Goat IgG Fraction to á-Galactosidase, 1mL

The total protein is measured by using the Biuret procedure, with bovine albumin as a standard. Antibody titer is standardized by equivalence-point precipitation. The IgG fraction is tested for purity at 20 mg/mL using immunoelectrophoresis; No trace of albumin is detected. The antibody is produced by hyperimmunizing goats with the enzyme β-galactosidase from Escherichia coli. The IgG fraction is prepared by delipidation, ammonium sulfate fractionation, and anion exchange chromatography, and is further purified by solid-phase absorption to remove antibodies to non-β-galactosidase E. coli proteins. The product is dialyzed into 0.02M sodium phosphate, 0.14M sodium chloride, pH 7.3, adjusted to standard titer, filtered through a 0.22 μm filter, and vialed. No preservative is added. β galactosidase is coded by a gene (lac z) in the lac operon of Escherichia coli. It is a metalloenzyme that splits lactose into glucose and galactose. It hydrolyzes terminal, non-reducing β-D-galactose residues in β-D-galactosides. Activation by cations seems to be substrate dependent. K+, Na+, NH4+, Rb+, Cs+ and Mn2+ all activate enzyme activity based upon the substrate used. Goat IgG fraction to β-Galactosidase is used in enzyme Immunoassays, fluorescein Immunoassays, blots, cell or tissue immunostaining. Gives sharp precipitation lines in IEP and ID techniques. Suitable for conjugation with enzymes, radiolabels, fluorochromes, or other markers; suitable for attachment to solid supports for use as an immunoadsorbant. It is specially prepared for the detection and purification of recombinant proteins. Product is goat IgG fraction to β-galactosidase (no cross to E. coli) and buffer salts.