Quantitative proteomics reveals cellular responses to individual mAb expression and tunicamycin in CHO cells.
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Abstract in brief
- Quantitative proteomic analysis of CHO cells revealed that protein folding and UPR-related proteins are differentially expressed in high versus low antibody-producing cell lines and under tunicamycin-induced ER stress.
- Key proteins such as Hspa9, Dnaja3, Nedd8, and Lgmn are involved in stress responses and protein folding processes, indicating their potential role in enhancing antibody production.
- The study highlights that tunicamycin treatment activates the unfolded protein response at a low level, providing insights into how cellular stress mechanisms impact bioproduction in CHO cells.]
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Proteomics of CHO Cells Reveals Stress Responses to mAb Expression and Tunicamycin
Quantitative proteomics of CHO cells unveils how protein folding and stress response proteins differ between high and low antibody producers under ER stress, providing insights into improving bioproduction efficiency.
Proteomic Insights into CHO Cell Responses to mAb Expression and Tunicamycin
Quantitative proteomics reveals cellular responses to individual mAb expression and tunicamycin in CHO cells, highlighting stress response mechanisms and proteins involved in improving antibody production efficiency.
Proteomic Insights into CHO Cell Responses for Bioproduction Optimization
Quantitative proteomics of CHO cells revealed protein folding and UPR-related proteins are differentially expressed under stress and high antibody production, providing insights to improve bioproduction efficiency.
Cellular Responses to mAb Expression and Tunicamycin in CHO Cells
Quantitative proteomic analysis of CHO cells revealed differential expression of protein folding and UPR-related proteins under stress conditions, providing insights into improving antibody production efficiency and…
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