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Citas y referencias (156)
Invitrogen™
Coelenterazine
La coelenteracina y los análogos sintéticos de la coelenteracina son útiles para reconstituir la ecuorina en células que se hanMás información
| Número de catálogo | Cantidad |
|---|---|
| C2944 | 250 μg |
Número de catálogo C2944
Precio (CLP)
410.892
Each
Cantidad:
250 μg
Precio (CLP)
410.892
Each
La coelenteracina y los análogos sintéticos de la coelenteracina son útiles para reconstituir la ecuorina en células que se han transfectado con el ADNc de la apoecuorina.
Obtenga más información sobre los indicadores de iones, incluidos los indicadores de calcio, potasio, pH y potencial de membrana ›
Obtenga más información sobre los indicadores de iones, incluidos los indicadores de calcio, potasio, pH y potencial de membrana ›
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
Tipo de productoCoelenteracina
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Citations & References (156)
Citations & References
Abstract
Monitoring dynamic changes in free Ca2+ concentration in the endoplasmic reticulum of intact cells.
Journal:EMBO J
PubMed ID:8521803
'Direct monitoring of the free Ca2+ concentration in the lumen of the endoplasmic reticulum (ER) is an important but still unsolved experimental problem. We have shown that a Ca(2+)-sensitive photoprotein, aequorin, can be addressed to defined subcellular compartments by adding the appropriate targeting sequences. By engineering a new aequorin chimera
Differential gel electrophoresis and transgenic mitochondrial calcium reporters demonstrate spatiotemporal filtering in calcium control of mitochondria.
Journal:J Biol Chem
PubMed ID:16670086
'Mitochondria must adjust both their intracellular location and their metabolism in order to balance their output to the needs of the cell. Here we show by the proteomic technique of time series difference gel electrophoresis that a major result of neuroendocrine stimulation of the Drosophila renal tubule is an extensive
Crystal structure of a Ca2+-discharged photoprotein: implications for mechanisms of the calcium trigger and bioluminescence.
Journal:J Biol Chem
PubMed ID:15155735
'Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for
Cotranslational formation of active photoprotein obelin in a cell-free translation system: direct ultrahigh sensitive measure of the translation course.
Journal:Anal Biochem
PubMed ID:10036164
'Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in
Measurement of changes in sarcoplasmic reticulum [Ca2+] in rat tail artery with targeted apoaequorin delivered by an adenoviral vector.
Journal:Cell Calcium
PubMed ID:9056079
'The physiologic relevance of Ca2+ release from the sarcoplasmic reticulum in arterial smooth muscle contraction is controversial. Therefore, we sought to measure changes in sarcoplasmic reticulum free [Ca2+] (i.e. [Ca2+]sr) in the intact rat tail artery. We exploited a novel technique to measure [Ca2+]sr with genetically targeted apoaequorin acting as