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Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells
by
Park, Jin Hyoung
, Jin, Jong Hwa
, Lee, Gyun Min
, Lim, Myung Sin
, An, Hyun Joo
, Kim, Jong Won
in
13/1
/ 13/106
/ 38
/ 45
/ 631/1647/2067
/ 631/61/17/1511
/ 64
/ 82
/ 82/58
/ 82/83
/ Animals
/ Antibodies, Monoclonal - genetics
/ Antibodies, Monoclonal - metabolism
/ Antibody Formation
/ Batch Cell Culture Techniques - methods
/ Batch culture
/ Cell culture
/ Cell Proliferation
/ CHO Cells
/ Chromatography, Liquid - methods
/ Cricetinae
/ Cricetulus
/ Culture Media, Conditioned - metabolism
/ Fed-batch culture
/ Glycosylation
/ Humanities and Social Sciences
/ Liquid chromatography
/ Mass spectrometry
/ Mass Spectrometry - methods
/ Mass spectroscopy
/ Monoclonal antibodies
/ multidisciplinary
/ Protein purification
/ Proteins
/ Proteome - genetics
/ Proteome - metabolism
/ Proteomics - methods
/ Quality
/ Recombinant Proteins - metabolism
/ Science
2017
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Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells
by
Park, Jin Hyoung
, Jin, Jong Hwa
, Lee, Gyun Min
, Lim, Myung Sin
, An, Hyun Joo
, Kim, Jong Won
in
13/1
/ 13/106
/ 38
/ 45
/ 631/1647/2067
/ 631/61/17/1511
/ 64
/ 82
/ 82/58
/ 82/83
/ Animals
/ Antibodies, Monoclonal - genetics
/ Antibodies, Monoclonal - metabolism
/ Antibody Formation
/ Batch Cell Culture Techniques - methods
/ Batch culture
/ Cell culture
/ Cell Proliferation
/ CHO Cells
/ Chromatography, Liquid - methods
/ Cricetinae
/ Cricetulus
/ Culture Media, Conditioned - metabolism
/ Fed-batch culture
/ Glycosylation
/ Humanities and Social Sciences
/ Liquid chromatography
/ Mass spectrometry
/ Mass Spectrometry - methods
/ Mass spectroscopy
/ Monoclonal antibodies
/ multidisciplinary
/ Protein purification
/ Proteins
/ Proteome - genetics
/ Proteome - metabolism
/ Proteomics - methods
/ Quality
/ Recombinant Proteins - metabolism
/ Science
2017
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Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells
by
Park, Jin Hyoung
, Jin, Jong Hwa
, Lee, Gyun Min
, Lim, Myung Sin
, An, Hyun Joo
, Kim, Jong Won
in
13/1
/ 13/106
/ 38
/ 45
/ 631/1647/2067
/ 631/61/17/1511
/ 64
/ 82
/ 82/58
/ 82/83
/ Animals
/ Antibodies, Monoclonal - genetics
/ Antibodies, Monoclonal - metabolism
/ Antibody Formation
/ Batch Cell Culture Techniques - methods
/ Batch culture
/ Cell culture
/ Cell Proliferation
/ CHO Cells
/ Chromatography, Liquid - methods
/ Cricetinae
/ Cricetulus
/ Culture Media, Conditioned - metabolism
/ Fed-batch culture
/ Glycosylation
/ Humanities and Social Sciences
/ Liquid chromatography
/ Mass spectrometry
/ Mass Spectrometry - methods
/ Mass spectroscopy
/ Monoclonal antibodies
/ multidisciplinary
/ Protein purification
/ Proteins
/ Proteome - genetics
/ Proteome - metabolism
/ Proteomics - methods
/ Quality
/ Recombinant Proteins - metabolism
/ Science
2017
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Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells
Journal Article
Proteomic Analysis of Host Cell Protein Dynamics in the Culture Supernatants of Antibody-Producing CHO Cells
2017
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Overview
Chinese hamster ovary (CHO) cells are the most common cell line used for the production of therapeutic proteins including monoclonal antibodies (mAbs). Host cell proteins (HCPs), secreted and released from lysed cells, accumulate extracellularly during the cultures of recombinant CHO (rCHO) cells, potentially impairing product quality. In an effort to maintain good mAb quality during the cultures, HCPs accumulated extracellularly in batch and fed-batch cultures of a mAb-producing rCHO cell line were identified and quantified by nanoflow liquid chromatography-tandem mass spectrometry, followed by their gene ontology and functional analysis. Due to higher cell concentration and longer culture duration, more HCPs were identified and quantitated in fed-batch culture (2145 proteins identified and 1673 proteins quantified) than in batch culture (1934 proteins identified and 1486 proteins quantified). Clustering analysis of HCPs showed that the concentration profiles of HCPs affecting mAb quality (Lgmn, Ctsd, Gbl1, and B4galt1) correlated with changes in mAb quality attributes such as aggregation, charge variants, and
N
-glycosylation during the cultures. Taken together, the dataset of HCPs obtained in this study provides insights into determining the appropriate target proteins to be removed during both the cultures and purification steps for ensuring good mAb quality.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 13/106
/ 38
/ 45
/ 64
/ 82
/ 82/58
/ 82/83
/ Animals
/ Antibodies, Monoclonal - genetics
/ Antibodies, Monoclonal - metabolism
/ Batch Cell Culture Techniques - methods
/ Chromatography, Liquid - methods
/ Culture Media, Conditioned - metabolism
/ Humanities and Social Sciences
/ Proteins
/ Quality
/ Recombinant Proteins - metabolism
/ Science
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