7/30/2023 0 Comments Antibody production cellsGangwar N, Mishra R, Budholiya N, Rathore AS (2021) Effect of vitamins and metalions on productivity and charge heterogeneity of IgG1 expressed in CHO cells. įreilich R, Arhar T, Abrams JL, Gestwicki JE (2018) Protein-protein interactions in the molecular chaperone network. Įszterhas SK, Bouhassira EE, Martin DI, Fiering S (2002) Transcriptional interference by independently regulated genes occurs in any relative arrangement of the genes and is influenced by chromosomal integration position. ĭoronina VA, Wu C, de Felipe P, Sachs MS, Ryan MD, Brown JD (2008) Site-specific release of nascent chains from ribosomes at a sense codon. ĭe Nardis C, Hendriks LJA, Poirier E, Arvinte T, Gros P, Bakker ABH, de Kruif J (2017) A new approach for generating bispecific antibodies based on a common light chain format and the stable architecture of human immunoglobulin G(1). ĭahodwala H, Lee KH (2019) The fickle CHO: a review of the causes, implications, and potential alleviation of the CHO cell line instability problem. Ĭromwell ME, Hilario E, Jacobson F (2006) Protein Aggregation and Bioprocessing. Ĭhennamsetty N, Helk B, Voynov V, Kayser V, Trout BL (2009) Aggregation-prone motifs in human immunoglobulin G. īuchanan A, Clementel V, Woods R, Harn N, Bowen MA, Mo W, Popovic B, Bishop SM, Dall’Acqua W, Minter R, Jermutus L, Bedian V (2013) Engineering a therapeutic IgG molecule to address cysteinylation, aggregation and enhance thermal stability and expression. īrinkmann U, Kontermann RE (2017) The Making of Bispecific Antibodies. īorth N, Mattanovich D, Kunert R, Katinger H (2005) Effect of increased expression of protein disulfide isomerase and heavy chain binding protein on antibody secretion in a recombinant CHO cell line. īickel F, Herold EM, Signes A, Romeijn S, Jiskoot W, Kiefer H (2016) Reversible NaCl-induced aggregation of a monoclonal antibody at low pH: characterization of aggregates and factors affecting aggregation. īayat H, Hossienzadeh S, Pourmaleki E, Ahani R, Rahimpour A (2018) Evaluation of different vector design strategies for the expression of recombinant monoclonal antibody in CHO cells. īarzadd MM, Lundqvist M, Harris C, Malm M, Volk AL, Thalén N, Chotteau V, Grassi L, Smith A, Abadi ML, Lambiase G, Gibson S, Hatton D, Rockberg J (2022) Autophagy and intracellular product degradation genes identified by systems biology analysis reduce aggregation of bispecific antibody in CHO cells. Reducing the aggregations can improve the quality of recombinant antibodies.Īlam ME, Slaney TR, Wu L, Das TK, Kar S, Barnett GV, Leone A, Tessier PM (2020) Unique impacts of methionine oxidation, tryptophan oxidation, and asparagine deamidation on antibody stability and aggregation.Intracellular environment and extracellular parameters influence recombinant antibody aggregation.The recombinant antibody aggregation in mammalian cell systems is reviewed. In this review, we discuss recent progress in the field of RTAs aggregation, with a focus on factors that cause aggregation during RTA production and the development of strategies for overcoming RTA aggregation. Therefore, the mechanisms underlying RTA aggregation and measures for avoiding aggregation are interesting topics in RTAs research. RTA aggregations are especially concerning as they can trigger human immune responses in humans and may be fatal. A major limitation associated with the use of RTAs is their aggregation, which can be caused by a variety of factors this results in a reduction of quality. Recombinant therapeutic antibodies (RTAs) are among the most important and promising RTPs for biomedical applications. Nowadays, most RTPs approved for marketing are produced in Chinese hamster ovary (CHO) cells. In the HAT medium, aminopterin, a dihydrofolate reductase inhibitor, is used to inhibit de novo nucleotide synthesis pathway, while exogenous hypoxanthine and thymidine are supplied to ensure DNA synthesis can be carried out via the salvage pathway.Mammalian cell lines are frequently used as the preferred host cells for producing recombinant therapeutic proteins (RTPs) having post-translational modified modifications similar to those observed in proteins produced by human cells.
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