抗体| Bio-Rad研究抗体

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Western blot detection of immunoprecipitated proteins is a commonly used technique to study protein-protein interactions and immunoprecipitation (IP) is often performed to enrich low abundant proteins in a sample to enable their detection.

In contrast to other sample types, the observed western blot background when detecting IP samples is often higher due to antibodies/IgGs being released from beads during the IP procedure.

These IgGs then become denatured during the IP sample preparation procedure and are detected by conventional heavy and light chain secondary antibodies used in western blotting experiments.

This binding results in two distinct bands that can be observed on the western blot; the IgG heavy chain at 50 kDa and the IgG light chain at 25 kDa. The IgG chains might mask the protein of interest and make detection difficult especially when the immunoprecipitated proteins have a molecular weight of ~50 kDa or 25 kDa.

TidyBlot Reagent prevents detection of endogenous immunoglobulins

The animation below outlines the different steps in an IP procedure using SureBeads Magnetic Beads and highlights how you can use TidyBlot to mitigate obstruction from IgG heavy and light chains. TidyBlot, in contrast to conventional secondary antibodies, only binds to the native antibody used during the western blotting procedure and therefore enables the western blot detection of IP samples without interference from IgG heavy and light chains.