GFP Antibody

Green Fluorescent Protein (GFP) is a protein that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range. Originally isolated from the jellyfish Aequorea victoria, GFP has become a crucial tool in molecular and cellular biology due to its unique properties .

GFP was first purified in the 1960s and 1970s by Osamu Shimomura, who studied its properties along with the luminescent protein aequorin . The gene encoding GFP was cloned in 1992 by Douglas Prasher, and Martin Chalfie’s lab successfully expressed the sequence in vivo . Roger Tsien’s lab later improved GFP, making it a widely used research tool . In recognition of their contributions, Shimomura, Chalfie, and Tsien were awarded the Nobel Prize in Chemistry in 2008 .

GFP has a major excitation peak at a wavelength of 395 nm and a minor one at 475 nm, with an emission peak at 509 nm . This makes it an excellent tool for various biological applications, including:

• Gene Expression Monitoring: GFP can be used as a reporter gene to monitor gene expression in living organisms .
• Protein Localization and Dynamics: GFP-tagged proteins can be visualized to study their localization and movement within cells .
• Biosensors: Modified forms of GFP have been used to create biosensors for detecting various cellular conditions .

Monoclonal antibodies against GFP, such as those produced in mice, are essential tools for detecting and studying GFP-tagged proteins. These antibodies are typically derived from hybridoma cells produced by fusing mouse myeloma cells with splenocytes from immunized mice . Mouse monoclonal antibodies against GFP are highly specific and can be used in various techniques, including Western blotting, immunoprecipitation, and ELISA .