WGA HRP, also known as Wheat Germ Agglutinin Horseradish Peroxidase, is a type of conjugate made by linking the enzyme horseradish peroxidase (HRP) to the lectin wheat germ agglutinin (WGA).
WGA is a protein extracted from wheat germ that specifically binds to N-acetyl-D-glucosamine and sialic acid residues present on the surface of cells and glycoproteins. It is commonly used as a biological tool in various research applications, including cell labeling and visualization, cell sorting, and studying cell surface carbohydrates.
HRP, on the other hand, is an enzyme derived from horseradish that catalyzes the oxidation of a substrate in the presence of hydrogen peroxide, resulting in the generation of a detectable colorimetric or chemiluminescent signal. It is widely used in enzyme-linked immunosorbent assays (ELISAs), Western blotting, immunohistochemistry, and other immunological techniques for the detection and quantification of specific molecules.
By conjugating HRP with WGA, researchers can take advantage of both the lectin's ability to bind specifically to certain cell surface carbohydrates and the enzymatic activity of HRP. This conjugate is employed to detect the presence or localization of specific saccharide moieties on cells or glycoproteins, as well as to amplify the signal for enhanced detection sensitivity.
In summary, WGA HRP is a complex formed by linking wheat germ agglutinin lectin with the horseradish peroxidase enzyme. It is widely used in biological and immunological research for a variety of applications involving the detection and visualization of specific carbohydrates and glycoproteins.
