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Mant-GppNHp

(Mant-GMPPNP)

2'/3'-O-(N-Methyl-anthraniloyl)-guanosine-5'-[(β,γ)-imido]triphosphate, Triethylammonium salt

Cat. No. Amount Price (EUR) Buy / Note
NU-207S 10 μl (10 mM) 126,24 Add to Basket/Quote Add to Notepad
NU-207L 5 x 10 μl (10 mM) 369,76 Add to Basket/Quote Add to Notepad
Structural formula of Mant-GppNHp ((Mant-GMPPNP), 2'/3'-O-(N-Methyl-anthraniloyl)-guanosine-5'-[(β,γ)-imido]triphosphate, Triethylammonium salt)
Structural formula of Mant-GppNHp

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.

Shelf Life: 6 months after date of delivery

Molecular Formula: C18H24N7O14P3 (free acid)

Molecular Weight: 655.34 g/mol (free acid)

CAS#: 148821-01-6

Purity: ≥ 90 % (HPLC)

Form: colorless to slightly yellow solution in water

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

Applications:
Inhibition of AC-isoforms[1, 2]

Specific Ligands:

Gs/Gi-proteins[3]

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. (2003) 2' (3')-O- (N-methylanthraniloyl)-substituted GTP analogs: a novel class of potent competitive adenylyl cyclase inhibitors. J. Biol. Chem. 278:12672.
[3] Gille and Seifert (2003) Low affinity interactions of BODIPY-FL-GTPyS and BODIPY-FL-GppNHp with Gi- and Gs-proteins. Naunyn Schmiedebergs Archiv of Pharmacology 368:210.
Wehner et al. (2012) The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis. FEBS J. 279 (2):203.
Ugolev et al. (2008) Dissociation of Rac1 (GDP).RhoGDI Complexes by the Cooperative Action of Anionic Liposomes Containing Phosphatidylinositol 3,4,5-Trisphosphate, Rac Guanine Nucleotide Exchange Factor, and GTP. J. Biol. Chem. 283 (32):22257.
Ugolev et al. (2008) Liposomes Comprising Anionic but Not Neutral Phospholipids Cause Dissociation of Rac (1 or 2).RhoGDI Complexes and Support Amphiphile-independent NADPH Oxidase Activation by Such Complexes. J. Biol. Chem. 281 (28):19204.
Kambach et al. (2007) Human OLA1 Defines an ATPase subfamily in the Obg Family of GTP-binding proteins. J. Biol. Chem. 282 (27):19928.
Pick et al. (2007) Tripartite Chimeras Comprising Functional Domains Derived from the Cytosolic NADPH Oxidase components p47phox, p67phox, and Rac1 elicit Activator-independent Superoxide Production by Phagocyte Membranes. J. Biol. Chem. 282 (30):22122.
Pick et al. (2006) Liposomes Comprising Anionic but not neutral Phospholipids cause dissociation of Rac (1 or 2)RhoGDI Complexes and support Amphiphile-independent NADPH oxidase Activation by Such Complexes. J. Biol. Chem. 281 (28):19204.
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.
Diebold et al. (2001) Molecular basis for Rac2 regulation of phagocyte NADPH oxidase. Nature Immunol. 2:211.
Graham et al. (1999) The conserved arginine in rho-GTPase-activating protein is essential for efficient catalysis but not for complex formation with Rho.GDP and aluminum fluoride. Biochemistry 38:985.
Nisimoto et al. (1997) Rac binding to p67 (phox). Structural basis for interactions of the Rac1 effector region and insert region with components of the respiratory burst oxidase. J. Biol. Chem. 272:18834.
Herrmann et al. (1996) Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271:6794.
Herrmann et al. (1995) Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase. J. Biol. Chem. 270:2901.
Neal et al. (1990) Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. Proc. Natl. Acad. Sci. USA 87:3562.