Protein expression and purification最新文献_第3页

Purification and characterization of full-length monomeric TEC family kinase, ITK

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-31 DOI: 10.1016/j.pep.2025.106682

Udumbara M. Rathnayake , Junya Wada , Vanessa E. Wall , Jane Jones , Lisa M. Jenkins , Amy H. Andreotti , Lawrence E. Samelson

{"title":"Purification and characterization of full-length monomeric TEC family kinase, ITK","authors":"Udumbara M. Rathnayake , Junya Wada , Vanessa E. Wall , Jane Jones , Lisa M. Jenkins , Amy H. Andreotti , Lawrence E. Samelson","doi":"10.1016/j.pep.2025.106682","DOIUrl":"10.1016/j.pep.2025.106682","url":null,"abstract":"<div><div>An early step in the activation of T cells via the T cell antigen receptor is the phosphorylation and activation of phospholipase C-γ1 (PLC-γ1) by the TEC family tyrosine kinase, interleukin-2 (IL-2) inducible T cell kinase (ITK). PLC-γ1 activation occurs within a multi-protein complex comprised of the enzymes ITK, PLC-γ1, and VAV, and the adapter molecules, LAT, Gads, SLP-76, and NCK. Studies of ITK activation and the role of this heptameric complex in regulating ITK activation and function have not been possible due to the lack of success in the expression and purification of full-length, monomeric ITK protein. In this study, we have produced soluble full-length wild-type ITK protein by co-expressing an N-terminal solubility-tagged ITK construct with a kinase-specific co-chaperone CDC37 in an insect cell line. Although the majority of the purified ITK protein is oligomerized, there is a 13-fold increase in the yield of monomeric protein production compared to the last reported purification. Previous studies suggest that the ITK oligomerization is mediated by intermolecular interactions. We created several mutants to disrupt these self-associations. Expression of one of these, the C96E/T110I mutant, produced 20 times more monomer than the wild-type construct. The <em>in vitro</em> characterization of these protein constructs showed that the purified protein is stable and functional. This successful purification and <em>in vitro</em> characterization of full-length monomeric ITK protein will aid in understanding the mechanism by which ITK is recruited into the heptameric complex and is enabled to phosphorylate and activate PLC-γ1.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106682"},"PeriodicalIF":1.4,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143080758","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

A FRET-based competitive binding assay using coumestrol and the ligand-binding domain of human estrogen receptor alpha tagged with mTurquoise2 efficiently expressed in E. coli with ethanol

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-30 DOI: 10.1016/j.pep.2025.106667

Edith O. López-Romero , Emma L. Arévalo-Salina , César Arcos-Hernández , Yoloxochitl Sánchez-Guevara , Carmen Beltrán , Gloria Saab-Rincón , Takuya Nishigaki

{"title":"A FRET-based competitive binding assay using coumestrol and the ligand-binding domain of human estrogen receptor alpha tagged with mTurquoise2 efficiently expressed in E. coli with ethanol","authors":"Edith O. López-Romero , Emma L. Arévalo-Salina , César Arcos-Hernández , Yoloxochitl Sánchez-Guevara , Carmen Beltrán , Gloria Saab-Rincón , Takuya Nishigaki","doi":"10.1016/j.pep.2025.106667","DOIUrl":"10.1016/j.pep.2025.106667","url":null,"abstract":"<div><div>The estrogen receptor (ER) is a nuclear receptor and one of the most extensively researched targets in the study of endocrine-disrupting chemicals (EDCs). Many biosensors and bioassays for estrogenic EDCs use the ligand-binding domain of human ERα (LBD-hERα) as a biological recognition element. However, the LBD-hERα is poorly stable and difficult to produce as a functional LBD-hERα in the <em>E. coli</em> expression system. In this study, we efficiently expressed the functional LBD-hERα tagged with the cyan fluorescent protein, mTurquoise2 (LBD-hERα-mTq2) by the addition of ethanol (3 %) to <em>E. coli</em> suspension during protein expression (> 40 times more compared to without ethanol). We found that ethanol not only promoted the proper folding of LBD-hERα-mTq2, but also prevented the proteolysis of poorly folded recombinant proteins. We established a FRET-based binding assay between a fluorescent estrogen, coumestrol, and the LBD-hERα-mTq2, in which the formation of the complex exhibits a significant degree of FRET. A subsequent competitive binding assay with diethylstilbestrol demonstrates that our system successfully functions as a simple and reliable bioassay to detect estrogenic EDCs.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106667"},"PeriodicalIF":1.4,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143075100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Preparation and characterization of LGR5 LOOP region-specific nanobodies

