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•Technical Note: Rapid Screening And Selection Of Optimal Antibody Capturing Agents Using The ProteOn XPR36 Protein Interaction Array System

By Bio-Rad Laboratories, Inc.

The production of antibodies for use as research tools or for diagnostic and therapeutic applications is a major focus for many life science researchers. Immunoglobulin (Ig) binding proteins of bacterial origin have long been used for purification of antibodies, and for the detection of those antibodies in immunological assays. Each of these Ig binding proteins has different antibody-binding properties in terms of the portion of the antibody that is recognized, as well as the species and class of antibodies it will bind. Proteins A, G, A/G, and L are native and recombinant proteins that bind almost exclusively with the IgG class of antibodies and are widely available commercially. Protein A is generally preferred for rabbit, pig, dog and cat IgG. Protein G has better binding capacity for a broader range of mouse and human IgG subclasses (IgG1, IgG2, etc.). Protein A/G is a recombinant fusion protein that includes the IgG-binding domains of both protein A and protein G and binds a very broad range of IgG subclasses from rabbit, mouse, human, and other mammalian samples. Protein L binds to certain immunoglobulin k light chains, which occur in all classes of Igs (i.e., IgG, IgM, IgA, IgE, and IgD). Only those antibodies within each class that possess the appropriate k light chains will bind. For any given antibody screening and/or purification, empirical testing is best used to determine which of these antibody-binding proteins is best suited to the application, and knowing the strength of binding of each of these proteins to the antibody(ies) of interest will aid in that determination.

Click Here To Download:
•Technical Note: Rapid Screening And Selection Of Optimal Antibody Capturing Agents Using The ProteOn XPR36 Protein Interaction Array System