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2'/3'-O-(N-Methyl-anthraniloyl)-guanosine-5'-triphosphate, Triethylammonium salt

Product Cat. No. Amount Price (EUR) Buy / Note
Mant-GTP NU-206S 150 μl (10 mM) 115,56 Add to Basket/Quote Add to Notepad
Mant-GTP NU-206L 5 x 150 μl (10 mM) 338,49 Add to Basket/Quote Add to Notepad

Structural formula of Mant-GTP

For research use only!

Shipping: shipped on blue ice

Storage Conditions: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible. If stored as recommended, Jena Bioscience guarantees optimal performance of this product for 12 months after date of delivery.

Shelf Life: 12 months

Molecular Formula: C18H23N6O15P3 (free acid)

Molecular Weight: 656.33 g/mol (free acid)

CAS#: 148821-03-8

Purity: ≥ 95 % (HPLC)

Form: colorless to slightly yellow solution in water, pH 7.5 ±0.5

Concentration: 10 mM - 11 mM

pH: 7.5 ±0.5

Spectroscopic Properties: λmax 252/355 nm; ε 22.6/5.7 L mmol-1 cm-1 (Tris-HCl pH 7.5); λexc 355 nm; λem 448 nm

Inhibition of AC-isoform[1] and GTPs[2]
Activity measurement: GC[3]
Specifity measurements with isoforms of ACs[4]
FRET: AC[5], edema factor[6]
Inhibition of edema factor (anthrax)[6]

Selected References:
[1] Gille et al. (2003) Mant-substituted guanine nucleotides: A novel class of potent adenylyl cyclase inhibitors. Life Sciences 74:271.
[2] Gille et al. (2004) Differential inhibition of adenylyl cyclase isoforms and soluble guanylyl cyclase by purine and pyrimidine nucleotides. J. Biol. Chem. 279:19955.
[3] Newton et al. (2010) A real-time fluorescent assay of the purified nitric oxide receptor, guanylyl cyclase. Analytical Biochem. 402:129.
[4] Mou et al. (2006) Broad specifity of mammalian adenylyl cyclase for interaction with 2,3-substituted purine- and pyrimidine-nucleotide inhibitors. Molecular Pharmacology 70:878.
[5] Goettle et al. (2007) Molecular analysis of the interaction of Bordetella pertussis adenylyl cyclase with fluorescent nucleotides. Molecular Pharmacology 72 (3):526.
[6] Suryanarayana et al. (2009) Distinct interactions of 2- and 3-O- (N-methyl)anthraniloyl-isomers of ATP and GTP with the adenylyl cyclase toxin from Bacillus anthraxis, edema factor. Biochem. Pharmacol. 78:224.
Seifert et al. (2012) Inhibitors of membranous adenylyl cyclases. Trends Pharmacol Sci. 33 (2):64.
Erdorf et al. (2011) Pharmacological characterization of adenylyl cyclase isoforms in rabbit kidney membranes. Naunyn Schmiedebergs Arch. Pharmacol. 383 (4):357.
Labesse et al. (2011) Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation. Nucleic Acids Res. 39 (8):3458.
Pinto et al. (2011) Structure-activity relationships for the interactions of 2'- and 3'- (O)- (N-methyl)anthraniloyl-substituted purine and pyrimidine nucleotides with mammalian adenylyl cyclases. Biochem. Pharmacol. 82 (4):358.
Spangler et al. (2011) Interaction of the diguanylate cyclase YdeH of Escherichia coli with 2', (3')-substituted purine and pyrimidine nucleotides. J. Pharmacol. Exp. Ther. 336 (1):234.
Wang et al. (2011) Charge isomers of myelin basic protein: structure and interactions with membranes, nucleotide analogues, and calmodulin. PLoS One. 6 (5):e19915.
Goettle et al. (2010) Cytidylyl and uridylyl cyclase activity of bacillus anthracis edema factor and Bordetella pertussis CyaA. Biochemistry. 49 (26):5494.
Taha et al. (2009) Molecular Analysis of the Interaction of Anthrax Adenylyl Cyclase Toxin, Edema Factor, with 2' (3')-O- (N- (methyl)anthraniloyl)-Substituted Purine and Pyrimidine Nucleotides. Molecular Pharmacology. 75 (3):693.
Wang et al. (2009) Regulation of Immature Dendritic Cell Migration by RhoA Guanine Nucleotide Exchange Factor Arhgef5. J. Mol. Chem. 284 (42):28599.
Dahl et al. (2008) The Importance of P-loop and Domain Movements in EF-Tu for Guanine Nucleotide Exchange. J. Biol. Chem. 281 (30):21139.
Kambach et al. (2007) Human OLA1 Defines an ATPase subfamily in the Obg Family of GTP-binding proteins. J. Biol. Chem. 282 (27):19928.
Pestova et al. (2006) Kinetic Analysis of Interaction of Eukaryotic Release Factor 3 with Guanine Nucleotides. J. Biol. Chem. 281 (52):40224.
Sprang et al. (2006) Broad and Specifity of Mammalian Adenylyl Cyclase for Interaction with 2',3'-Substituted Purine- and Pyrimidine Nucleotide Inhibitors. Mol. Pharmacol. 70:878.
Wintermeyer et al. (2006) Role and timing of GTP binding and hydrolysis during EF-G-dependent RNA translocation on the ribosome. PNAS 103 (37):13670.
Alexandrov et al. (2001) Fluorescence methods for monitoring interactions of Rab proteins with nucleotides, Rab escort protein, and geranylgeranyltransferase. Methods Enzymol. 329:14.
Simon et al. (1996) Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions. J. Biol. Chem. 271:20470.
Remmers et al. (1994) Fluorescent guanine nucleotide analogs and G protein activation. J. Biol. Chem. 269:13771.
Brownbridge et al. (1993) Interaction of GTPase activating proteins (GAPs) with p21ras measured by a novel fluorescence anisotropy method. Essential role of Arg-903 of GAP in activation of GTP hydrolysis on p21ras. J. Biol. Chem. 268:10914.
Hazlett et al. (1993) Solution dynamics of p21ras proteins bound with fluorescent nucleotides: a time-resolved fluorescence study. Biochemistry 32:13575.
Eccleston et al. (1991) Fluorescence approaches to the study of the p21ras GTPase mechanism. Biochem. Soc. Trans. 19:432.