Human IgG protein (Fc) (31C-CH3022)
Purified Human IgG, Fc fragment
|Synonyms||Immunoglobulin G protein (Human) (Fc)|
SDS-PAGE analysis of Human IgG protein (Fc) (31C-CH3022)
Lane 1: Non-reduced Human IgG Fc Lane 2: Non-reduced Human IgG Whole Molecule Lane 3: Non-reduced Human IgG Fab Fragment Lane 4: Non-reduced Human IgG F(ab')2 Fragment. Middle Lane: 5uL MW Marker. Lane 5: Reduced Human IgG Fc Lane 6: Reduced Human IgG Whole Molecule Lane 7: Reduced Human IgG Fab Fragment Lane 8: Reduced Human IgG F(ab')2 Fragment. Load: 1ug per lane. Human IgG Whole Molecule, Human IgG Fab Fragment and Human IgG F(ab')2 Fragment ran as controls. Predicted/Observed size: Non-reduced at 50 kDa, reduced at 25 kDa/Non-reduced at 55-60 kDa, reduced at 30-33 kDa.
|Method of Purification||Human IgG protein (Fc) was purified by delipidation, salt fractionation and ion exchange chromatography followed by papain digestion and dialysis.|
|Form & Buffer||Liquid in 0.02M K3PO4, pH 7.2, with 0.15M NaCl, and 0.01% NaN3.|
Storage & Safety
|Storage||Store at 4 deg C. Dilute only prior to immediate use.|
|Biohazard Information||This product contains sodium azide as preservative. Although the amount of sodium azide is very small appropriate care must be taken when handling this product.|
|Biological Significance||Immunoglobulin G (IgG) are antibody molecules. Each IgG is composed of four peptide chains - two heavy chains and two light chains. Each IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. The Fc regions of IgGs bear a highly conserved N-glycosylation site. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and alpha-2,6-linked sialic acid residues.|
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