Protein expression and purification最新文献_第2页

Column-free purification of functional HIV-1 capsid protein and its application in assembly and inhibitor assays 功能性HIV-1衣壳蛋白的无柱纯化及其在组装和抑制剂检测中的应用

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-28 DOI: 10.1016/j.pep.2025.106766

Da-Wei Zhang , Xiao-Shuang Xu , Yimin Li , Shan Chang

{"title":"Column-free purification of functional HIV-1 capsid protein and its application in assembly and inhibitor assays","authors":"Da-Wei Zhang , Xiao-Shuang Xu , Yimin Li , Shan Chang","doi":"10.1016/j.pep.2025.106766","DOIUrl":"10.1016/j.pep.2025.106766","url":null,"abstract":"<div><div>The HIV-1 capsid protein (CA) is essential for viral replication and serves as a validated antiviral drug target. Traditional purification of CA relies on multi-step chromatographic protocols, which are time-consuming and labor-intensive. In this study, we established a rapid, column-free purification strategy using a cleavable self-aggregating tag (cSAT) to produce functional wild-type CA protein from E. coli with >95 % purity within a single day. The workflow is compatible with high-throughput formats and scalable from microplates to fermenters, offering significant advantages over conventional purification methods. The purified CA retained full biological activity, as demonstrated by its ability to assemble into higher-order structures in a salt- and protein concentration–dependent manner in vitro. We further evaluated the effects of two well-characterized capsid modulators: CAI, a peptide inhibitor, and lenacapavir (LEN), a clinically approved capsid-targeting drug. Turbidity-based assembly assays confirmed that CAI inhibited and LEN enhanced CA assembly in a dose-dependent manner. When co-administered, CAI and LEN exhibited mutually antagonistic effects. Preincubation with CAI abolished LEN-mediated enhancement, indicating a potential conformational lock imposed by CAI. These findings demonstrate that the column-free strategy enables efficient production of functionally active CA protein suitable for downstream biochemical and inhibitor screening assays. The approach provides a practical tool for accelerating HIV-1 capsid research and antiviral discovery.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106766"},"PeriodicalIF":1.4,"publicationDate":"2025-06-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144517787","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Co-expression enhances cloning efficiency and protein production in CHO cells 共表达提高CHO细胞的克隆效率和蛋白产量。

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-18 DOI: 10.1016/j.pep.2025.106763

Yan Fang, Lani Shi, Yan Wang, Congcong Jin, Zhen Sun, Xi Chen, Kang Zhang, Jie Chen, Jiali Qi

{"title":"Co-expression enhances cloning efficiency and protein production in CHO cells","authors":"Yan Fang, Lani Shi, Yan Wang, Congcong Jin, Zhen Sun, Xi Chen, Kang Zhang, Jie Chen, Jiali Qi","doi":"10.1016/j.pep.2025.106763","DOIUrl":"10.1016/j.pep.2025.106763","url":null,"abstract":"<div><div>Chinese hamster ovary (CHO) cell lines are widely used in the biopharmaceutical industry, particularly for the production of monoclonal antibodies and recombinant protein drugs. Recombinant cell lines are typically derived from single-cell clones to ensure product consistency and stability. However, the difficult-to-express recombinant proteins may impair single-cell proliferation, thereby significantly reducing cloning efficiency. In this study, co-expression of insulin-like growth factor-1 (IGF-1) was used to improve the single-cell cloning efficiency. Co-expression of IGF-1 significantly improved bulk pool growth and increased cloning efficiency by 53–196 %. Batch cell culture evaluation studies further demonstrated that IGF-1 co-expression enhanced monoclonal cell density by 29–64 % and recombinant protein yield by 47–89 %. Additionally, the growth profile, titer, and critical quality attributes of selected cell clones remained stable over 60 generations. The results of this study demonstrate that IGF-1 co-expression represents an effective single-cell cloning strategy by significantly enhancing cloning efficiency and enabling stable production of difficult-to-express proteins.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106763"},"PeriodicalIF":1.4,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144336894","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

