CPM (7-dietilamino-3-(4'-maleimididenil)-4-metilocumarina)
CPM (7-dietilamino-3-(4'-maleimididenil)-4-metilocumarina)
Invitrogen™

CPM (7-dietilamino-3-(4'-maleimididenil)-4-metilocumarina)

La cumarina tiol reactiva CPM muestra una fluorescencia muy débil hasta que ha reaccionado con tioles produciendo un conjugado conMás información
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Número de catálogoCantidad
D34625 mg
Número de catálogo D346
Precio (MXN)
-
Cantidad:
25 mg
La cumarina tiol reactiva CPM muestra una fluorescencia muy débil hasta que ha reaccionado con tioles produciendo un conjugado con excitación/emisión máxima de ∼384/470 nm.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaTiol
Emisión470 nm
Excitación384 nm
Etiqueta o tinteMetilocumarina
Tipo de productoCPM
Cantidad25 mg
Fracción reactivaMaleimida
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador (de -5 °C a -30 °C) y proteger de la luz.

Citations & References (151)

Citations & References
Abstract
Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1.
Authors:Shapiro AB, Gibson KD, Scheraga HA, McCarty RE
Journal:J Biol Chem
PubMed ID:1832671
Equilibrium dialysis measurements of adenine nucleotide binding to chloroplast coupling factor 1 suggest that the enzyme has six binding sites for ADP, adenylyl-beta,gamma-imidodiphosphate (AMP-PNP), and 2'(3')-O-2,4,6-trinitrophenyl-ATP (TNP-ATP). High affinity binding at all six sites requires the divalent cation, Mg2+. Three of the nucleotide-binding sites, sites 1, 2, and 3, have ... More
Arrangement of the COOH-terminal and NH2-terminal domains of caldesmon bound to actin.
Authors:Graceffa P
Journal:Biochemistry
PubMed ID:9092808
'Smooth muscle caldesmon is a single polypeptide chain with its NH2- and COOH-terminal domains separated by a long alpha-helix. Caldesmon was labeled at either Cys-153 in the NH2 domain or Cys-580 in the COOH domain with a variety of fluorescence probes. Fluorescence intensity, peak position, and polarization of probes on ... More
The pleckstrin homology domain of phospholipase Cbeta transmits enzymatic activation through modulation of the membrane-domain orientation.
Authors:Drin G, Douguet D, Scarlata S
Journal:Biochemistry
PubMed ID:16669615
'Phospholipase Cbeta (PLCbeta) enzymes are activated by Galpha q and Gbetagamma subunits and catalyze the hydrolysis of the minor membrane lipid phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2]. Activation of PLCbeta2 by Gbetagamma subunits has been shown to be conferred through its N-terminal pleckstrin homology (PH) domain, although the underlying mechanism is unclear. Also ... More
Structural organization of chloroplast coupling factor.
Authors:Snyder B, Hammes GG
Journal:Biochemistry
PubMed ID:2859887
'Fluorescence resonance energy transfer measurements have been used to construct spatial maps for the accessible sulfhydryl of the gamma subunit (dark site) and the essential tyrosine residue of the beta subunits relative to previously mapped sites on the H+-ATPase from chloroplasts. The extent of energy transfer was measured between a ... More
Signaling through a G Protein-coupled receptor and its corresponding G protein follows a stoichiometrically limited model.
Authors:Philip F, Sengupta P, Scarlata S
Journal:J Biol Chem
PubMed ID:17420253
'The bradykinin receptor is a G protein-coupled receptor (GPCR) that is coupled to the Galpha(q) family of heterotrimeric G proteins. In general, a GPCR can exert intracellular signals either by transiently associating with multiple diffusing G protein subunits or by activating a G protein that is stably bound to the ... More