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-30 DOI: 10.1016/j.pep.2025.106680

Li Jia , Huarui Qiao , Yuting Ding , Qianqian Cui , Yingjun Wang , Jing Geng , Junming Tang , Jianfeng Xu , Yuanyuan Dai , Yong Geng

{"title":"Preparation and characterization of LGR5 LOOP region-specific nanobodies","authors":"Li Jia , Huarui Qiao , Yuting Ding , Qianqian Cui , Yingjun Wang , Jing Geng , Junming Tang , Jianfeng Xu , Yuanyuan Dai , Yong Geng","doi":"10.1016/j.pep.2025.106680","DOIUrl":"10.1016/j.pep.2025.106680","url":null,"abstract":"<div><div>Leucine-rich repeat-containing G-protein-coupled receptor 5 (LGR5), also known as G-protein-coupled receptor 49 (GPR49), is a class A G-protein-coupled receptor (GPCR) that plays a pivotal role in embryonic development and functions as a marker for adult stem cells in various tissues and organs. LGR5 possesses a large extracellular domain (ecto-domain) enriched with leucine-rich repeats (LRR), primarily responsible for binding to ligands such as R-spondins. The C-terminal LRR extracellular LOOP region of LGR5 refers to the loop structure connecting the C-terminus of LGR5 to the first transmembrane helix. As the LOOP region is located extracellularly, it is readily accessible to exogenous molecules such as antibodies, nanobodies, or small-molecule drugs. In this study, we successfully expressed and purified the LGR5 LOOP region protein in a prokaryotic expression system. The purified protein was subsequently used as an antigen to immunize camels, leading to the generation of nanobodies. These nanobodies are composed solely of the variable domain of the heavy-chain antibody (VHH), with a molecular weight of approximately 15 kDa. Using the purified LGR5 LOOP region protein as an antigen, we isolated nanobodies that specifically bind to it. Subsequent assays demonstrated that the selected nanobody, NB 4C4 and NB 3E8, specifically targeted the LGR5 LOOP region, exhibited an inhibitory effect on β-catenin-mediated Wnt signaling to a certain extent. This study provides insights for the development of LGR5-targeted diagnostic reagents and antibody-based therapeutic strategies.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106680"},"PeriodicalIF":1.4,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143075103","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

Screening and preparation of nanobodies for SIGLEC-15 detection

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-27 DOI: 10.1016/j.pep.2025.106679

Shuaiying Zhao , Lingyun Li , Zhongyun Lan , Xiangyun Hou , Ruimin Huang , Quanfang Jin , Qiting Huang , Li Jia , Yingying Kong , Jianchuan Wen , Huarui Qiao , Yiang Wang , Yiwen Xu , Dongna Zhang , Yong Geng , Jianfeng Xu , Yuanyuan Dai

