IgG4-Fc Protein (Native)

28.02.2012

Produkt-Information IgG4 Protein

Synonym :	IgG4
Protein Construction:	A DNA sequence encoding the human IgG4 Fc region (P01861) (Glu 99- Lys 327, 108Ser/Pro) was expressed and purified.
Source:	Human
Expression Host:	Human Cells

IgG4 Protein QC Testing

Purity:	> 95 % as determined by SDS-PAGE	SDS-PAGE: IgG4 protein
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 IgG4-Fc consists of 229 amino acids and has a predicted molecular mass of 25.5 kDa. As a result of glycosylation, the apparent molecular mass of IgG4-Fc is approximately 35 kDa in SDS-PAGE under reducing conditions.
Formulation:	Supplied as a 0.2μm filtered solution of PBS, pH7.4 Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

IgG4 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.

Verwandte Produkte & Themen von IgG4 Protein

Verwandte Bereiche:

Proteine:

Antikörper:

Beschreibung von IgG4 Protein

Immunoglobulin G4 (IgG4) is a member of many immunoglobulinG developed and secreted by effective B cells. IgG4 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). Experiment results suggest that Autoimmune pancreatitis (AIP) is not simply pancreatitis but that it is a pancreatic lesion involved in IgG4-related systemic disease with extensive organ involvement.

References

Kamisawa T. et al., 2003, J Gastroenterol. 38 (10): 982-4.
Hamano H. et al., 2001, N Engl J Med. 344 (10): 732-8.
Aalberse RC. et al., 1983, J Immunol. 130 (2): 722-6.

Sino Biological Inc. liefert IgG4-Fc Protein (Native) mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

Weitere Informationen über IgG4-Fc Protein (Native) lesen Sie bitte: http://www.sinobiological.com/goods.php?id=8327