From Silkroad to Bioroad–Silkworm Biotechnology– 从丝绸之路到生物之路——蚕生物技术。

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-16 DOI: 10.1016/j.pep.2025.106762

Enoch Y. Park

{"title":"From Silkroad to Bioroad–Silkworm Biotechnology–","authors":"Enoch Y. Park","doi":"10.1016/j.pep.2025.106762","DOIUrl":"10.1016/j.pep.2025.106762","url":null,"abstract":"<div><div>Silkworms have shared history with humans for 5000 years and have significantly contributed to human welfare. Silkworms' ability to produce silk has attracted significant attention as an innovative protein expression system in 21st-century biotechnology, leading to the development of a protein production facility known as the silkworm biofactory. Unlike <em>Escherichia coli</em> expression systems, silkworms can produce recombinant proteins with the added benefits of post-translational modification, easy scalability, and low production costs, as they do not require bioreactors or specialized facilities and expensive media. Numerous recombinant proteins, including secretory and membrane proteins and virus-like particles (VLPs), have been successfully expressed in silkworms and purified, demonstrating their biological functions. Additionally, purification methods have been developed to manufacture recombinant proteins in silkworms. This review provides a comprehensive overview of the silkworm expression system, tracing its development from the past to the present. It highlights advancements in bioengineering related to the production of enveloped and non-enveloped VLPs. Furthermore, the review discusses the technology for displaying antigens on the surface of VLPs, aiming to improve vaccine efficacy through surface conjugations.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106762"},"PeriodicalIF":1.4,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144326727","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Molecular chaperones: A revolutionary approach for increased solubility of recombinant mAbs from bacterial and yeast systems 分子伴侣：从细菌和酵母系统中增加溶解度的重组单克隆抗体的革命性方法

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-13 DOI: 10.1016/j.pep.2025.106764

Niharika Ashish Kulkarni, Prabir Kumar Das, Arjun P, Venkata Dasu Veeranki

{"title":"Molecular chaperones: A revolutionary approach for increased solubility of recombinant mAbs from bacterial and yeast systems","authors":"Niharika Ashish Kulkarni, Prabir Kumar Das, Arjun P, Venkata Dasu Veeranki","doi":"10.1016/j.pep.2025.106764","DOIUrl":"10.1016/j.pep.2025.106764","url":null,"abstract":"<div><div>Recombinant protein expression has revolutionized biotechnology, enabling the production of therapeutic proteins, enzymes, and antibodies with high specificity and functionality. <em>Escherichia coli</em> can be a prominent host for recombinant protein production due to its rapid growth, well-characterized genetics, and cost-effectiveness. However, the formation of insoluble protein aggregates, misfolding, and stability issues are significant challenges. This review explores the integration of molecular chaperones such as GroEL/GroES, DnaK/DnaJ/GrpE, and Skp in recombinant systems to enhance folding, solubility, and activity of recombinant monoclonal antibodies (mAbs). It also examines advances in co-expression strategies, secretion pathways, and the role of engineered host strains in overcoming these bottlenecks. Further, the review highlights comparative approaches in other expression systems in yeast, including <em>Saccharomyces cerevisiae</em> and <em>Pichia pastoris</em>, focusing on the molecular chaperone-assisted folding of full-length and fragmented mAbs using Hsp70-90 (analogs of DnaJ and K, respectively), tailless complex polypeptide 1 ring complex (TRiC), and ribosome-associated complex (RAC)/nascent polypeptide-associated complex (NAC) system. Innovations such as the application of polymer nanoparticles as artificial chaperones and mRNA engineering for co-translational folding underscore the potential for optimizing recombinant protein production. Collectively, these findings offer a thorough grasp of the role of chaperones and engineering strategies in improving mAbs quality, with implications for biopharmaceutical manufacturing and industrial applications.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106764"},"PeriodicalIF":1.4,"publicationDate":"2025-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144288687","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Efficient synchronization of high expression and site-specific biotinylation of the PTBP1 RRM3/4 domain PTBP1 RRM3/4结构域的高表达和位点特异性生物素化的高效同步

