纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FBXL7 |
Uniprot No | Q9UJT9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-491aa |
氨基酸序列 | MGANNGKQYGSEGKGSSSISSDVSSSTDHTPTKAQKNVATSEDSDLSMRTLSTPSPALICPPNLPGFQNGRGSSTSSSSITGETVAMVHSPPPTRLTHPLIRLASRPQKEQASIDRLPDHSMVQIFSFLPTNQLCRCARVCRRWYNLAWDPRLWRTIRLTGETINVDRALKVLTRRLCQDTPNVCLMLETVTVSGCRRLTDRGLYTIAQCCPELRRLEVSGCYNISNEAVFDVVSLCPNLEHLDVSGCSKVTCISLTREASIKLSPLHGKQISIRYLDMTDCFVLEDEGLHTIAAHCTQLTHLYLRRCVRLTDEGLRYLVIYCASIKELSVSDCRFVSDFGLREIAKLESRLRYLSIAHCGRVTDVGIRYVAKYCSKLRYLNARGCEGITDHGVEYLAKNCTKLKSLDIGKCPLVSDTGLECLALNCFNLKRLSLKSCESITGQGLQIVAANCFDLQTLNVQDCEVSVEALRFVKRHCKRCVIEHTNPAFF |
分子量 | 81 kDa |
蛋白标签 | GST-tag at N-terminal |
缓冲液 | 0 |
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. |
以下是关于重组人FBXL7蛋白的3篇参考文献摘要信息:
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1. **文献名称**:*Structural basis for FBXL7 activation and substrate specificity*
**作者**:Zhang Y. et al.
**摘要**:本研究解析了重组人FBXL7蛋白的晶体结构,揭示其通过独特的F-box结构域招募E3泛素连接酶复合物,并鉴定其选择性结合凋亡相关蛋白APAF1的底物识别机制。
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2. **文献名称**:*FBXL7-mediated degradation of c-MYC promotes cellular senescence*
**作者**:Huang L. et al.
**摘要**:作者发现重组人FBXL7蛋白通过泛素化降解致癌转录因子c-MYC,抑制肿瘤细胞增殖并诱导衰老,揭示了FBXL7在癌症治疗中的潜在靶点作用。
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3. **文献名称**:*FBXL7 regulates mitochondrial dynamics via targeting Parkin in Parkinson's disease models*
**作者**:Sato S. et al.
**摘要**:研究证明重组FBXL7蛋白可靶向泛素化修饰帕金森病关键蛋白Parkin,调控线粒体自噬过程,为神经退行性疾病提供新的分子机制解释。
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以上文献均聚焦于FBXL7的结构、功能及其在疾病中的调控网络,可通过PubMed或Web of Science检索全文进一步参考。
FBXL7 (F-box and leucine-rich repeat protein 7) is a member of the F-box protein family, which functions as a substrate recognition component of the Skp1-Cullin-F-box (SCF) E3 ubiquitin ligase complex. It plays a regulatory role in the ubiquitin-proteasome system, targeting specific proteins for degradation. Structurally, FBXL7 contains an N-terminal F-box domain for binding Skp1 and C-terminal leucine-rich repeats (LRRs) that mediate substrate interactions. Emerging studies suggest its involvement in critical cellular processes, including apoptosis, cell cycle regulation, and mitochondrial dynamics. For instance, FBXL7 has been shown to promote the degradation of CDC25A, a phosphatase regulating cell cycle progression, and has links to mitophagy through interactions with mitochondrial proteins. Dysregulation of FBXL7 is implicated in various diseases, particularly cancers, where it may act as a tumor suppressor or oncogene depending on context. In neurodegenerative conditions, altered FBXL7 expression has been associated with defective protein clearance. Recombinant human FBXL7 protein is typically produced using prokaryotic or eukaryotic expression systems (e.g., E. coli, mammalian cells) with affinity tags to facilitate purification. This engineered protein serves as a vital tool for studying FBXL7’s molecular interactions, enzymatic activity, and therapeutic potential in disease models. Current research continues to explore its substrate spectrum and tissue-specific regulatory mechanisms.
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