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Titlebook: Recombinant Gene Expression; Argelia Lorence Book 2012Latest edition Springer Science+Business Media, LLC 2012 Bacteria.Bacteria.Recombina

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发表于 2025-3-21 20:08:34 | 显示全部楼层 |阅读模式
书目名称Recombinant Gene Expression
编辑Argelia Lorence
视频video
概述Contains new protocols and topics not yet covered.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts.Includes supplementary m
丛书名称Methods in Molecular Biology
图书封面Titlebook: Recombinant Gene Expression;  Argelia Lorence Book 2012Latest edition Springer Science+Business Media, LLC 2012 Bacteria.Bacteria.Recombina
描述.Studies related to recombinant gene expression have brought new advance such as  the emergence of the “omics” technologies. While Escherichia coli, Sacharomyces cerevisiae and insect cells continue to be the dominant production platforms of recombinant proteins. .In Recombinant Gene Expression: Review and Protocols, Third Edition., expert researchers in the field detail many of the methods now commonly used to study recombinant gene expression. These include methods and techniques for bacteria, lower eukaryotes, fungi, plants and plant cells, and animals and animal cells. Written in the highly successful .Methods in Molecular Biology™. series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.. .Authoritative and practical, .Recombinant Gene Expression: Review and Protocols, Third Edition. seeks to aid scientists in the further study of this crucially important research into recombinant gene expression. .
出版日期Book 2012Latest edition
关键词Bacteria; Bacteria; Recombinant Gene Expression; animal cells; animal cells; fungi; fungi; lower eukaryotes
版次3
doihttps://doi.org/10.1007/978-1-61779-433-9
isbn_softcover978-1-4939-6221-1
isbn_ebook978-1-61779-433-9Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC 2012
The information of publication is updating

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A New Bacterial Co-expression System for Over-expressing Soluble Protein and Validating Protein–ProtHEX, which is compatible, and thus can be partnered, with many commercially available . vectors, such as pGEX and pMAL. Either of the vectors allows proteins to be expressed individually as a tagged fusion protein and can be used directly for protein co-purification. This protocol presents the experimental procedure for the co-expression method.
发表于 2025-3-22 02:24:17 | 显示全部楼层
Recombinant Protein Production in the Eukaryotic Protozoan Parasite ,: A Reviewmammalian-type posttranslational modification of target proteins. Although there are few examples of recombinant protein expression using this system, it can be an attractive alternative to using mammalian cells. This chapter presents an overview of the newly developed protein expression system based on ..
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Routine Identity Confirmation of Recombinant Proteins by MALDI-TOF Mass Spectrometry direct means to unequivocally confirm identity of recombinant proteins based on predicted peptide profiles. Many universities or research institutions now carry mass spectrometry instrumentation as part of their core bioanalytical facilities or provide public service to outside investigators. This
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A Matter of Packaging: Influence of Nucleosome Positioning on Heterologous Gene Expression genes. Genome-wide chromatin analyses have shown that there are common chromatin organization patterns for most genes but have also revealed important differences in nucleosome positioning throughout the genome. Such chromatin heterogeneity is one of the reasons why recombinant gene expression is h
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Tools of the Trade: Developing Antibody-Based Detection Capabilities for Recombinant Proteinsrtant and widely used antibody-based procedures for recombinant protein applications are Western immunoblotting and enzyme-linked immunosorbent assays (ELISAs). These analyses require well-characterized, sensitive, and high-affinity antibodies that specifically and selectively recognize the recombin
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Optimization of Purification Protocols Based on the Step-by-Step Monitoring of the Protein Aggregatee aggregates of different complexity widely represented in such fractions. The use of fusing target protein domains to highly soluble carriers may strongly contribute to soluble aggregate accumulation. Therefore, reliable analytical methods must be used to evaluate the biophysical characteristics of
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