Titlebook: Recombinant Protein Expression in Mammalian Cells; Methods and Protocol David L. Hacker Book 2018 Springer Science+Business Media, LLC, par

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Genome-Wide High-Throughput RNAi Screening for Identification of Genes Involved in Protein Productie had a profound impact in many areas of basic and applied research. Many groups, both academic and industrial, have been focusing on developing cost-effective methods to improve the production of mammalian proteins that would support potential therapeutic applications. As it stands, while a wide ra

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Application of the CRISPR/Cas9 Gene Editing Method for Modulating Antibody Fucosylation in CHO Cellove both the productivity of recombinant cell lines as well as the quality of therapeutic antibodies. Antibody glycosylation is a critical quality attribute for therapeutic biologics because the glycan patterns on the antibody fragment crystallizable (Fc) region can alter its clinical efficacy and s

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Scalable Production and Purification of Adeno-Associated Viral Vectors (AAV),um in orbital shaken bioreactors and the subsequent purification of vector particles. The protocol for expression of AAV components is based on polyethyleneimine (PEI) mediated transfection of a 2-plasmid system and is specified for production in milliliter to liter scales. After PEI and plasmid DNA

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Considerations in the Use of Codon Optimization for Recombinant Protein Expression,e (1) degeneracy of the genetic code enables most amino acids to be encoded by multiple codons and (2) different mRNAs encoding the same protein can vary dramatically in the amount of protein expressed. However, because codon optimization potentially disrupts overlapping information encoded in mRNA

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Versatile Cell-Free Protein Synthesis Systems Based on Chinese Hamster Ovary Cells,ered mammalian cell lines, this protocol describes the preparation and principle of cell-free protein synthesis systems based on CHO cell lysates. The CHO cell-free system contains endogenous microsomes derived from the endoplasmic reticulum, which enables a direct integration of membrane proteins i

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PEI-Mediated Transient Gene Expression in CHO Cells,ng pDNA, 2.7?mg/L of nonspecific (filler) DNA and 15?mg/L of PEI. The production phase is performed at 31?°C in the presence of 0.25% .,.-dimethylacetamide (DMA). We also provide information on culture vessel options, recommended working volumes, and recommended shaking speeds for transfections at scales from 2?mL to 2?L.

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Recombinant CHO Cell Pool Generation Using piggyBac Transposon System,(PEI). This is followed by a genetic selection for the generation of a cell pool. The resulting cell pool can be used to start a batch or fed-batch culture. Alternatively it can be used for generation of clonal cell lines or generation of cell banks for future use.