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Citas y referencias (151)
Invitrogen™
Tetramethylrhodamine-5-Iodoacetamide Dihydroiodide (5-TMRIA), single isomer
El dihidroyoduro de tetrametilrodamina-5-yodoacetamida (5-TMRIA) reactivo a tioles puede utilizarse para crear bioconjugados brillantes de color rojo anaranjado fluorescente conMás información
| Número de catálogo | Cantidad |
|---|---|
| T6006 | 5 mg |
Número de catálogo T6006
Precio (MXN)
-
Cantidad:
5 mg
El dihidroyoduro de tetrametilrodamina-5-yodoacetamida (5-TMRIA) reactivo a tioles puede utilizarse para crear bioconjugados brillantes de color rojo anaranjado fluorescente con un máximo de excitación/emisión de ∼ 555/580.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaTiol
Emisión580
Excitación555
Etiqueta o tinteIsómeros de rodamina, TMR (tetrametilrodamina)
Tipo de productoTetrametilrodamina-5-Iodoacetamida dihidroyoduro
Cantidad5 mg
Fracción reactivaHaluro de alquilo, yodoacetamida
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Unit Size5 mg
Contenido y almacenamiento
Almacenar en el congelador (de – 5 a – 30 °C) y proteger de la luz.
Citations & References (151)
Citations & References
Abstract
Rapid binding of synapsin I to F- and G-actin. A study using fluorescence resonance energy transfer.
Journal:FEBS Lett
PubMed ID:8365471
Synapsin I is a nerve terminal phosphoprotein which interacts with synaptic vesicles and actin in a phosphorylation-dependent manner. By using fluorescence resonance energy transfer between purified components labeled with fluorescent probes, we now show that the binding of synapsin I to actin is a rapid phenomenon. Binding of synapsin I
A non-radioactive automated method for DNA sequence determination.
Journal:J Biochem Biophys Methods
PubMed ID:3559035
A method and instrument for automated DNA sequencing without radioactivity have been developed. In spite of the success with radioactive labels there are drawbacks attached to the technique, such as hazards in the handling, storage and disposal of radioactive materials, and the considerable cost of the radiolabelled nucleoside triphosphates. In
Functional studies of the domains of talin.
Journal:J Cell Biol
PubMed ID:2110569
'The protein talin has two domains of approximately 200 and 47 kD, which can be cleaved apart by a variety of proteases. To examine the function of these two structural domains of talin, we have digested purified talin with a calcium-dependent protease and separated the resulting fragments chromatographically. Both fragments
Low molecular-weight G-actin binding proteins involved in the regulation of actin assembly during myofibrillogenesis.
Journal:Cell Struct Funct
PubMed ID:9113405
'We previously demonstrated that small G-actin binding proteins, cofilin, ADF and profilin, are involved in the actin dynamics during myofibrillogenesis (OBINATA, T. (1993). Int. Rev. Cytol., 143: 153-189.). To better understand how they are responsible for the regulation of actin assembly, the amounts of the actin-binding proteins were quantified by
Association of microinjected myosin and its subfragments with myofibrils in living muscle cells.
Journal:J Cell Biol
PubMed ID:3058721
'Purified skeletal muscle myosin was labeled with iodoacetamidofluorescein and microinjected into cultured chick myotubes. The fluorescent myosin analogue became incorporated within 10-15 min after injection, into either periodic (mean periodicity = 2.23 +/- 0.02 micron) bands or apparently continuous fibrillar structures. Comparison of rhodamine-labeled alpha-actinin with coinjected fluorescein-labeled myosin suggested