Mouse IgG (Fab'2) (31C-CH1019)
Purified Mouse IgG (Fab'2)
|Synonyms||Mouse Immunoglobulin G (Fab'2)|
SDS-PAGE analysis of Mouse IgG (Fab'2) (31C-CH1019)
Lane 1: 5 uL MW Marker. Lane 2: Reduced Mouse IgG Whole Molecule. Lane 3: Reduced Mouse F(c) Fragment. Lane 4: Reduced Mouse F(ab')2 Fragment. Lane 5: Mouse IgM Kappa Myeloma Protein. Load: 1 ug per lane. Predicted/Observed size: IgG at 50 and 25 kDa; F(c) at 25 kDa; F(ab')2 at 25 kDa; IgM K at 70 and 23 kDa. Observed F(c) Fragment migrates slightly higher.
|Method of Purification||Mouse IgG (Fab'2) was purified by delipidation, salt fractionation and ion exchange chromatography followed by dialysis.|
|Form & Buffer||Lyophilized from 0.02M K3PO4, pH 7.2, with 0.15M NaCl, and 0.01% NaN3.|
Storage & Safety
|Storage||Store at 4 deg C until reconstitution. Following reconstitution aliquot and freeze at -20 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|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 fragment antigen-binding (Fab fragment) is a region on an antibody that binds to antigens. It is composed of one constant and one variable domain of each of the heavy and the light chain. These domains shape the paratope — the antigen-binding site — at the amino terminal end of the monomer. The two variable domains bind the epitope on their specific antigens. Treatment with pepsin produces an F(ab)'2 fragment.|
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