About InVivoMAb anti-rat FcRn heavy chain heterodimers The 2G3 antibody was raised against soluble rat neonatal Fc receptor (FcRn) in an adjuvant. FcRn is a heterodimer composed of a membrane bound heavy chain attached non-covalently to β2-microgloublin. It is structurally similar to MHC class I molecules. The 2G3 antibody is used in studies of the MHC class I heavy chain FcRn heterodimers and their interaction with IgG. InVivoMAb anti-rat FcRn heavy chain heterodimers Specifications IsotypeMouse IgG1 Recommended Isotype Control(s)InVivoMAb mouse IgG1 isotype control, unknown specificity Recommended Dilution BufferInVivoPure pH 7.0 Dilution Buffer ImmunogenPurified soluble FcRn Reported ApplicationsELISA Flow cytometry FormulationPBS, pH 7.0 Contains no stabilizers or preservatives Endotoxin<2EU/mg (<0.002EU/μg) Determined by LAL gel clotting assay Purity>95% Determined by SDS-PAGE Sterility0.2 μm filtered ProductionPurified from cell culture supernatant in an animal-free facility PurificationProtein G RRIDAB_10950633 Molecular Weight150 kDa StorageThe antibody solution should be stored at the stock concentration at 4°C. Do not freeze. Application ReferencesInVivoMAb anti-rat FcRn heavy chain heterodimers (CLONE: 2G3)Raghavan, M., et al (1994). "Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand" Immunity 1(4): 303-315. PubMedThe neonatal Fc receptor (FcRn) is structurally similar to class I major histocompatibility molecules. FcRn transports maternal immunoglobulin G (IgG) from ingested milk into the blood. IgG is bound at the pH of milk (pH 6.0-6.5) in the gut and released at the pH of blood (pH 7.5). We find that alteration of a histidine pair within the alpha 3 domain of FcRn and of a nearby loop (the FcRn counterpart of the class I CD8-binding loop) affects the affinity for IgG. Inhibition studies suggest the involvement of the FcRn B2-microglobulin domain in IgG binding. Fragment B of protein A inhibits FcRn binding to IgG, localizing the binding site on Fc for FcRn to the CH2-CH3 domain interface. Three histidines present at the CH2-CH3 domain interface of Fc could be partially responsible for the pH-dependent interaction between FcRn and IgG.
