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Green Fluorescent Protein （GFP） is a bioluminescent polypeptide consisting of 238 residues, originally isolated from the jellyfish Aequorea victoria. GFP converts the blue chemiluminescent light of aequorin into green fluorescent light, with an excitation peak at 395 nm and a minor peak at 475 nm, and an emission peak at 508 nm. The protein's structure includes a β-barrel with an α-helix running through its center, containing the fluorophore responsible for its fluorescence. GFP has become a crucial tool in research for monitoring gene expression, cellular localization, protein mobility, and interactions between various proteins. Mutant forms of GFP have been engineered to improve its photostability and to produce different colors, expanding its utility in various biological systems.