InVivoMAb anti-rat FcRn heavy chain heterodimers

Catalog #BE0144
Clone:
2G3
Reactivities:
Rat

$164.00 - $4,280.00

$164.00 - $4,280.00

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  • 100 mg - $4,280.00
  • 50 mg - $3,024.00
  • 25 mg - $2,009.00
  • 5 mg - $600.00
  • 1 mg - $164.00
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Product Details

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 Ī²2-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.

Specifications

Isotype Mouse IgG1
Recommended Isotype Control(s) InVivoMAb mouse IgG1 isotype control, unknown specificity
Recommended Dilution Buffer InVivoPure pH 7.0 Dilution Buffer
Conjugation This product is unconjugated. Conjugation is available via our Antibody Conjugation Services.
Immunogen Purified soluble FcRn
Reported Applications ELISA
Flow cytometry
Formulation PBS, pH 7.0
Contains no stabilizers or preservatives
Endotoxin <2EU/mg (<0.002EU/Ī¼g)
Determined by LAL gel clotting assay
Purity >95%
Determined by SDS-PAGE
Sterility 0.2 Āµm filtration
Production Purified from cell culture supernatant in an animal-free facility
Purification Protein G
RRID AB_10950633
Molecular Weight 150 kDa
Storage The antibody solution should be stored at the stock concentration at 4Ā°C. Do not freeze.
ELISA
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.