明了其特异性识别K48链型泛素的结构机制，并证明其在TLR/IL-1R信号通路中通过去泛素化TRAF3负调控炎症反应。
3. **标题**: *OTUD7B suppresses tumor metastasis via deubiquitinating and stabilizing Scribble*
**作者**: Wang H, et al.
**摘要**: 研究利用重组OTUD7B蛋白进行功能分析，发现其通过去泛素化并稳定细胞极性蛋白Scribble，抑制EMT过程，从而阻碍乳腺癌细胞的迁移和侵袭，为癌症治疗提供潜在靶点。
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如需实际文献，建议通过PubMed或Web of Science检索关键词“OTUD7B recombinant protein”或“OTUD7B deubiquitinase”。
OTUD7B (OTU deubiquitinase 7B) is a member of the ovarian tumor (OTU) domain-containing deubiquitinating enzyme (DUB) family, which regulates cellular processes by selectively cleaving ubiquitin chains from substrate proteins. This enzyme plays a critical role in maintaining protein homeostasis, modulating signaling pathways, and influencing immune responses. Structurally, OTUD7B contains a conserved OTU domain responsible for its catalytic activity, enabling it to hydrolyze lysine-linked polyubiquitin chains. Unlike many DUBs, OTUD7B exhibits unique substrate specificity, targeting proteins involved in NF-κB signaling, DNA repair, and apoptosis.
Studies highlight OTUD7B's dual regulatory roles. It negatively regulates NF-κB activation by deubiquitinating key signaling components, thereby influencing inflammatory and immune pathways. Conversely, it stabilizes pro-survival factors like CLIMP-63. linking it to cancer cell proliferation and resistance to therapy. Dysregulation of OTUD7B has been implicated in diseases such as cancers, neurodegenerative disorders, and autoimmune conditions, making it a potential therapeutic target.
Recombinant OTUD7B protein is engineered for in vitro studies, enabling mechanistic exploration of its enzymatic activity, substrate interactions, and structural properties. Researchers utilize it to screen for modulators (inhibitors/activators) that could fine-tune its activity in pathological contexts. Its production typically involves expression in bacterial or mammalian systems, followed by purification to retain catalytic integrity. Ongoing research focuses on elucidating its context-dependent roles and therapeutic potential, bridging fundamental biology with translational applications.
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