8-Br-cAMP inhibits the transient expression of firefly luciferase
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چکیده
منابع مشابه
Transient transfection and expression of firefly luciferase in Giardia lamblia.
We have developed a gene transfer system for the protozoan parasite Giardia lamblia. This organism is responsible for many cases of diarrhea worldwide and is considered to be one of the most primitive eukaryotes. Expression of a heterologous gene was detected in this parasite after electroporation with appropriate DNA constructs. We constructed a series of transfection plasmids using flanking s...
متن کاملCloning of firefly luciferase cDNA and the expression of active luciferase in Escherichia coli.
A cDNA library was constructed from firefly (Photinus pyralis) lantern poly(A)+ RNA, using the Escherichia coli expression vector lambda gt11. The library was screened with anti-P. pyralis luciferase (Photinus luciferin:oxygen 4-oxidoreductase, EC 1.13.12.7) antibody, and several cDNA clones expressing luciferase antigens were isolated. One clone, lambda Luc1, contained 1.5 kilobase pairs of cD...
متن کاملDevelopment of a thermostable firefly luciferase
Firefly luciferase forms the basis of a wide range of analytical techniques. However, the enzyme is unstable and rapidly loses activity even at room temperature. This leads to losses in sensitivity and precision in analytical applications and also severely limits the fieldability of devices incorporating luciferase-based technologies. A number of point mutations have previously been identified ...
متن کاملThe nuclear factor κB inhibitor (E)-2-fluoro-4′-methoxystilbene inhibits firefly luciferase
Photinus pyralis (firefly) luciferase is widely used as a reporter system to monitor alterations in gene promoter and/or signalling pathway activities in vitro. The enzyme catalyses the formation of oxyluciferin from D-luciferin in an ATP-consuming reaction involving photon emission. The purpose of the present study was to characterize the luciferase-inhibiting potential of (E)-2-fluoro-4'-meth...
متن کاملSpyTag/SpyCatcher Cyclization Enhances the Thermostability of Firefly Luciferase
SpyTag can spontaneously form a covalent isopeptide bond with its protein partner SpyCatcher. Firefly luciferase from Photinus pyralis was cyclized in vivo by fusing SpyCatcher at the N terminus and SpyTag at the C terminus. Circular LUC was more thermostable and alkali-tolerant than the wild type, without compromising the specific activity. Structural analysis indicated that the cyclized LUC i...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1989
ISSN: 0014-5793
DOI: 10.1016/0014-5793(89)80620-9