IgG2 Protein Price Inquiry ( Available Sizes )
IgG2 Protein Product Information
||A DNA sequence encoding the human IgG2 Fc region (P01859) (Glu 99- Lys 327, 257Ser/Ala) was expressed and purified.
IgG2 Protein QC Testing
||> 90 % as determined by SDS-PAGE
|Measured by its ability to bind human CD32a-His (Cat:10374-H08H1) in a functional ELISA.
||< 1.0 EU per μg of the protein as determined by the LAL method
||Samples are stable for up to twelve months from date of receipt at -70℃
|Predicted N terminal:
||The recombinant human IgG2-Fc consists of 228 amino acids and has a predicted molecular mass of 25 kDa. As a result of glycosylation, the apparent molecular mass of IgG2-Fc is approximately 34 kDa in SDS-PAGE under reducing conditions.
||Lyophilized from sterile PBS, pH7.4
- Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
- Please contact us for any concerns or special requirements.
IgG2 Protein Usage Guide
||Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
||A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
IgG2 Protein Related Products & Topics
IgG2 Protein Description
Immunoglobulin G2 (IgG2) is a member of many immunoglobulin G developed and secreted by effective B cells. IgG2 is an antibody moleculer induced by infection. Immunoglobulins are composed of four peptides chain-two heavy gamma 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. There are two members of IgG2: IgG2a and IgG2b. It was found that IgG2a was superior to IgG1 in activating complement. 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).
- Warmerdam PA. et al., 1991, J Immunol. 147 (4): 1338-43.
- Oxelius VA. et al., 1982, N Engl J Med. 306 (9): 515-7.
- Oxelius VA. 1974, Clin Exp Immunol. 17 (1): 19-27.