A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors.
Sign Up to like & getrecommendations! Published in 2019 at "Methods in molecular biology"
DOI: 10.1007/978-1-4939-8958-4_20
Abstract: Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines. Such Fc-effector functions are largely controlled by posttranslational modifications (PTMs) within the Fc, including… read more here.
Keywords: detect binding; binding hyper; glycan receptors; method detect ... See more keywords
Target-Mediated Drug Disposition Affects the Pharmacokinetics of Interleukin-10 Fragment Crystallizable Fusion Proteins at Pharmacologically Active Doses
Sign Up to like & getrecommendations! Published in 2022 at "Drug Metabolism and Disposition"
DOI: 10.1124/dmd.121.000799
Abstract: Fragment crystallizable (Fc) fusion is commonly used for extending the half-life of biotherapeutics such as cytokines. In this work, we studied the pharmacokinetics of Fc-fused interleukin-10 (IL-10) proteins that exhibited potent antitumor activity in mouse… read more here.
Keywords: disposition; fusion; pharmacologically active; fragment crystallizable ... See more keywords