Gaussia luciferase is a luminescent protein with quantum yields higher than the luciferases from
Renilla sp. and firefl y. The enzyme catalyzes the oxidation decarboxylation of coelenterazine to give light (λmax = 485nm) and coelenteramide. ATP is not needed for activity.
Gaussia luciferase is salt tolerant and retains its activity in the presence of non-ionic detergents, cholate, and deoxycholate. In addition, the enzyme is thermal tolerant and can retain activity at temperatures up to 60˚C.
The protein is also resistant to irreversible denaturation. Enzymatic activity can be recovered after treatment with 7M guanidine HCl or 8M urea in the presence of detergent.
PRODUCT PROPERTIES |
MW: | | ~25kDa (SDS-PAGE) |
Source: | | Produced in Gaussia. |
Short Term Storage: | | +4°C |
Long Term Storage: | | -80°C |
Background / Technical Information: | | For the Original Manufacturer's data sheet please click here. |
|
|
FIGURES
The diagram depicts the oxidation of coelenterazine by Gaussia luciferase to yield light. Coelenterazine-utilizing luciferases, such as Gaussia luciferase, do not require accessory high-energy molecules such as ATP for their signal. Gaussia luciferase is the brightest of all luciferase enzymes, which makes it superior to other luminescent proteins in assays requiring very low detection limits.
|