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G0635 Sigma

Guanosine 5′-[β,γ-imido]triphosphate trisodium salt hydrate

≥85% (HPLC), powder

Synonym: β:γ-Imidoguanosine 5′-triphosphate trisodium salt hydrate, 5′-Guanylyl-imidodiphosphate trisodium salt hydrate, GMP-PNP, Gpp(NH)p



Related Categories Biochemicals and Reagents, Cell Biology, Cell Signaling and Neuroscience, Cofactors, Core Bioreagents,
assay   ≥85% (HPLC)
form   powder
color   white
solubility   H2O: soluble50 mg/mL
shipped in   dry ice
storage temp.   −20°C



Non-hydrolyzable analog of GTP; the preferred GTP analog to activate ADP-ribosylation factor.

Guanosine 5′-[β,γ-imido]triphosphate (GMP-PNP, Gpp(NH)p) is a non-hydrolyzable analog of GTP that binds and irreversibly activates G proteins. Gpp(NH)p is used in a variety of applications that involve GTP binding, including GTP-activation, GTP-inhibition, GTP transport, GTP hydrolysis, and GTP structure stabilization. Since a cycle of GTP binding, hydrolysis, and release is required for the initiation of protein translocation across the endoplasmic reticulum, guanosine 5′-[β,γ-imido]triphosphate is often used in studies of protein synthesis. Gpp(NH)p is used to activate ADP-ribosylation factors and to modulate G proteins involved in cell signaling, protein synthesis and other metabolic processes.

Biochem/physiol Actions

Binds and irreversibly activates G proteins.1 Since a cycle of GTP binding, hydrolysis, and release is required for the initiation of protein translocation across the endoplasmic reticulum, this non-hydrolyzable GTP analog is often used in studies of protein synthesis.2,3

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Safety & Documentation

Safety Information

GHS07  GHS07
Signal word 
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
WGK Germany 
Protocols & Articles
Peer-Reviewed Papers


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1. G proteins. Hepler, J.R., and Gilman, A.G. Trends Biochem. Sci. 17, 383-387, (1992)


2. A GTPase cycle in initiation of protein translocation across the endoplasmic reticulum membrane. Miller, J.D., and Walter, P. Ciba Found. Symp. 176, 147-163, (1993)


3. Requirement of GTP hydrolysis for dissociation of the signal recognition particle from its receptor. Connolly, T., et al. Science 252, 1171-1173, (1991)


Structural switch of the γ subunit in an archaeal aIF2 α γ heterodimer. Yatime L, Mechulam Y, et al. Structure 14, 119-128, (2006)


Loss Of Function Of The Tumor Suppressor DKC1 Perturbs P27 Translation Control And Contributes To Pituitary Tumorigenesis. Bellodi, C., et al. Cancer Res. 70, 6026-35, (2010)


Ultracytochemical demonstration of soluble guanylate cyclase activation in rat aorta by NCX4016, a NO-releasing aspirin derivative. Rambotti MG, Mariucci G, et al. J. Submicrosc. Cytol. Pathol. 38, 149-154, (2006)


Cholera toxin-catalyzed [32P]ADP-ribosylation of proteins. Gill, D.M., and Woolkalis, M.J. Meth. Enzymol. 195, 267-280, (1991)


Agonist binding fraction of dopamine D2/3 receptors in rat brain: a quantitative autoradiographic study. Minuzzi L, Cumming P. Neurochem. Int. 56, 747-752, (2010)


Crystal structure of M-Ras reveals a GTP-bound "off" state conformation of Ras family small GTPases. Ye M, Shima F, Muraoka S, et al. J. Biol. Chem. 280, 31267-31275, (2005)


Characterization of active and inactive states of CB1 receptor and the differential binding state modulation by cannabinoid agonists, antagonists and inverse agonists. Gullapalli S, Amrutkar D, Gupta S, et al. Neuropharmacology 58, 1215-1219, (2010)


Decrease in apparent α1-adrenoceptor-G protein coupling during maturation in rat aorta. Gurdal H, Friedman E, et al. J. Gerontol. A. Biol. Sci. Med. Sci. 53, B268-B273, (1998)


Preliminary biochemical characterization of the novel, non-AT1, non-AT2 angiotensin binding site from the rat brain. Karamyan VT, Arsenault J, et al. Endocrine 37, 442-448, (2010)


Insights from reconstitution reactions of COPII vesicle formation using pure components and low mechanical perturbation. Daum S, Krüger D, Meister A, et al. Biol. Chem. 395(7-8), 801-12, (2014)


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