Sheng-Jiun Wu

TL;DR: Adding an N-linked carbohydrate to the CDR was the most effective route for enhancing the solubility of CNTO607, and the consensus N-glycosylation site in H-CDR2 was reintroduced which was found in the original antibody.

TL;DR: Interestingly, this structure also reveals significant structural differences in the p35 subunit and p35/p40 interface, compared with the published crystal structure of human IL-12, suggesting unusual and potentially functionally relevant structural flexibility of p35, as well as p40/p35 recognition.

TL;DR: Retention times of the antibodies tested were found to be inversely related to solubility, with antibodies prone to precipitate at low concentrations in PBS being retained longer on the columns with broader peaks.

TL;DR: The results provide direct support for the aggregation model that CNTO607 precipitation results primarily from the specific interaction of the Fab arms of neighboring antibodies followed by the development of an extensive network of antibodies inducing large-scale aggregation and precipitation.

TL;DR: The phosphoepitope of AT8 was characterized through both peptide binding studies and costructures with phosphopeptides, and it was shown that AT8 bound to the triply phosphorylated tau peptide 30‐fold stronger than to the pS202/pT205 peptide, supporting the role of pS208 in AT8 recognition.