{"title":"Screening and preparation of nanobodies for SIGLEC-15 detection","authors":"Shuaiying Zhao , Lingyun Li , Zhongyun Lan , Xiangyun Hou , Ruimin Huang , Quanfang Jin , Qiting Huang , Li Jia , Yingying Kong , Jianchuan Wen , Huarui Qiao , Yiang Wang , Yiwen Xu , Dongna Zhang , Yong Geng , Jianfeng Xu , Yuanyuan Dai","doi":"10.1016/j.pep.2025.106679","DOIUrl":"10.1016/j.pep.2025.106679","url":null,"abstract":"<div><div>As an important member of the Siglec family, SIGLEC-15 plays an important role in osteoclast differentiation, bone remodeling, and tumor immune evasion. In the tumor microenvironment, SIGLEC-15 functions independently of the B7-H1/PD-1 pathway. In this study, the SIGLEC-15 fusion protein (SIGLEC-15-Fc) was successfully expressed and purified using a eukaryotic expression system. This protein was then used as an antigen to immunize camelids, inducing the production of specific nanobodies (VHHs) targeting SIGLEC-15. The resulting nanobodies exhibited a molecular weight of approximately 15 kDa. After screening, we identified two nanobody strains, Nb1C8 and Nb2D7, both of which bind SIGLEC-15 without competition. We confirmed the nanobodies’ high affinity and stability through Octec platform and stability analyses. Flow cytometry analysis demonstrated that Nb1C8 and Nb2D7 specifically binds to SIGLEC-15 which naturally expressed on bladder cancer cells. This study marks the first development of nanobodies specifically targeting SIGLEC-15, providing a solid foundation for the development of SIGLEC-15-related diagnostic tools and antibody therapeutics.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106679"},"PeriodicalIF":1.4,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143067526","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

Praesto Jetted A50 HipH, a mild pH elution protein A resin, exhibits improved aggregate separation capability and protein elution from it shows unique response to mobile phase additive sodium chloride

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-27 DOI: 10.1016/j.pep.2025.106677

Wenwen Lu, Yan Wan, Yifeng Li

{"title":"Praesto Jetted A50 HipH, a mild pH elution protein A resin, exhibits improved aggregate separation capability and protein elution from it shows unique response to mobile phase additive sodium chloride","authors":"Wenwen Lu, Yan Wan, Yifeng Li","doi":"10.1016/j.pep.2025.106677","DOIUrl":"10.1016/j.pep.2025.106677","url":null,"abstract":"<div><div>Protein A affinity chromatography has been widely used for product capture in monoclonal antibody (mAb), bispecific antibody (bsAb) and Fc-fusion protein purification. However, the low pH (i.e., 3.0–3.5) required for elution may cause aggregation and/or truncation for pH-sensitive molecules. Praesto Jetted A50 HipH from Purolite is a newly launched Protein A resin whose ligand is engineered to enable antibody/Fc-fusion elution at a milder pH (i.e., 4.6 or above) and therefore is more suitable to pH-sensitive molecules. In the current study, we demonstrated that this new Protein A resin, besides allowing mild elution, also possesses improved aggregate separation capability in comparison to traditional Protein A resins. While traditional Protein A resins generally lack any aggregate separation capability, Jetted A50 HipH can remove up to 70% of the aggregates in the load while maintaining good monomer recovery. In addition, we discovered that protein elution from Jetted A50 HipH column responded to mobile phase additive sodium chloride differently from that from traditional Protein A columns (elution was promoted rather than suppressed). This property enables elution at further increased pH (i.e., 5) when proper amount of sodium chloride is included in the elution buffer. Thus, Jetted A50 HipH is a better choice than traditional Protein A resins for pH-sensitive and/or aggregation-prone mAbs, bsAbs and Fc-fusion proteins.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106677"},"PeriodicalIF":1.4,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143047668","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

Simplified purification process of AsnB3 deamidated insulin variant and its comparison with human insulin

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-26 DOI: 10.1016/j.pep.2025.106665

Chinnappa Reddy V , Koduru Srivatsa , Navratna Vajpai , Ganeshan R , Aditya Upadhya , Apoorva Srivastava , Somesh B P , Kishore K.R. Tetala , Ashutosh Kumar , Partha Hazra

