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Citas y referencias (82)
Invitrogen™
MANT-ATP (2'-(or-3')-O-(N-Methylanthraniloyl) Adenosine 5'-Triphosphate, Trisodium Salt)
El análogo nucleótido MANT ATP se modifica en la fracción de la ribosa. La madurez compacta del fluoróforo de MANTMás información
| Número de catálogo | Cantidad |
|---|---|
| M12417 | 400 μl |
Número de catálogo M12417
Precio (CLP)
501.708
Each
Cantidad:
400 μl
Precio (CLP)
501.708
Each
El análogo nucleótido MANT ATP se modifica en la fracción de la ribosa. La madurez compacta del fluoróforo de MANT y su posición de fijación resulta en análogos de nucleótidos que inducen una perturbación mínima de las interacciones de nucleótidos-proteínas. Debido a que la fluorescencia de MANT es sensible al ambiente del fluoróforo, las interacciones nucleótido-proteína pueden ser directamente detectables. Los nucleótidos MANT son valiosas sondas de la estructura y actividad enzimática de las proteínas de unión a nucleótidos.
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
Especificaciones
Etiqueta o tinteMANT (N-Methylanthraniloyl)
Tipo de productoMANT-ATP
Cantidad400 μl
Condiciones de envíoHielo húmedo
Concentración5 mM
Unit SizeEach
Contenido y almacenamiento
Almacenar en el congelador de -5 °C a -30 °C y proteger de la luz.
Citations & References (82)
Citations & References
Abstract
Journal:
PubMed ID:11063593
A mechanistic model for Ncd directionality.
Journal:J Biol Chem
PubMed ID:11278404
Ncd is a kinesin-related protein that drives movement to the minus-end of microtubules. Pre-steady-state kinetic experiments have been employed to investigate the cooperative interactions between the motor domains of the MC1 dimer and to establish the ATPase mechanism. Our results indicate that the active sites of dimeric Ncd free in
Moving a microtubule may require two heads: a kinetic investigation of monomeric Ncd.
Journal:Biochemistry
PubMed ID:10684615
'Ncd is a minus-end-directed microtubule motor and a member of the kinesin superfamily. The Ncd dimer contains two motor domains, and cooperative interactions between the heads influence the interactions of each respective motor domain with the microtubule. The approach we have taken to understand the cooperativity between the two motor
Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein.
Journal:Biochemistry
PubMed ID:11041861
'Quantitative analyses of the interactions of nucleotide cofactors with the Escherichia coli replicative factor DnaC protein have been performed using thermodynamically rigorous fluorescence titration techniques. This approach allowed us to obtain stoichiometries of the formed complexes and interaction parameters, without any assumptions about the relationship between the observed signal and
The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity.
Journal:Biochemistry
PubMed ID:10090768
'We are interested in the role that solvent-exposed, proteolytically sensitive surface loops play in myosin function. The 25-50K loop, or loop 1, is near the ATP binding site, while the 50-20K loop (loop 2) is in the actin binding site. Through chimeric studies, we have found that loop 1 affects