Mouse IgG3-Fc Protein (Native)

Verwandte Bereiche:

Proteine:

Antikörper:

Immunoglobulin G3 (IgG3) is a member of many immunoglobulinG developed and secreted by effective B cells. IgG3 is an antibody moleculer induced by infection. Immunoglobulins are composed of four peptides chain-two heavy γ chains and two light chains. These two heavy chains are each linked and linked with one light chain through disulfide bonds. Thus the immunoglobulin forms a Y-like formation. There are two antigen binding sites at the top of Y-like fork's two arms. The disulfide bond site of both heavy chains is also pepsin site. In wake of cutting by pepsin, IgG is divided into two F(ab)s with one antigen binding site and a high conserved Fc segment. The Fc segment bears a highly conserved N-glycosylation site. The glycosylation of the circulating immunoglobulin-γ (IgG) antibody molecules changes in rheumatoid arthritis. The extent of the changes correlates with the disease severity and reverses in remission. It has been elucidated that the alteration in glycosylation associated with rheumatoid arthritis can create a new mode for the interaction of IgG with complement through binding to the collagenous lectin mannose-binding protein (MBP). Rheumatoid arthritis is associated with a marked increase in IgG glycoforms that lack galactose (referred to as G0 glycoforms) in the Fc region of the molecule and that terminate in N-acetyl glucosamine (GlcNAc). Fc receptor is a protein found on the surface of certain cells – including natural killer cells, macrophages, neutrophils, and mast cells - that contribute to the protective functions of the immune system.

1. Briles DE. et al., 1981, Nature. 294 (5836): 88-90.
2. Amoura Z. et al., 2000, Arthritis Rheum. 43 (1): 76-84.
3. Brière F. et al., 1994, J Exp Med. 179 (2): 757-62.