引用次数: 0

Expression, characterization and anti-colon cancer activity of recombinant ginseng peptides with amino acid tandem repeats

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-23 DOI: 10.1016/j.pep.2025.106663

Yu Feng , Weina Li , Weigang Yuwen , Ru Xu , Chenhui Zhu , Zhiguang Duan , Daidi Fan

{"title":"Expression, characterization and anti-colon cancer activity of recombinant ginseng peptides with amino acid tandem repeats","authors":"Yu Feng , Weina Li , Weigang Yuwen , Ru Xu , Chenhui Zhu , Zhiguang Duan , Daidi Fan","doi":"10.1016/j.pep.2025.106663","DOIUrl":"10.1016/j.pep.2025.106663","url":null,"abstract":"<div><div>Ginseng peptides, small molecule active ingredients in ginseng, are mainly extracted naturally or synthesized chemically, but high costs and difficulties hinder further research. In this study, a ginseng hexapeptide FKEHGY, named antitumor peptide 0601 (AT0601) and its five tandem sequence repeats AT0605, were expressed in <em>Bacillus subtilis</em> WB600 for the first time, and the bioactivity study showed that the anticancer activity of AT0605 was even significantly higher than that of AT0601 for colon cancer CT26 cells, with IC50s of 16.82 ± 1.3 μM (48 h) and 855.57 ± 6.04 μM (48 h), respectively, i.e. AT0605 achieves the same inhibition rate for CT26 cells at a concentration 50 times lower than that of AT0601. Similar to the ginseng peptide AT0601, recombinant AT0605 also inhibited cell growth by blocking cells in the G1 phase and activated the mitochondria-associated caspase pathway to induce apoptosis. In conclusion, all two kinds of the recombinant ginseng peptides could also inhibit cell proliferation through mechanisms such as inhibiting cell cycle arrest and inducing a decrease in mitochondrial membrane potential.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106663"},"PeriodicalIF":1.4,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143041299","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

Bacterial expression, purification and characterization of the human Dectin-1 lectin domain for structural and functional studies

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-23 DOI: 10.1016/j.pep.2025.106668

Hanako Chiba , Noriyoshi Manabe , Junko Naito , Norihisa Nishida , Naohito Ohno , Yoshiki Yamaguchi

{"title":"Bacterial expression, purification and characterization of the human Dectin-1 lectin domain for structural and functional studies","authors":"Hanako Chiba , Noriyoshi Manabe , Junko Naito , Norihisa Nishida , Naohito Ohno , Yoshiki Yamaguchi","doi":"10.1016/j.pep.2025.106668","DOIUrl":"10.1016/j.pep.2025.106668","url":null,"abstract":"<div><div>Dectin-1 (CLEC7A), a C-type lectin-like receptor that recognizes β-1,3 glucans, has a key role in the innate immune system. While the lectin domain of mouse Dectin-1 has been solubilized and refolded from inclusion bodies in <em>Escherichia coli</em>, similar refolding of the human Dectin-1 lectin domain is hindered by the formation of misfolded multimers with aberrant intermolecular disulfide bonds. The aim of this study was to develop a method for the large-scale production of the human Dectin-1 lectin domain. Based on a protocol for the murine domain, the human Dectin-1 lectin domain was expressed as a fusion protein with Protein G B1, a solubility-enhancing tag. The refolding and purification conditions were then optimized by testing a range of buffers with and without Ca<sup>2+</sup> ions. The inclusion of 1 mM Ca<sup>2+</sup> ions in both the refolding and purification buffers resulted in high yields of a monomeric form of the human Dectin-1 lectin. The resulting recombinant protein was demonstrated to be functional, showing specific binding to the β-glucan laminarin as verified by thermal shift assays, gel filtration chromatography and NMR. Furthermore, NMR experiments revealed that the human Dectin-1 lectin domain binds Ca<sup>2+</sup> ions. The recombinant protein will support structural biology studies to clarify differences in β-glucan binding specificity between human and mouse Dectin-1, and to explore the effects of mutations on the functionality of human Dectin-1.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106668"},"PeriodicalIF":1.4,"publicationDate":"2025-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143041295","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 recombinant human FVII in CHO cells using the piggyBac transposon system

