InVivoMAb anti-rat FcRn heavy chain heterodimers

Clone Catalog # Category
2G3 BE0144 InVivoMab Antibodies
$95 - $3250

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

Isotype

Mouse IgG1

Recommended Isotype Control(s) InVivoMAb mouse IgG1 isotype control, unknown specificity(BE0083)
Recommended InVivoPure Dilution Buffer InVivoPure pH 7.0 Dilution Buffer(IP0070)
Immunogen

Purified soluble FcRn

Reported Applications
  • ELISA
  • Flow cytometry
Endotoxin
  • <2EU/mg (<0.002EU/μg)
  • Determined by LAL gel clotting assay
Purity
  • >95%
  • Determined by SDS-PAGE
Formulation
  • PBS, pH 7.0
  • Contains no stabilizers or preservatives
Sterility

0.2 μM filtered

Production

Purified from tissue culture supernatant in an animal free facility

Purification

Protein G

Storage

The antibody solution should be stored at the stock concentration at 4°C. Do not freeze.

RRID

AB_10950633

Molecular Weight

150 kDa

Application References

InVivoMAb 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. PubMed

The 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.

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