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Citas y referencias (51)
Invitrogen™
MANT-GDP (2'-(or-3')-O-(N-Methylanthraniloyl) Guanosine 5'-Diphosphate, Disodium Salt)
El análogo nucleótido MANT GDP se modifica en la fracción de la ribosa. La madurez compacta del fluoróforo de MANTMás información
| Número de catálogo | Cantidad |
|---|---|
| M12414 | 400 μl |
Número de catálogo M12414
Precio (MXN)
-
Cantidad:
400 μl
El análogo nucleótido MANT GDP 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
Método de etiquetadoMarcaje químico, marcaje directo
Etiqueta o tinteMANT (N-Methylanthraniloyl)
Tipo de productoMANT-GDP
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 (51)
Citations & References
Abstract
Journal:
PubMed ID:11063593
The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins.
Journal:J Biol Chem
PubMed ID:10843989
'The biological activities of Rho family GTPases are controlled by their guanine nucleotide binding states in cells. Here we have investigated the role of Mg(2+) cofactor in the guanine nucleotide binding and hydrolysis processes of the Rho family members, Cdc42, Rac1, and RhoA. Differing from Ras and Rab proteins, which
Kinetics of Cdc42 membrane extraction by Rho-GDI monitored by real-time fluorescence resonance energy transfer.
Journal:Biochemistry
PubMed ID:10026253
'The mechanisms underlying the ability of the Rho-GDP dissociation inhibitor (RhoGDI) to elicit the release of Rho-related GTP-binding proteins from membranes is currently unknown. In this report, we have set out to address this issue by using fluorescence resonance energy transfer approaches to examine the functional interactions of the RhoGDI
Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for RhoGTPases.
Journal:J Biol Chem
PubMed ID:10521431
'RhoGTPases are key regulators of eukaryotic cell physiology. The bacterial enteropathogen Salmonella typhimurium modulates host cell physiology by translocating specific toxins into the cytoplasm of host cells that induce responses such as apoptotic cell death in macrophages, the production of proinflammatory cytokines, the rearrangement of the host cell actin cytoskeleton
Alanine scan mutagenesis of the switch I domain of the Caulobacter crescentus CgtA protein reveals critical amino acids required for in vivo function.
Journal:Mol Microbiol
PubMed ID:11251813
'The Caulobacter crescentus CgtA protein is a member of the Obg/GTP1 subfamily of monomeric GTP-binding proteins. In vitro, CgtA displays moderate affinity for both GDP and GTP and displays rapid exchange rate constants for either nucleotide, indicating that the guanine nucleotide-binding and exchange properties of CgtA are different from those