Fluorescent Proteins

Fluorescent proteins (FPs) are widely used as optical sensors. Photochromic FP Dronpa mutants can be used to control the photoactivity of proteins. By fusing the Dronpa domain into the two ends of the enzyme domain, a fluorescent light induced protein was created. In the dark, the Dronpa domain binds and traps proteins, but light induces Dronpa to dissociate and activate proteins. This method can optically control guanine nucleotide exchange factor and protease domain without extensive screening. In this way, the application range of FPS is extended from simple sensing function to optogenetic control.

PYP domain (photoactive yellow protein) is a p-coumaric acid binding protein domain. It is another kind of photogenetic switch belonging to fluorescent proteins. It exists in various bacterial proteins. It is a highly soluble globular protein with α/β Folding structure. It is a member of the PAS domain superfamily, which also contains many other types of photosensitive proteins.

Creative BioMart provides plenty of services and related solutions based on the Fluorescent Proteins switch systems.

Basic Parameters and Characteristics of Fluorescent Protein Switch

	Dronpa145K/N	Dronpa145N	PhoCl	PYP
Photoreceptor	Dronpa145K, Dronpa145N	Dronpa145N	PhoCl	PYP
Binding partner	/	/	/	/
Cofactor	None	None	None	P-coumaric acid
Source organism	Pectiniidae	Pectiniidae	Clavularia sp.	Halorhodospira halophila
Mode of action	Heterodimerization, dissociation	Heterodimerization, dissociation	Photocleavage	Intramolecular conformational change
Excitation wavelength	500 nm	500 nm	380 nm	450 nm
Reversion wavelength	400 nm	400 nm	irreversible switch	Dark
Excitation time	Seconds	Seconds	Minutes	Seconds
Reversion time	Seconds	Seconds		Seconds