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ADCC,CDC,ADCP enhancement, silence and half-life extension serviceOne-stop solution from sequence design to pharmacology
The basic structure of an antibody contains an antigen-binding domain (Fab domain) and a crystalline segment (Fc domain). The function of therapeutic antibodies depends not only on the activity of the Fab domain in binding target antigens but also on the interaction of the Fc domain with the Fc receptor. The Fc receptor is expressed on the surface of specific immune cell receptors and is associated with the Fc domain, it can be classified as FcγRI (CD64), FcγRII (CD32), FcγRIII (CD16) and FcRn. The antibody efficacy and half-life can be improved by modifying the amino acid sequence of the Fc region.
ProBio provides the most comprehensive Fc engineering(enhancement, silence, half-life extension ) service and one-stop Fc engineering solutions from sequence design to in vitro bioassay and in vivo pharmacology.
STR Fc silencing technology
Comprehensive services
One-stop solution
ProBio is partnered with mAbsolve to offer STR silencing technology. Customers benefit directly from STR Fc silencing technology licensed by ProBio.
ProBio offers mAbsolve's licensed STR technology and free-to-operate Fc silencing technologies according to customers' needs. Click "Contact Us" for more details.
Fc domain binding to Fc receptors mediates the different antibody effects, such as ADCC and ADCP effects by FcγRs, CDC effects by C1q, and FcRn is associated with the half-life of proteins.
The enhancement of Fc region-mediated effector functions, for instance, ADCC or ADCP effects enhanced by the affinity of the Fc domain to the FcγRIII(CD16), improves antibody efficacy.
ProBio provides multiple Fc engineering solutions for ADCC, CDC, and ADCP enhancement.
Click “Contact Us” , get Fc function enhancement solutions
Two mutated Fc constructs were evaluated for their potency of ADCC and CDC against PA-1 target cells. As claimed, the published Fc mutation sequences showed enhanced ADCC and CDC activities on PA-1 cells.
IgG recycling begins with IgG binding to the FcRn with IgG uptake into an endothelial cell via an acidified endosome. It ultimately ends up with the release of IgG back into the blood. Enhancement of the binding between IgG & FcRn will promote a higher ratio of IgG recycling and improve the antibody serum half-life.
ProBio provides two strategies to elongate antibody serum half-life: FTO mutants, Library screening for novel Fc mutation.
We are keen to benchmark our unique integrated strategy, in particular, the combination of PML and HTP FASEBA affinity screening platforms, applied in Fc engineering strategies to discover variants with higher affinity towards FcRn. In this case, the result showed that the best variant was improved by 33 fold compared to WT, and 3.3 fold comparing the YTE combo.
Raghavan, M., Bonagura, V.R., Morrison, S.L., and Bjorkman, P.J. (1995). Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants. Biochemistry 34, 14649–14657.
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