2025年2月11日 · Please note, from 2022 the Print ISSN is not in active use as this journal is no longer published in print. International Journal of Digital Earth is a journal focusing on the theories, technologies, applications and societal implications of Digital Earth.. International Journal of Digital Earth is the official journal of the International Society for Digital Earth.

FabALACTICA (IgdE) is a cysteine protease that digests human IgG1 at a specific site above the hinge, generating intact and homogenous Fab and Fc fragments. The enzyme facilitates the characterization of bi- and multispecific antibodies and analyses of …

A novel cysteine protease, IgdE from Streptococcus agalactiae has recently been discovered (1) and has been recombinantly expressed and characterized by Genovis. IgdE digests human IgG1 just above the hinge cysteines, thus gen-erating intact Fab and Fc fragments and was further investigated using clinically approved mAbs.

2016年10月17日 · The novel IgdE family proteases of S. agalactiae, S. pseudoporcinus and S. equi showed IgG subtype specificity, i.e. IgdE from S. agalactiae and S. pseudoporcinus cleaved human IgG1, while IgdE from S. equi was subtype specific for equine IgG7.

2023年12月17日 · IgdE and BdpK have adjacent albeit distinct cleavage sites, whereby BdpK cleaves one Threonine amino acid closer to the N-terminus of IgG1 compared to IgdE. Here, we set out to evaluate whether also BdpK can be used for plasma IgG1 clonal profiling, benchmarking it directly versus IgdE.

IgdE may be utilized for applications including characterization of bi- or multispecific antibodies, monovalent binding studies, crystallization and NMR studies of higher order structure of antibodies.

The inhibition of enzymatic activity with iodoacetamide and Z-LVG-CHN 2 and most importantly the lack of enzymatic activity of the IgdE C302S and IgdE H333A mutant variants strongly suggest that IgdE is a novel and so far unique member of the cysteine protease family.

2018年4月19日 · IgdE is a cysteine protease that cleaves the heavy chains above the hinge disulfide bonds (…KSCDKT/HTCPPC…), yielding two identical Fabs and one Fc fragment. After IgdE digestion, samples were treated with PNGase F and CpB to reduce heterogeneity arising from N-glycosylation and C-terminal lysine.

2018年2月5日 · In this study, we introduced the use of a new enzyme (IgdE) that cleaves mAbs with high specificity at their upper hinge region in non-reducing conditions to investigate their disulfide bridge oxidation state.

Recently we have discovered an IgG degrading enzyme of the endemic pig pathogen S. suis designated IgdE that is highly specific for porcine IgG. This protease is the founding member of a novel cysteine protease family assigned C113 in the MEROPS ...