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-05 DOI: 10.1016/j.pep.2025.106755

Zhangheng Ye , Hong Gu , Yuanhang Wang, Yingyi Liu, Yilan Huang, Meiyi Mao, Lan Sun, Mingxing Huang

{"title":"Efficient synchronization of high expression and site-specific biotinylation of the PTBP1 RRM3/4 domain","authors":"Zhangheng Ye , Hong Gu , Yuanhang Wang, Yingyi Liu, Yilan Huang, Meiyi Mao, Lan Sun, Mingxing Huang","doi":"10.1016/j.pep.2025.106755","DOIUrl":"10.1016/j.pep.2025.106755","url":null,"abstract":"<div><div>Polypyrimidine tract-binding protein 1 (PTBP1), a key regulator of mRNA alternative splicing, has emerged as a promising therapeutic target for neurodegenerative diseases and cancer treatment. Given the critical role of its RRM4 domain's lysine residues in binding to polypyrimidine single-stranded RNA, nonspecific biotinylation could potentially alter PTBP1's activity. Here, we describe a method for the concurrent high-level expression and site-specific biotinylation of the PTBP1 RRM3/4 domain using the pQE80L vector and AVB101 host strain. By optimizing codon usage and GC content, we achieved a maximum expression level of approximately 85 μg/mL in bacterial culture, with over 99 % purity and a 72.4 % biotinylation rate. The recombinant 6His-Avi<sup>Biotin</sup>-PTBP1 demonstrated the ability to emit chemiluminescence when coupled with HRP-streptavidin, to be immunoprecipitated by streptavidin magnetic beads, and to interact specifically with (CU)<sub>8</sub> RNA, exhibiting a dissociation constant (K<sub>D</sub>) of 38 nM as determined by Bio-Layer Interferometry (BLI). Collectively, these results indicate that the recombinant 6His-Avi<sup>Biotin</sup>-PTBP1 is suitable for inhibitor screening and kinetic parameter analysis.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106755"},"PeriodicalIF":1.4,"publicationDate":"2025-06-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144239799","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Efficient production of functional proaerolysin in E. coli 大肠杆菌中功能性原溶素的高效生产。

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-04 DOI: 10.1016/j.pep.2025.106754

Quynh Thi-Huong Pham , Ayako Tagawa , Narumi Iwata , Masaru Nakao , Yusuke Miyanari

{"title":"Efficient production of functional proaerolysin in E. coli","authors":"Quynh Thi-Huong Pham , Ayako Tagawa , Narumi Iwata , Masaru Nakao , Yusuke Miyanari","doi":"10.1016/j.pep.2025.106754","DOIUrl":"10.1016/j.pep.2025.106754","url":null,"abstract":"<div><div>Proaerolysin is a bacterial toxin produced by <em>Aeromonas hydrophila</em> that specifically binds to GPI-anchored proteins on the plasma membrane, forming transmembrane pores that induce cell death. Leveraging this unique property, proaerolysin is widely used in diagnostic tests for paroxysmal nocturnal hemoglobinuria (PNH), a disease caused by somatic mutations in the <em>PIGA</em>, a gene involved in the biosynthesis of GPI anchors. Beyond diagnostics, proaerolysin has recently been applied in basic research, including its use as a counter-selection agent in genetic manipulations and as an engineered nanopore for single-molecule detection. Although the bacterial expression and purification of proaerolysin have been previously reported, the yields were low due to its low solubility. Here, we demonstrate that using the SHuffle <em>E. coli</em> strain, which facilitates the disulfide bond formation in the cytoplasm, significantly improves the solubility and proper folding of proaerolysin. We achieved a high yield of proaerolysin, approximately 3 mg from a 50 mL bacterial culture, with a purity exceeding 99 %. The functionality of recombinant proaerolysin was confirmed through testing in mouse embryonic stem cells (mESCs), demonstrating that this high-yield production method provides a reliable and cost-effective source of functional proaerolysin for a wide range of biotechnological applications.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106754"},"PeriodicalIF":1.4,"publicationDate":"2025-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144249359","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Strategies for generating soluble and monomeric samples of Ycf1p NBD2 生成Ycf1p NBD2可溶性和单体样品的策略

