10411523001
Roche
Luciferase
from Photinus pyralis (American firefly)
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About This Item
form
lyophilized (recrystallized twice)
specific activity
~8 units/g protein (At 25 °C with 0.1 mM luciferin and 0.7 mM ATP as the substrates (0.1 M Tris-acetate, pH 7.75).)
packaging
pkg of 1 mg
manufacturer/tradename
Roche
optimum pH
7.5
shipped in
wet ice
General description
Luciferase is a class of enzymes naturally found in organisms like protists, fungi, insects, bacteria which belong to phylogenic kingdom. It is used as a molecular marker for biological imaging as it specifically cleaves luciferin substrate which results in emitting light.
Luciferase is an enzyme, that produces light. It is present in insect fireflies and in luminous marine and terrestrial microorganisms. Luciferase proteins are available in two forms, such as firefly (Photinus pyralis) and bacterial.
Application
Luciferase has been used as a component in Mix B respiration medium for the determination of the ATP synthetic activity of the H+-ATP synthase. It has also been used in thermal aggregation to assay CnoX (YbbN) activity.
Biochem/physiol Actions
Firefly luciferase oxidizes luciferin to oxyluciferin using molecular oxygen and ATP in the reaction and liberates light at 560 nm.
Quality
Contaminants: <1 mU ATPase/mg lyophilizate, and <10 mU nucleoside diphosphatase kinase/mg lyophilizate. The lyophilizate contains neither luciferin nor arsenate.
Sequence
Enzyme consists of two subunits, one of them is active.
Preparation Note
Storage conditions (working solution): -15 to -25 °C
Store the reconstituted solution in aliquots at -15 to -25 °C.
Avoid repeated freezing and thawing.
Information Note: Do not store in plastic vessels.
Store the reconstituted solution in aliquots at -15 to -25 °C.
Avoid repeated freezing and thawing.
Information Note: Do not store in plastic vessels.
Reconstitution
Cool the original glass vial (1 mg or 5 mg protein, respectively) to 0 °C in an ice-bath and dissolve the containing luciferase by adding 1 ml or 5 ml, respectively, 0.5 M ice-cold Tris-acetate buffer, pH 7.5, and let it stand for 10 minutes. (The dissolved enzyme is sensitive to shaking and to storage in plastic vessels). This concentrated solution is stable for several
months when stored frozen in portions of approximately 50 μl. Diluted solutions are unstable and should be prepared directly before use and should be kept in an ice-bath.
One microgram luciferase corresponds to approximately 107 arbitrary luciferase units.
months when stored frozen in portions of approximately 50 μl. Diluted solutions are unstable and should be prepared directly before use and should be kept in an ice-bath.
One microgram luciferase corresponds to approximately 107 arbitrary luciferase units.
Storage and Stability
Store at 2 to 8 °C. (A decrease in activity of approximately 20% may occur within 12 months.)
Other Notes
For life science research only. Not for use in diagnostic procedures.
WGK
WGK 1
Flash Point(F)
does not flash
Flash Point(C)
does not flash
Regulatory Information
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Certificates of Analysis (COA)
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Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation
Molecular Cell, 70(4) (2018)
Marker/Reporter Enzymes
Enzymology Primer for Recombinant DNA Technology, 567-645 (1996)
High-resolution temporal analysis of global promoter activity in Bacillus subtilis
Methods in Microbiology, 39, 1-26 (2012)
Determination of the H+-ATP synthase and hydrolytic activities.
Garcia-Bermudez, et al.
Bio-protocol, 6(16), e1905-e1905 (2016)
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