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Citas y referencias (25)
Invitrogen™
Oregon Green™ 488 Maleimide
La maleimida Oregon Green™ 488 reactiva al tiol puede usarse para crear bioconjugados de fluorescencia verde con una excitación/emisión máximaMás información
| Número de catálogo | Cantidad |
|---|---|
| O6034 | 5 mg |
Número de catálogo O6034
Precio (CLP)
460.472
Each
Cantidad:
5 mg
Precio (CLP)
460.472
Each
La maleimida Oregon Green™ 488 reactiva al tiol puede usarse para crear bioconjugados de fluorescencia verde con una excitación/emisión máxima de ∼496/524 nm.
Este análogo fluorado de la fluoresceína supera algunas de las limitaciones clave de la fluoresceína, incluidas una mayor fotoestabilidad y una pKa más baja (pKa ∼ 4,7 frente a 6,4 de la fluoresceína), lo que hace que su fluorescencia sea esencialmente insensible al pH en el rango de pH fisiológico.
Este análogo fluorado de la fluoresceína supera algunas de las limitaciones clave de la fluoresceína, incluidas una mayor fotoestabilidad y una pKa más baja (pKa ∼ 4,7 frente a 6,4 de la fluoresceína), lo que hace que su fluorescencia sea esencialmente insensible al pH en el rango de pH fisiológico.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Reactividad químicaTiol
Emisión524
Excitación496
Etiqueta o tinteOregon Green™ 488
Tipo de productoMaleimida
Cantidad5 mg
Fracción reactivaMaleimida
Condiciones de envíoTemperatura ambiente
Tipo de etiquetaColorantes clásicos
Línea de productosOregon Green
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador (de – 5 a – 30 °C) y proteger de la luz.
Citations & References (25)
Citations & References
Abstract
Effect of the substitution of muscle actin-specific subdomain 1 and 2 residues in yeast actin on actin function.
Journal:J Biol Chem
PubMed ID:16882670
'Muscle and yeast actins display distinct behavioral characteristics. To better understand the allosteric interactions that regulate actin function, we created a muscle/yeast hybrid actin containing a muscle-specific outer domain (subdomains 1 and 2) and a yeast inner domain (subdomains 3 and 4). Actin with muscle subdomain 1 and the two
Activation of human acid sphingomyelinase through modification or deletion of C-terminal cysteine.
Journal:J Biol Chem
PubMed ID:12801930
'One form of Niemann-Pick disease is caused by a deficiency in the enzymatic activity of acid sphingomyelinase. During efforts to develop an enzyme replacement therapy based on a recombinant form of human acid sphingomyelinase (rhASM), purified preparations of the recombinant enzyme were found to have substantially increased specific activity if
A pathway of structural changes produced by monastrol binding to Eg5.
Journal:J Biol Chem
PubMed ID:16434397
'Monastrol is a small molecule inhibitor that is specific for Eg5, a member of the kinesin 5 family of mitotic motors. Crystallographic models of Eg5 in the presence and absence of monastrol revealed that drug binding produces a variety of structural changes in the motor, including in loop L5 and
A fluorescent glycolipid-binding peptide probe traces cholesterol dependent microdomain-derived trafficking pathways.
Journal:PLoS ONE
PubMed ID:18716682
'BACKGROUND: The uptake and intracellular trafficking of sphingolipids, which self-associate into plasma membrane microdomains, is associated with many pathological conditions, including viral and toxin infection, lipid storage disease, and neurodegenerative disease. However, the means available to label the trafficking pathways of sphingolipids in live cells are extremely limited. In order
Structure-function relationships in OxlT, the oxalate/formate transporter of Oxalobacter formigenes. Topological features of transmembrane helix 11 as visualized by site-directed fluorescent labeling.
Journal:J Biol Chem
PubMed ID:9651403
'Analysis of hydropathy suggests that in OxlT, the oxalate/formate antiporter of Oxalobacter formigenes, lysine 355 is within transmembrane helix no. 11. To test this idea, we used single-cysteine, histidine-tagged OxlT variants to study the organization of a 30-residue segment (residues 344-373) containing this region. Topology was examined by probing the