Introducing AlligBAITOR™: A Universal Antibody-Binding Protein for Pan-Antibody Capture and Depletion
A recent study published on bioRxiv (Kadavá et al., 2026) sheds new light on the remarkable binding properties of AlligBAITOR — revealing why it stands out as a truly universal immunoglobulin-binding tool.
AlligBAITOR was shown to bind all major human antibody isotypes and subclasses — IgG1–4, IgA1–2, and IgM — with high affinity and without detectable bias. In affinity pull-down experiments from human serum, AlligBAITOR captured more than 99% of IgG and IgA, and 93% of IgM, while co-purifying minimal non-antibody proteins. This pan-isotype specificity is unique to AlligBAITOR, enabling a broader application potential than isotype-specific immunoglobulin binders.
The study also revealed a highly consistent binding stoichiometry: exactly two AlligBAITOR molecules bind per antibody protomer, regardless of oligomeric state, light chain type, Fab glycosylation, or J-chain incorporation. This predictable behavior makes AlligBAITOR well-suited for quantitative applications.
AlligBAITOR binds conserved regions of the Fab domain, meaning AlligBAITOR can engage antibodies across isotypes at the antigen-binding site — enabling efficient displacement of antigens from pre-formed immune complexes — while leaving Fc-mediated interactions intact.
These properties position AlligBAITOR as a versatile new tool for:
- Pan-antibody affinity capture from complex biological matrices such as serum
- Antibody depletion for downstream proteomics or functional assays
- Isotype-unbiased antibody profiling
AlligBAITOR is now available from Genovis! 🌟
