Description

Using the biotin-streptavidin system, proteins can be biotinylated (i.e., labeled with biotin) to specifically bind with streptavidin. This enables applications such as antigen-antibody recognition, biomolecule capture, and protein interaction detection.

Biotinylation methods are generally divided into chemical biotinylation and Avitag-biotinylation.

Protein Biotinylation Methods:

1. Chemical Biotinylation: After purifying the recombinant protein, biotinylation is achieved using chemical methods. Biotin’s carboxyl group is chemically modified to create derivatives with various active groups, which then react with the recombinant protein. This method involves harsh reaction conditions, which can inactivate sensitive proteins. Additionally, since activated biotin does not specifically recognize particular proteins, chemical biotinylation is non-specific.

2. Avitag Biotinylation: The recombinant protein is expressed with an Avitag fusion, and biotin labeling is performed in vitro. This method provides specific site-directed modification with minimal impact on protein activity and results in highly specific products. However, this method requires fusion expression of the target protein with the biotin tag, followed by purification to obtain high-purity recombinant protein.

Product Content

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