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-03 DOI: 10.1016/j.pep.2025.106752

Sarah E.S. Quail , Jeffrey Youn , Voula Kanelis

{"title":"Strategies for generating soluble and monomeric samples of Ycf1p NBD2","authors":"Sarah E.S. Quail , Jeffrey Youn , Voula Kanelis","doi":"10.1016/j.pep.2025.106752","DOIUrl":"10.1016/j.pep.2025.106752","url":null,"abstract":"<div><div>The yeast cadmium factor 1 protein (Ycf1p) is an ATP-binding cassette (ABC) transporter that is located in the vacuolar membrane and is responsible for transporting glutathione-conjugated metals from the cytoplasm into the vacuole. Ycf1p contains the ABC core structure of two transmembrane domains (TMD1, TMD2) and two nucleotide-binding domains (NBD1, NBD2). As a member of the C-subfamily of ABC proteins (ABCC), Ycf1p also contains an N-terminal extension comprised of an additional TMD (TMD0) and L0 linker. Although high-resolution structures of many ABC transporters have been determined, the NBDs can be at low resolution in cryo-EM maps. Thus, studies of the isolated cytosolic NBDs are crucial for obtaining molecular-level details of the dynamics of these catalytic entities, for example. In this study, we present a scheme for obtaining samples of NBD2 from the yeast cadmium factor 1 protein (Ycf1p) in a soluble, monomeric, and functional form. While production of NBD1 from Ycf1p and other ABC proteins has been accomplished, generating samples of NBD2 from different ABC proteins has been elusive for the most part, particularly for ABCC proteins. We show that NBD2 preparation necessitates minimizing dimerization and aggregation of the protein at multiple steps during the purification, which is accomplished by employing a solubility tag, eliminating nucleotides from the buffers, and limiting the duration of spin concentrating steps. This work lays the foundation for detailed studies of Ycf1p NBD2 and provides an outline for optimizing the generation of samples of NBD2 from other ABC proteins.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106752"},"PeriodicalIF":1.4,"publicationDate":"2025-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144231596","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Expression, purification and functional study of mycobacteriophage D29 histidine-asparagine-histidine endonuclease 分支噬菌体D29组氨酸-天冬酰胺-组氨酸内切酶的表达、纯化及功能研究。

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-06-02 DOI: 10.1016/j.pep.2025.106753

Bo Fu, Lvming Wu, Xin Wang, Hongbin Sun

引用次数: 0

Bioinformatics analysis and molecular cloning of squalene synthase from Simaroubaceae 角鲨烯合成酶的生物信息学分析及分子克隆。

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-05-30 DOI: 10.1016/j.pep.2025.106751

Yiqing Zhu , Shiyu Wu , Yi Zhang , Shiyang Zhang , Qianyu Zhou , Weidong Zhang , Jinxin Wang , Zhimin Hu

