IgG3-Fc / IGHG3 Protein (Native)

Immunoglobulin heavy constant gamma 3 (G3m marker) Protein Datasheet

IgG3-Fc / IGHG3 Protein Product Information

• Synonym: IGHG3
• Protein Construction: A DNA sequence encoding the human IgG3 Fc region (P01860) (Glu 99- Lys 377) was expressed and purified.
• Source: Human
• Expression Host: Human Cells

IgG3-Fc / IGHG3 Protein QC Testing

• Purity: > 96 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Glu 99
• Molecular Mass: The recombinant human IgG3-Fc consists of 279 amino acids and has a predicted molecular mass of 31.2 kDa. As a result of glycosylation, the apparent molecular mass of IgG3-Fc is approximately 38 kDa in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile PBS,pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: IgG3-Fc / IGHG3 protein

IgG3-Fc / IGHG3 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

IgG3-Fc / IGHG3 Protein Description

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.

References

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.