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-22 DOI: 10.1016/j.pep.2025.106666

Zhen Yang , Xueyun Wang , Shan Luo , Hui Li , Jiangbo Xu , Linlin Liang , Zhimin He , Guangyuan Wang , Zhuobin Wu , Nan Zhong , Haijun Xiang , Zhan Zhang , Caiping Guo , Yunjia Zhang , Fei Yan

{"title":"Efficient production of recombinant human FVII in CHO cells using the piggyBac transposon system","authors":"Zhen Yang , Xueyun Wang , Shan Luo , Hui Li , Jiangbo Xu , Linlin Liang , Zhimin He , Guangyuan Wang , Zhuobin Wu , Nan Zhong , Haijun Xiang , Zhan Zhang , Caiping Guo , Yunjia Zhang , Fei Yan","doi":"10.1016/j.pep.2025.106666","DOIUrl":"10.1016/j.pep.2025.106666","url":null,"abstract":"<div><div>As an important coagulation factor, activated coagulation factor VII (FVIIa) is mainly used to treat the bleeding of hemophilia patients who have developed inhibitory antibodies against FVIII and FIX conventional treatment. Recombinant human factor VII (rhFVII) produced in mammalian cell lines have been developed as the most important resource of FVIIa. However, cell lines express rhFVII protein derived from an exogenous expression vector at a lower level than most other proteins. In the current study, we have shown efficient rhFVII production in CHO cell lines using piggyBac (PB) transposon system. rhFVII is successfully expressed in fed-batch culture of CHO cells, and the expression of rhFVII up to 100 mg/L. Moreover, the purified secreted rhFVII was determined by SDS-PAGE and Western Blot. The coagulation activity was determined by the chromogenic Activity ELISA kit. In conclusion, this study has demonstrated that the piggyBac transposon system can be used for an efficient production of recombinant FVII.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"229 ","pages":"Article 106666"},"PeriodicalIF":1.4,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143028957","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

A systematic approach for scalable purification of virus-like particles 一种可扩展的病毒样颗粒纯化的系统方法。

IF 1.4 4区生物学

Protein expression and purification Pub Date : 2025-01-17 DOI: 10.1016/j.pep.2025.106664

Enoch Y. Park , Robert Minkner

{"title":"A systematic approach for scalable purification of virus-like particles","authors":"Enoch Y. Park , Robert Minkner","doi":"10.1016/j.pep.2025.106664","DOIUrl":"10.1016/j.pep.2025.106664","url":null,"abstract":"<div><div>Virus-like particles (VLPs) are increasingly recognized as promising vaccine candidates and drug-delivery platforms because they do not contain genetic materials, mimic viral structures, and possess strong antigenic properties. Various hosts, including microorganisms, yeast, and insect cells, are commonly used for VLP expression. Recently, silkworms have emerged as a significant host for producing VLPs, providing a cost-effective and straightforward approach for large-scale expression. Despite the progress in VLP expression technology, purification methods for VLPs are still in their infancy and often rely on unscalable ultracentrifugation techniques. Moreover, VLP purification represents a substantial portion of the overall production cost, highlighting the urgent need for efficient and scalable downstream processing methods to overcome the current challenges in VLP production. Considering their differing structures and properties, this review systematically summarizes the published results of scalable downstream processes for both enveloped and non-enveloped VLPs. Its aim is to provide a comprehensive overview and significantly contribute to developing future VLP production for pharmaceutical applications, thereby guiding and inspiring further research in this field.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"228 ","pages":"Article 106664"},"PeriodicalIF":1.4,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010350","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