{"title":"Bioinformatics analysis and molecular cloning of squalene synthase from Simaroubaceae","authors":"Yiqing Zhu , Shiyu Wu , Yi Zhang , Shiyang Zhang , Qianyu Zhou , Weidong Zhang , Jinxin Wang , Zhimin Hu","doi":"10.1016/j.pep.2025.106751","DOIUrl":"10.1016/j.pep.2025.106751","url":null,"abstract":"<div><div>Quassinoids are a class of highly oxygenated triterpenoids with C-18, C-19, C-20, C-22, or C-25 skeletons. Squalene synthase (SQS), a key enzyme in the quassinoids biosynthetic pathway, serves as the first step in controlling carbon flux flow into downstream quassinoids. In this study, we screened and analyzed the SQSs from the transcriptome data of the Simaroubaceae family, including AaSQS, BjSQS, AeSQS, QaSQS, ElSQS, and SaSQS. Bioinformatics analysis showed that these SQSs contain C-terminal transmembrane regions and exhibit over 80 % sequence identity with that of <em>Glycyrrhiza glabra</em> (GgSQS1). Phylogenetic analysis revealed that the SQSs from the Simaroubaceae family are more closely related to <em>Malus domestica</em> and <em>Crataegus pinnatifida</em> within the Rosales clade, suggesting an evolutionary trajectory that corroborates the taxonomic classification of Simaroubaceae within the Rosanae superorder. To characterize the function of the SQS from the Simaroubaceae family, the full-length <em>AaSQS</em> was cloned. A soluble AaSQS was obtained by expressing the truncated version lacking 24 amino acids at the C-terminal region in <em>Escherichia coli</em>. Functional analysis showed that AaSQS could catalyze the production of squalene from farnesyl pyrophosphate (FPP). Structural prediction and molecular docking indicated that residues S50, F51, L205, N209, R212, C286, P289, and M313 may be key catalytic residues in AaSQS. Further mutation analysis revealed that all mutants except C286A showed reduced squalene accumulation compared to the wild type (WT). These results provide guidance for quassinoid biosynthesis through metabolic engineering and synthetic biology strategies, particularly by engineering key amino acid residues to enhance enzymatic activity. This study advances the understanding of SQSs in the Simaroubaceae family and provides an important foundation for the study of quassinoid biosynthesis.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"234 ","pages":"Article 106751"},"PeriodicalIF":1.4,"publicationDate":"2025-05-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144199861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Expression and purification of functional recombinant Cullin1-Rbx1/2 in E. coli 功能性重组Cullin1-Rbx1/2在大肠杆菌中的表达与纯化

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-05-28 DOI: 10.1016/j.pep.2025.106750

Fangyu Zhao , Chuntong Li , Xu Li , Luyu Shi , Yingyue Zhang , Han Wang , Shuzhe Sun , Lu-Jun Liang

{"title":"Expression and purification of functional recombinant Cullin1-Rbx1/2 in E. coli","authors":"Fangyu Zhao , Chuntong Li , Xu Li , Luyu Shi , Yingyue Zhang , Han Wang , Shuzhe Sun , Lu-Jun Liang","doi":"10.1016/j.pep.2025.106750","DOIUrl":"10.1016/j.pep.2025.106750","url":null,"abstract":"<div><div>Protein ubiquitination is a crucial post-translational modification in eukaryotes that is mediated by E1-E2-E3 enzymatic cascades and regulates a wide range of cellular processes. Cullin-RING E3 ligases (CRLs) represent the largest family of RING-type E3 ligases and play pivotal roles in these processes. Generating full-length, active Cullin1-Rbx1 (CRL1) is essential for biochemical and biophysical investigations. In this study, we developed an efficient strategy to produce functional CRL1 complexes from <em>E. coli</em>, by fusing an MsyB protein to N-terminus of Cullin1 to improve its solubility. The recombinant CRL1 demonstrated full functionality, successfully assembling with substrate receptor Skp1-Skp2-Cks1 and mediating the polyubiquitination of Ub-p27-degron substrate. Using recombinant CRL1, we found that phosphorylation at Ser65 inhibited the CRL1-UBE2R1 mediated ubiquitin chain elongation on Ub-p27-degron. Furthermore, using the same strategy, we successfully generated Cullin1-Rbx1 mutants and Cullin1-Rbx2 complexes, thereby expanding the applicability of our method. Collectively, this work establishes a rapid and cost-effective platform for the production of CRL1 complexes, facilitating structural and functional studies.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"233 ","pages":"Article 106750"},"PeriodicalIF":1.4,"publicationDate":"2025-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144177701","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0