Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

High‐Level Expression of Recombinant IgG in the Human Cell Line PER.C6

1 Jan 2003

Abstract excerpt

The number of therapeutic monoclonal antibodies in production is expected to rise rapidly in the next few years. As a result, there is much focus on the optimization of antibody expression platforms. Several issues are important including the speed of transition from bench to manufacturing, yield of IgG, and quality (particularly of the glycan structures present on immunoglobulins). We have characterized the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Monoclonal and Polyclonal Antibodies Research
Share to Viral Infectious Diseases and Gene Expression in Insects
Share to Xenotransplantation and immune response

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 12573020
DOI: 10.1021/bp025574h

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

High‐Level Expression of Recombinant IgG in the Human Cell Line PER.C6PMID 12573020Read ↗

High level expression of functional human IgMs in human PER.C6® cellsSemantic proximity Read ↗

Generation of stable cell clones expressing mixtures of human antibodiesSemantic proximity Read ↗

Advances in recombinant antibody manufacturingSemantic proximity Read ↗

The human cell line PER.C6 provides a new manufacturing system for the production of influenza vaccinesSemantic proximity Read ↗

High-throughput generation and engineering of recombinant human antibodiesSemantic proximity Read ↗

Enhancing recombinant antibody yield in Chinese hamster ovary cellsSemantic proximity Read ↗

Production systems for recombinant antibodiesSemantic proximity Read ↗

N‐linked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgGSemantic proximity Read ↗

Glycoengineering design options for IgG1 in CHO cells using precise gene editingSemantic proximity Read ↗

Strategies and Considerations for Improving Recombinant Antibody Production and Quality in Chinese Hamster Ovary CellsSemantic proximity Read ↗

Cell-based production of Fc-GlcNAc and Fc-alpha-2,6 sialyl glycan enriched antibody with improved effector functions through glycosylation pathway engineeringSemantic proximity Read ↗

A global RNA‐seq‐driven analysis of CHO host and production cell lines reveals distinct differential expression patterns of genes contributing to recombinant antibody glycosylationSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.