What is biotin labeling?

Biotinylation, also known as biotin labeling, is the process of covalently attaching biotin(s) to biomolecules: such as proteins, antibodies, peptide, oligonucleotide, and other macromolecules.

What protein binds with biotin?

Avidin, Streptavidin or NeutrAvidin Protein can bind up to four biotin molecules, which are normally conjugated to an enzyme, antibody or target protein to form an Avidin-biotin complex.

What is streptavidin biotin assay system?

The streptavidin-biotin system is a protein-ligand interaction present in nature that has been successfully used in a number of applications including detection of proteins, nucleic acids, and lipids as well as protein purification.

What is the importance of biotin in labeling?

Biotin tagging or labeling is extremely useful in protein research and can be used in a number of applications, including enzyme-linked immunosorbent assay (ELISA) and Western blot analysis. It can also be used for immunohistochemistry, immunoprecipitation, cell surface labeling, and flow cytometry.

What is AviTag?

The AviTag™ is a popular fusion tag due to its powerful and versatile properties. Fused to your protein, the AviTag™ provides a multi-functional system useful for many applications including: Expression. Imaging. Detection.

Where does biotin bind to the antibody?

Biotinylation of antibody is a straightforward procedure that can be achieved by using a succinimidyl ester of biotin. This water-soluble reagent reacts with primary amines of the lysine residues or the amino terminus of the antibody to form amide bond.

How does biotin streptavidin work?

The strong streptavidin-biotin interaction can be used to attach various biomolecules to one another or onto a solid support. Harsh conditions are needed to break the streptavidin-biotin interaction, which often denatures the protein of interest being purified.