MANT-GDP (2'-(or-3')-<i>O</i>-(<i>N</i>-Methylanthraniloyl) Guanosine 5'-Diphosphate, Disodium Salt)
Invitrogen™

MANT-GDP (2'-(or-3')-O-(N-Methylanthraniloyl) Guanosine 5'-Diphosphate, Disodium Salt)

L’analogue nucléotidique MANT GDP est modifié sur la fraction ribose. La mature compacte du fluorophore MANT et sa position d’adhérenceAfficher plus
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RéférenceQuantité
M12414400 μl
Référence M12414
Prix (EUR)
674,00
Each
Quantité:
400 μl
Prix (EUR)
674,00
Each
L’analogue nucléotidique MANT GDP est modifié sur la fraction ribose. La mature compacte du fluorophore MANT et sa position d’adhérence entraînent des analogues de nucléotides qui induisent une perturbation minimale des interactions nucléotides-protéines. La fluorescence MANT étant sensible à l’environnement du fluorophore, les interactions nucléotides-protéines peuvent être directement détectables. Les nucléotides MANT constituent des sondes importantes de la structure et de l’activité enzymatique des protéines liant les nucléotides.
Usage exclusivement réservé à la recherche. Ne pas utiliser pour des procédures de diagnostic.
Spécifications
Méthode d’étiquetageMarquage chimique, marquage direct
Marqueur ou colorantMANT (N-méthylanthraniloyle)
Type de produitMANT-GDP
Quantité400 μl
Conditions d’expéditionGlace humide
Concentration5 mM
Unit SizeEach
Contenu et stockage
Stocker au congélateur (entre -5°C et -30°C) à l’abri de la lumière.

Citations et références (51)

Citations et références
Abstract
Authors:
Journal:
PubMed ID:11063593
The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins.
Authors:Zhang B, Zhang Y, Wang Z, Zheng Y
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 ... More
Kinetics of Cdc42 membrane extraction by Rho-GDI monitored by real-time fluorescence resonance energy transfer.
Authors:Nomanbhoy TK, Erickson JW, Cerione RA
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 ... More
Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for RhoGTPases.
Authors:Rudolph MG, Weise C, Mirold S, Hillenbrand B, Bader B, Wittinghofer A, Hardt WD
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 ... More
Alanine scan mutagenesis of the switch I domain of the Caulobacter crescentus CgtA protein reveals critical amino acids required for in vivo function.
Authors:Lin B, Skidmore JM, Bhatt A, Pfeffer SM, Pawloski L, Maddock JR
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 ... More