aequorin การใช้

• Both aequorin and GFP are important tools used in biological research.
• Work on aequorin began with E . Newton Harvey in 1921.
• Step4 : Ca2 + channel is opened and aequorin emits photons.
• When coelenterazine is bound, it is called aequorin.
• Chemical characterization of aequorin indicates the protein is somewhat resilient to harsh treatments.
• Aequorin is presumably encoded in the genome of Aequorea.
• The B cells are genetically engineered to produce aequorin.
• Aequorin is a calcium binding protein ( CaBP ) isolated from the coelenterate Aequorea victoria.
• Aequorin is a photoprotein isolated from the bioluminescent jellyfish " Aequorea victoria ".
• It is based on yeast cells expressing aequorin protein sensitive to change in intracellular calcium.
• Aequorin is a photoprotein that can be extracted from marine organisms such as luminescent fish.
• Calcium concentration microdomains can be visualised with fluorescence microscopy by using aequorin as a reporter protein.
• GFP is co-expressed with aequorin in small granules around the rim of the jellyfish bell.
• "' Aequorin "'is a resonant energy transfer, while aequorin by itself generates blue light.
• "' Aequorin "'is a resonant energy transfer, while aequorin by itself generates blue light.
• GFP, like aequorin, produces a blue fluorescent signal, but without the required addition of an exogenous substrate.
• Aequorin is a holoprotein composed of two distinct units, the kDa, and the prosthetic group coelenterazine, the luciferin.
• Aequorin is made up of two components  the calcium binding component apoaequorin ( AQ ) and the chemiluminescent molecule coelenterazine.
• Osamu Shimomura isolated the photoprotein aequorin and its cofactor coelenterazine from the crystal jelly " Aequorea victoria " in 1961.
• The crystal structure revealed that aequorin binds coelenterazine and oxygen in the form of a peroxide, coelenterazine-2-hydroperoxide.