Menu
0

FcRn/PK-Modulated Antibody Expression Vectors

Human IgG1 Fc-engineered expression vectors for investigating FcRn interactions, antibody recycling, and pharmacokinetic modulation, including YTE, LS, LA, QL, and other Fc variants.

FcRn / PK-MODULATED ANTIBODY EXPRESSION VECTOR SELECTION GUIDE

Compare eight human IgG1 Fc variants for studies of FcRn binding, antibody persistence, and altered clearance.

Catalog No. Variant Engineering Mechanism Selection Guidance
AFV-06 Human IgG1 (YTE) M252Y / S254T / T256E Established FcRn-engineering variant for investigating pH-dependent FcRn binding and potential half-life extension.
AFV-26 Human IgG1 (LA) M428L / N434A Dual-residue FcRn-interface variant for comparing recycling-related binding properties with LS and other Fc variants.
AFV-27 Human IgG1 (LS) M428L / N434S Widely studied FcRn-enhancing variant for evaluating extended antibody persistence.
AFV-28 Human IgG1 (QL) T250Q / M428L FcRn-interface engineering for studying pH-dependent binding and pharmacokinetic modulation.
AFV-29 Human IgG1 (YTE + KF) M252Y / S254T / T256E / H433K / N434F Combined FcRn-interface mutations for comparative binding and recycling studies; functional direction requires experimental validation.
AFV-30 Human IgG1 (I253A) I253A FcRn-contact-site substitution for investigating reduced FcRn binding and altered recycling or clearance.
AFV-31 Human IgG1 (N434A) N434A Single-residue FcRn-interface variant for comparative pH-dependent binding studies.
AFV-32 Human IgG1 (V308P) V308P Fc variant for investigating changes in FcRn interaction and antibody disposition.

FcRn affinity, pH selectivity, recycling, and in vivo half-life depend on antibody sequence, Fc context, species, and assay conditions. Evaluate binding at acidic and near-neutral pH and validate pharmacokinetics experimentally.

Showing all 8 results