IgG3-Fc / IGHG3 Protein|IgG3-Fc / IGHG3蛋白质|现货|厂家价格

IgG3-Fc / IGHG3蛋白产品信息

别名: IGHG3
表达方式: 
 A DNA sequence encoding the human IgG3 Fc region (P01860) (Glu 99- Lys 377) was expressed and purified.
种属: Human
表达宿主: Human Cells

IgG3-Fc / IGHG3 Protein QC Testing

纯度: > 96 % as determined by SDS-PAGE SDS-PAGE
内**: < 1.0 EU per μg of the protein as determined by the LAL method
稳定性: Samples are stable for up to twelve months from date of receipt at -70℃
预测N端: Glu 99
分子量: 
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.
缓冲液: 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.

IgG3-Fc / IGHG3 Protein Usage Guide

储存方法: 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蛋白背景综述

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.

参考文献

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

规格:100ug

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