2011-2012 Catalogue - PeproTech, Inc.

PEPROTECH ®www.peprotech.compurification protocols which exploit the binding affinity contains less than 0.2% of the desired antibody. The largeof antibodies to certain bio-molecules have yielded much quantity of unrelated IgGs found in these preparationsbetter results. For example, Protein A and Protein G are not only interferes with quantification of the relativebacterial (Staphylococcus)-derived proteins that possess amount of the cytokine-specific antibody, but also conhighbinding affinity toward the F c (Fragment crystallizable)region of immunoglobulins (IgGs), and when atbodyis used in analytical procedures such as ELISA,siderably increases the background noise when the antitachedto a solid-support matrix, enable efficient separationof IgGs from other serum constituents. Protein A/G ting. A superior method for isolating specific polyclonalneutralization, immunohistochemistry, and Western blot-affinity purification of serum-IgGs typically enriches the antibodies from antiserum is by affinity chromatography,which exploits the specificity of antibody-antigendesired antibody by more than 100-fold. Yet, in the caseof anti-cytokine antibodies, the total IgG fraction often interactions (Figure I-1). Here, the separation mediumFigure I-2Schematic illustration of column chromatography setup for antigen-affinity purification of antibodies.PB{ }INFORMATION & TECHNICAL SUPPORTNOTE: Elution is titrated with1M NaOH to pH 7.2.Bestellungen: Deutschland: Tel: 0800 436 99 10 • email: info@peprotech.dePour commander: France: Tel: +33 (0)1 46 24 58 20 • email: info@peprotechfr.comTo Order: NORDIC: Tel: +46 (0)8 640 41 07 • email: info@peprotech.se155