MANT-GTP (2'-(or-3')-<i>O</i>-(<i>N</i>-Methylanthraniloyl) Guanosine 5'-Triphosphate, Trisodium Salt)
Invitrogen™

MANT-GTP (2'-(or-3')-O-(N-Methylanthraniloyl) Guanosine 5'-Triphosphate, Trisodium Salt)

L’analogue nucléotidique MANT GTP est modifié sur la fraction ribose. La mature compacte du fluorophore MANT et sa position d’adhérenceAfficher plus
Have Questions?
RéférenceQuantité
M12415400 μl
Référence M12415
Prix (EUR)
642,00
Each
Quantité:
400 μl
Prix (EUR)
642,00
Each
L’analogue nucléotidique MANT GTP 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
Marqueur ou colorantMANT (N-méthylanthraniloyle)
Type de produitMANT-GTP
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 (48)

Citations et références
Abstract
Authors:
Journal:
PubMed ID:11063593
Activation of the superoxide-generating NADPH oxidase by chimeric proteins consisting of segments of the cytosolic component p67(phox) and the small GTPase Rac1.
Authors:Alloul N, Gorzalczany Y, Itan M, Sigal N, Pick E
Journal:Biochemistry
PubMed ID:11724569
'Activation of the superoxide (O2(-))-generating NADPH oxidase of phagocytes is the consequence of the assembly of a membrane-associated flavocytochrome b(559) with the cytosolic proteins p47(phox) and p67(phox) and the small GTPase Rac (1 or 2). We proposed that Rac1 serves as a membrane-targeting molecule for p67(phox). This hypothesis was tested ... More
A novel function for Cyclin A2: control of cell invasion via RhoA signaling.
Authors:Arsic N, Bendris N, Peter M, Begon-Pescia C, Rebouissou C, Gadéa G, Bouquier N, Bibeau F, Lemmers B, Blanchard JM,
Journal:J Cell Biol
PubMed ID:22232705
'Cyclin A2 plays a key role in cell cycle regulation. It is essential in embryonic cells and in the hematopoietic lineage yet dispensable in fibroblasts. In this paper, we demonstrate that Cyclin A2-depleted cells display a cortical distribution of actin filaments and increased migration. These defects are rescued by restoration ... More
Low affinity interactions of GDPbetaS and ribose- or phosphoryl-substituted GTP analogues with the heterotrimeric G protein, transducin.
Authors:Zera EM, Molloy DP, Angleson JK, Lamture JB, Wensel TG, Malinski JA
Journal:J Biol Chem
PubMed ID:8662741
'We have examined the effects of three commonly used classes of guanine nucleotide analogues on the retinal G protein, transducin (Gt), and found them to be quite different from those that might be expected from results with other GTP-binding proteins. The most surprising results were with guanosine 5''-O-(2-thiodiphosphate) (GDPbetaS); rather ... 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