Guanosine-5'-[( β,γ )-imido]triphosphate, Tetralithium salt
For research use only!
Shipping: shipped on dry 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: C10H17N6O13P3 (free acid)
Molecular Weight: 522.19 g/mol (free acid)
Exact Mass: 522.01 g/mol (free acid)
Purity: ≥ 95 % (HPLC)
Color: white to off-white
Spectroscopic Properties: λmax 252 nm, ε 13.7 L mmol-1 cm-1 (Tris-HCl pH 7.5)
X-ray elongation factor EF-G
X-ray with Rab27
Conformational switch of IF(α,β,y)
Dynamic of ribosomes
Intitiation factors IF2, IF(α,β,y) and elongation factor EF-G[5, 6]
Please note: For reasons of stability, please make sure that the pH value of a solution of this product never drops below 7.0. This can be achieved by dissolving the nucleotide in a buffer of your choice (50 - 100 mM, pH 7 - 10). Dissolve and adjust concentration photometrically.
When stored at -20 °C, product may hydrolyze, thereby forming GppNH2 at a rate of up to 1 % per month!
Please click the black arrow on the right to expand the citation list. Click publication title for the full text.
 Hansson et al. (2005) Crystall structure of a mutant elongation factor G trapped with a GTP analogue. FEBS Letters 579:4492.
 Chavas et al. (2009) Structural insights into Rab27 recruitment by ist effectors. Nippon Kessho Gakkaishi 51:334.
 Makoto et al. (2008) Thermodynamic analysisreveals that GTP Binding affects the interaction between the alpha- and gamma-subunits of translation initiation factor 2. Biochem. Biophys. Res. Com. 371:596.
 Ermolenko et al. (2007) Observation of intersubunit movement of the ribosome in solution using FRET. J. Mol. Biol. 370:530.
 Burakovsky et.al. (2007) The interaction with Escherichia coli 23S rRNA helices 89 and 91 contributes to the IF2 activity but is insignificant for the functioning of the elongation factors. Mol. Biol. 41:939.
 Spiegel et al. (2007) Elongation factor G stabilizes the hybrid-state conformation of 70S ribosome. RNA 13:1473.
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.
Yang et al. (2010) A guaninine nucleotide exchange factor is a component of the meiotic spindle pole body in Schizosaccharomyces pombe. Mol. Biol. Cell. 21 (7):1272.
Chang et al. (2005) Nitric Oxide-dependent Allosteric Inhibitory Role of a Second Nucleotide Binding Site in Soluble Guanylyl Cyclase. J. Biol. Chem. 280 (12):11513.
Esters et al. (2001) High-resolution crystal structure of S. cerevisiae Ypt51 (Delta C15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis. J. Mol. Biol. 298 (1):111.
Tarricone et al. (2001) The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature 411 (6834):215.
Chook et al. (1999) Structure of the nuclear transport complex karyopherin-beta 2-Ran center dot GppNHp. Nature 399 (6733):230.
Rudolph et al. (1999) Nucleotide binding to the G12V-mutant of Cdc42 investigated by x-ray diffraction and fluorescence spectroscopy: Two different nucleotide states in one crystal. Protein Sci. 8 (4):778.
Vetter et al. (1999) Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398 (6722):39.
Hirshberg et al. (1997)The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat. Struct. Biol. 4 (2):147.
Rittinger et al. (1997) Structure at 1.65 angstrom of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389 (6652):758.
Rittinger et al. (1997) Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature 388 (6643):693.
Nassar et al. (1995) The 2.2-Angstrom crystal-structure of the ras-binding domain of the serine threonine kinase c-Raf1 in complex with Rap1a and a GTP analog. Nature 375 (6532):554.
Tolkovsky (1980) 2'-deoxyadenosine functionally uncouples adenylate-cyclase from the guanyl nucleotide subunit without altering simultaneous gppnhp occupancy. FEBS Lett. 116 (2):165.