6-FAM (6-Carboxyfluorescein), single isomer
6-FAM (6-Carboxyfluorescein), single isomer
Invitrogen™

6-FAM (6-Carboxyfluorescein), single isomer

El isómero único, 6-FAM, contiene un ácido carboxílico que puede usarse para reaccionar con aminas primarias mediante la activación carbodiimidaMás información
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Número de catálogoCantidad
C1360100 mg
Número de catálogo C1360
Precio (MXN)
-
Cantidad:
100 mg
El isómero único, 6-FAM, contiene un ácido carboxílico que puede usarse para reaccionar con aminas primarias mediante la activación carbodiimida del ácido carboxílico. La fluoresceína es el reactivo de derivatización fluorescente más común para el etiquetado de biomoléculas. Además de su absorción relativamente alta, excelente rendimiento cuántico de fluorescencia y buena solubilidad en agua, la fluoresceína tiene un máximo de excitación que se ajusta estrechamente a la línea espectral de 488 nm del láser de iones de argón.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaAmina
Excitación488
Etiqueta o tinteFITC (fluoresceína)
Tipo de producto6-FAM
Cantidad100 mg
Fracción reactivaÁcido carboxílico
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Unit SizeEach
Contenido y almacenamiento
Almacenar a temperatura ambiente y proteger de la luz.

Citations & References (382)

Citations & References
Abstract
Membrane vesicles containing the Sendai virus binding glycoprotein, but not the viral fusion protein, fuse with phosphatidylserine liposomes at low pH.
Authors:Chejanovsky N, Zakai N, Amselem S, Barenholz Y, Loyter A
Journal:Biochemistry
PubMed ID:3021204
Membrane vesicles containing the Sendai virus hemagglutinin/neuraminidase (HN) glycoprotein were able to induce carboxyfluorescein (CF) release from loaded phosphatidylserine (PS) but not loaded phosphatidylcholine (PC) liposomes. Similarly, fluorescence dequenching was observed only when HN vesicles, bearing self-quenched N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylethanolamine (N-NBD-PE), were incubated with PS but not PC liposomes. Thus, fusion between ... More
Receptor-mediated endocytosis of antibody-opsonized liposomes by tumor cells.
Authors:Leserman LD, Weinstein JN, Blumenthal R, Terry WD
Journal:Proc Natl Acad Sci U S A
PubMed ID:7001454
'Specific receptor-mediated delivery of the contents of small, sonicated liposomes was studied with three murine tumor cell types: an IgG Fc receptor-negative nonphagocytic line (EL4); an Fc receptor-positive phagocytic line (P388D1); and an Fc receptor-positive nonphagocytic line (P388). The liposomes (formed from phosphatidylcholines, cholesterol, and dinitrophenyl-substituted phosphatidylethanolamine) contained carboxyfluorescein as ... More
Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein.
Authors:Zeidel ML, Ambudkar SV, Smith BL, Agre P
Journal:Biochemistry
PubMed ID:1510932
'Water rapidly crosses the plasma membranes of red blood cells (RBCs) and renal tubules through highly specialized channels. CHIP28 is an abundant integral membrane protein in RBCs and renal tubules, and Xenopus laevis oocytes injected with CHIP28 RNA exhibit high osmotic water permeability, Pf [Preston et al. (1992) Science 256, ... More
Mechanistic studies of lantibiotic-induced permeabilization of phospholipid vesicles.
Authors:Driessen AJ, van den Hooven HW, Kuiper W, van de Kamp M, Sahl HG, Konings RN, Konings WN
Journal:Biochemistry
PubMed ID:7849020
'Nisin is a cationic polycyclic bacteriocin secreted by some lactic acid bacteria. Nisin has previously been shown to permeabilize liposomes. The interaction of nisin was analyzed with liposomes prepared of the zwitterionic phosphatidylcholine (PC) and the anionic phosphatidylglycerol (PG). Nisin induces the release of 6-carboxyfluorescein and other small anionic fluorescent ... More
Luminal pH regulated calcium release kinetics in sarcoplasmic reticulum vesicles.
Authors:Donoso P, Beltrán M, Hidalgo C
Journal:Biochemistry
PubMed ID:8873610
'Calcium binding to triads isolated from rabbit skeletal muscle followed a single hyperbolic function in the pH range 5.5-8.0. Maximal binding was obtained at pH 8.0; decreasing the pH decreased the binding capacity and, at pH < or = 6.0, increased Kd 2-fold. These results indicate that lowering the pH ... More