Saltar al contenido
Merck
Todas las fotos(3)

Key Documents

View All Documentation

SRE0045

Sigma-Aldrich

Luciferase from Photinus pyralis (firefly)

recombinant, expressed in E. coli, lyophilized powder, ≥10×1010 units/mg protein

Sinónimos:

Luciferase firefly

Iniciar sesiónpara Ver la Fijación de precios por contrato y de la organización
Todas las fotos(3)

About This Item

Número de CAS:
61970-00-1
Comisión internacional de enzimas:
1.13.12.7 (BRENDA, IUBMB)
MDL number:
MFCD00131546
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

Quality Level

200

form

lyophilized powder

specific activity

≥10×1010 units/mg protein

mol wt

62 kDa

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

¿Está buscando productos similares? Visita Guía de comparación de productos

Application

Firefly luciferase is used extensively in molecular and cell biology, in particular for the efficient detection and quantitation of ATP and as a reporter for genetic function.

Biochem/physiol Actions

Firefly luciferase is a 62 kDa protein that catalyzes the production of light. The enzyme requires ATP, molecular oxygen, and the heterocyclic compound, firefly luciferin, to generate light in a two-step process. The light producing reaction is initiated by luciferin activation (adenylation of its carboxylate group) and proceeds in the presence of molecular oxygen to yield a photon of yellow-green light.

Unit Definition

One luciferase enzyme unit will produce one Relative Light Unit (RLU) at 20-25 °C over a 10 second period, measured in 100 μl assay mixture containing 40 pmol ATP and 15 nmol luciferin in Tris-glycine buffer, pH 7.6, using a GloMax 20/20 Luminometer.

Unit Definition Conversion Factor: There are approximately 9000 Relative Light Units (RLU) per one traditional Light Unit that uses a peak height equivalent to 0.02 μCi of 14C in a PPO/POPOP cocktail.

Physical form

Supplied as a lyophilized powder containing HEPES, pH 7.5, NaCl, MgCl2, EDTA, DTT and a carbohydrate stabilizer.
This product is a recombinant luciferase (62 kDa) from Photinus pyralis (American firefly) produced from the luc gene expressed in E. coli.

Preparation Note

To obtain maximal solubility it is important to reconstitute the enzyme at a high salt concentration, such as 1 M Tris buffer with any counter ion at pH 7-8. The enzyme can be prepared at a concentration of up to 5 mg protein/ml. Do not vortex and avoid agitation.
After reconstitution, the enzyme solutions can kept at 4-8 °C for up to 2 days or frozen in working aliquots at -20°C for at least one month. Repeated freezing and thawing is not recommended.

substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazardCorrosion
GHS08,GHS05

signalword

Danger

hcodes

H318,H334

Hazard Classifications

Eye Dam. 1 - Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

¿Ya tiene este producto?

Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

Los clientes también vieron

Slide 1 of 1

1 of 1

Firefly Lantern Extract pkg of 100 mg

Sigma-Aldrich

F6303

Firefly Lantern Extract

S R Ford et al.
Journal of bioluminescence and chemiluminescence, 7(3), 185-193 (1992-07-01)
Commercially available crystalline native and recombinant firefly luciferases were compared. The two types of luciferase had indistinguishable responses to variation in ATP and luciferin concentrations and to omission of reaction components. The time courses of light production, the responses to
Kanika Narula et al.
The Plant journal : for cell and molecular biology, 103(2), 561-583 (2020-03-15)
Pathogen-/microbe-associated molecular patterns (PAMPs/MAMPs) initiate complex defense responses by reorganizing the biomolecular dynamics of the host cellular machinery. The extracellular matrix (ECM) acts as a physical scaffold that prevents recognition and entry of phytopathogens, while guard cells perceive and integrate
Pratik Vyas et al.
Journal of the American Chemical Society, 145(15), 8344-8354 (2023-03-24)
Reactions involving the transfer of a phosphoryl (-PO32-) group are fundamental to cellular metabolism. These reactions are catalyzed by enzymes, often large and complex, belonging to the phosphate-binding loop (P-loop) nucleoside triphosphatase (NTPase) superfamily. Due to their critical importance in
Julia Adelöf et al.
Aging cell, 20(4), e13336-e13336 (2021-03-16)
With age, protein damage accumulates and increases the risk of age-related diseases. The proteasome activator PA28αβ is involved in protein damage clearance during early embryogenesis and has demonstrated protective effects against proteinopathy. We have recently discovered that adult female mice
Maura Greiser et al.
eLife, 12 (2023-06-05)
Mitochondrial ATP production in ventricular cardiomyocytes must be continually adjusted to rapidly replenish the ATP consumed by the working heart. Two systems are known to be critical in this regulation: mitochondrial matrix Ca2+ ([Ca2+]m) and blood flow that is tuned
Ver todos los artículos relacionados

Artículos

Bioluminescent Firefly Luciferase Assays

Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.

Bioluminescent Firefly Luciferase Assays

Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.

Bioluminescent Firefly Luciferase Assays

Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.

Bioluminescent Firefly Luciferase Assays

Firefly luciferase is a sensitive reporter for gene studies due to its absence in mammalian cells or tissues.

Nuestro equipo de científicos tiene experiencia en todas las áreas de investigación: Ciencias de la vida, Ciencia de los materiales, Síntesis química, Cromatografía, Analítica y muchas otras.

Póngase en contacto con el Servicio técnico