La coelenteracina h es uno de los diversos análogos sintéticos de la coelenteracina que confieren diferentes afinidades de Ca2+ yMás información
Have Questions?
Número de catálogo
Cantidad
C6780
también denominado C-6780
250 μg
Número de catálogo C6780
también denominado C-6780
Precio (MXN)
-
Cantidad:
250 μg
La coelenteracina h es uno de los diversos análogos sintéticos de la coelenteracina que confieren diferentes afinidades de Ca2+ y propiedades espectrales en el complejo de ecuorina. Al igual que la coelenteracina nativa, estos cinco nuevos derivados se pueden utilizar para reconstituir el complejo de ecuorina tanto in vivo como in vitro.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Método de detecciónBioluminiscente
Tipo de coloranteBasado en proteínas
Cantidad250 μg
Condiciones de envíoTemperatura ambiente
Para utilizar con (equipo)Luminómetro (microplaca), Luminómetro (basado en tubos)
Tipo de productoCoelenteracina h
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Citations & References (26)
Citations & References
Abstract
Intracellular Ca2+ signals in Dictyostelium chemotaxis are mediated exclusively by Ca2+ influx.
Authors:Nebl T, Fisher PR
Journal:J Cell Sci
PubMed ID:9427292
'We measured folate- and cAMP-induced changes in cytoplasmic free calcium concentration ([Ca2+]i) using recombinant aequorin reconstituted in living Dictyostelium cells with coelenterazine-h. The resulting semi-synthetic protein displayed increased sensitivity to Ca2+ allowing accurate measurement of chemoattractant-induced transients at low resting levels. Both folate- and cAMP-induced Ca2+ responses were developmentally regulated, ... More
Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer.
Authors:Mercier JF, Salahpour A, Angers S, Breit A, Bouvier M
Journal:J Biol Chem
PubMed ID:12244098
'Quantitative bioluminescence resonance energy transfer (BRET) analysis was applied to the study of beta(1)- and beta(2)-adrenergic receptor homo- and heterodimerization. To assess the relative affinity between each of the protomers, BRET saturation experiments were carried out in HEK-293T cells. beta(1)- and beta(2)-adrenergic receptors were found to have similar propensity to ... More
The use of Renilla luciferase, Oplophorus luciferase, and apoaequorin as bioluminescent reporter protein in the presence of coelenterazine analogues as substrate.
Authors:Inouye S, Shimomura O
Journal:Biochem Biophys Res Commun
PubMed ID:9144537
'To investigate the use of various luciferases as reporter protein, the substrate specificity of recombinant Renilla luciferase, Oplophorus luciferase and recombinant apoaequorin was examined using 23 kinds of coelenterazine analogues as the substrate. The intensity of luminescence was generally highest with Oplophorus luciferase and lowest with apoaequorin, but varied widely ... More
Characterization of coelenterazine analogs for measurements of Renilla luciferase activity in live cells and living animals.
Authors:Zhao H, Doyle TC, Wong RJ, Cao Y, Stevenson DK, Piwnica-Worms D, Contag CH
Journal:Mol Imaging
PubMed ID:15142411
'In vivo imaging of bioluminescent reporters relies on expression of light-emitting enzymes, luciferases, and delivery of chemical substrates to expressing cells. Coelenterazine (CLZN) is the substrate for a group of bioluminescent enzymes obtained from marine organisms. At present, there are more than 10 commercially available CLZN analogs. To determine which ... More
Imaging [Ca2+]i with aequorin using a photon imaging detector.