Immunoglobulin G (IgG) is sub-divided into IgG1, IgG2, IgG3, and IgG4 with different heavy chains, named γ1, γ2, γ3, and γ4, respectively. It is expressed in the serum and possesses two heavy chains and two light chains. Limited digestion using papain cleaves the antibody into three fragments, two of which are identical and contain the antigen-binding activity. They are known as Fragment antigen binding (Fab) fragments. These fragments contain the light chains paired with the VH and CH1 domains of the heavy chains. Maternal IgG is the only antibody transported across the placenta to the fetus. It passively immunizes the infants.
Specificity
This product was prepared from monospecific antiserum by immunoaffinity chromatography using Sheep IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities, papain digestion and chromatographic separation. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Fluorescein and Anti-Donkey Serum. No reaction was observed against Anti-Papain or Anti-Donkey IgG F(c).
Immunogen
Sheep IgG whole molecule
Physical properties
Antibody format: IgG Fab
Physical form
Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 with 10 mg/mL Bovine Serum Albumin (BSA) - Immunoglobulin and Protease free
Reconstitution
Reconstitute with 1.0 mL deionized water (or equivalent).
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Human placental Fc receptors and the transmission of antibodies from mother to fetus.
Simister NE and Story CM
Journal of Reproductive Immunology, 37(1), 1-23 (1997)
Antibody structure, instability, and formulation.
Wang W
Journal of Pharmaceutical Sciences, 96(1), 1-26 (2007)
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