IgG contributes to 10−20% of plasma protein and is regarded as one of the most predominant serum protein. It consists of four subclasses: IgG1, IgG2, IgG3 and IgG4. The IgG structure possesses four polypeptide chains containing two identical γ heavy (H) chains and two identical κ or λ light (L) chains of 50kDa and 25kDa respectively. Papain and pepsin digestion yields two main fragments of the antibody: Fab (antigen binding fragment) and Fc (fragment crystallization tail).
Specificity
This product was prepared from monospecific antiserum by immunoaffinity chromatography using Rat IgG coupled to agarose beads followed by solid phase adsorption(s) to remove any unwanted reactivities. Assay by immunoelectrophoresis resulted in a single precipitin arc against Anti-Rabbit Serum, Rat IgG, Rat IgG F(c) and Rat Serum. No reaction was observed against Rat IgG F(ab′)2.
Immunogen
Rat IgG F(c) fragment
Biochem/physiol Actions
IgG (immunoglobulin G) antibody provides protection against bacterial, fungal and viral infections. Maternal IgG is transferred to fetus through the placenta that is vital for the immune defense of the neonate against infections. The Fc (fragment crystallization tail) region of the antibody is implicated in complement activation in which it elicits an immune response by binding to the Fc receptor on macrophages.
Physical properties
Antibody format: IgG
Physical form
Supplied in 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
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.
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Structure and function of immunoglobulins.
Schroeder Jr H W and Cavacini L
The Journal of Allergy and Clinical Immunology, 125(2), S41-S52 (2010)
Of the five immunoglobulin isotypes, immunoglobulin G (IgG) is most abundant in human serum. The four subclasses, IgG1, IgG2, IgG3, and IgG4, which are highly conserved, differ in their constant region, particularly in their hinges and upper CH2 domains. These
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