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Citas y referencias (6)
Invitrogen™
Tetramethylrhodamine Cadaverine, 5-(and-6)-((N-(5-Aminopentyl) Amino) Carbonyl) Tetramethylrhodamine, mixed isomers
La amina alifática primaria de tetrametilrodamina cadaverina se puede acoplar de forma reversible a aldehídos y cetonas para formar unaMás información
| Número de catálogo | Cantidad |
|---|---|
| A1318 también denominado A-1318 | 10 mg |
Número de catálogo A1318
también denominado A-1318
Precio (CLP)
-
Cantidad:
10 mg
La amina alifática primaria de tetrametilrodamina cadaverina se puede acoplar de forma reversible a aldehídos y cetonas para formar una base de Schiff, que puede reducirse a un derivado de amina estable generado por el borohidruro de sodio (NaBH4) o cianoborohidruro de sodio (NaCNH3). Los ácidos carboxílicos de las proteínas y otros biopolímeros solubles en agua pueden acoplarse a esta molécula en una solución acuosa usando carbodiimidas solubles en agua como EDAC (E2247). Este material contiene el isómero 5 y 6. Consulte la estructura para obtener más detalles.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaÁcido carboxílico, cetona, aldehído
Etiqueta o tinteTMR (tetrametilrodamina)
Tipo de productoTetrametilrodamina cadaverina
Cantidad10 mg
Fracción reactivaAmina, cadaverina
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador (de – 5 a – 30 °C) y proteger de la luz.
Citations & References (6)
Citations & References
Abstract
Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin.
Journal:Biophys J
PubMed ID:16997870
'Cofilin/ADF, beryllium fluoride complex (BeFx), and phalloidin have opposing effects on actin filament structure and dynamics. Cofilin/ADF decreases the stability of F-actin by enhancing disorder in subdomain 2, and by severing and accelerating the depolymerization of the filament. BeFx and phalloidin stabilize the subdomain 2 structure and decrease the critical
Dynamic polymorphism of single actin molecules in the actin filament.
Journal:Nat Chem Biol
PubMed ID:16415860
'Actin filament dynamics are critical in cell motility. The structure of actin filament changes spontaneously and can also be regulated by actin-binding proteins, allowing actin to readily function in response to external stimuli. The interaction with the motor protein myosin changes the dynamic nature of actin filaments. However, the molecular
Synthesis and characterization of conjugates formed between periodate-oxidized ribonucleotides and amine-containing fluorophores.
Journal:Bioconjug Chem
PubMed ID:7849074
The synthesis and purification of new fluorescently labeled derivatives of GDP and ATP are described. The fluorescent groups are coupled initially through amine-containing linker arms to periodate-oxidized nucleotides. Reduction of the initial product yields primarily a six-membered morpholine-like ring. Fluorescein-labeled GDP, rhodamine-labeled GDP, and fluorescein-labeled ATP were characterized by absorbance
The mitogen-activated protein kinase kinase kinase dual leucine zipper-bearing kinase (DLK) acts as a key regulator of keratinocyte terminal differentiation.
Journal:J Biol Chem
PubMed ID:15695824
In the skin, epithelial cells undergo a terminal differentiation program leading to the formation of the stratum corneum. Although it is expected that the last phases of this process must be tightly regulated since it results in cell death, the signaling pathways involved in this induction remain ill defined. We
Orientation of actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation.
Journal:Biochemistry
PubMed ID:3166995
We have employed the method of radial distance measurements in order to orient the actin monomer in the F-actin filament. This method utilizes fluorescence resonance energy transfer measurements of the distance between two equivalent chemical points located on two different monomers. The interprobe distance obtained this way is used to