Guanosine 5'-triphosphate, Sodium salt
For in vitro 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: C10H16N5O14P3 (free acid)
Molecular Weight: 523.18 g/mol (free acid)
Purity: > 99 % (HPLC)
Form: clear aqueous solution, pH 8.0 ±0.2 (4 °C)
Concentration: 100 mM ±2 %
pH: 8.0 ±0.2
Spectroscopic Properties: λmax 252 nm; ε 14.2 L mmol-1 cm-1 (Tris-HCl pH 7.0)
Assembly of ribosomal units
Microdomain formation by small GTPases
Antiviral activity of large GTPases (dynamin superfamily)
Regulation of exocytosis by Rho GTPases
Mechanism of hydrolysis by ADP-ribosylation factors
Ultrapure GTP supplied as clear aqueous solution (pH 8.0).
Guanylate binding proteins
Quality Control Specifications: in vitro transcription: suitable; contamination with bacterial and human DNA: not detectable; activity of DNase, Protease or Phosphatase: not detectable
 Blombach et al. (2011) Assembling the archeal ribosome: roles for transition factor-related GTPases. Biochemical Society Transactions 39:45.
 Stuermer (2011) Microdomain-forming proteins and the role of the reggies/flottilins during axon regeneration in zebrafish. Biochimica Biophysica Acta, Molecular Basis of Disease 1812:415.
 Haller et al. (2011) Human MxA protein: An Interferon-induced Dynamin-like GTPase with broad antiviral activity. J. Interferon and Cytokine Research 31:79.
 Stephane et al. (2011) Rho GTPases and exocytosis: what are the molecular links? Seminars in Cell and Developmental Biology 22:27.
 East et al. (2011) Models for the function of Arf GAPs. Seminars in Cell and Developmentan Biology 22:3.
 Vestal et al. (2011) The guanylate binding proteins: Emerging insights into the biochemical properties and functions of this family of large interferon-induced guanosine triphosphatase. J. Interferon and Cytokine Research 31:89.
 Younghoon et al. (2011) Septin structure and function in yeast and beyond. Trends in Cell Biology 21:141.
Drummond et al. (2011) Reconstitution and Organization of Escherichia coli Proto-ring Elements (FtsZ and FtsA) inside Giant Unilamellar Vesicles Obtained from Bacterial Inner Membranes. Methods Mol. Biol. 777 :29.
Katsuki et al. (2011) Preparation of dual-color polarity-marked fluorescent microtubule seeds. Methods Mol. Biol. 777:117.
Ramachandran et al. (2009) Membrane Insertion of the Pleckstrin Homology Domain Variable Loop 1 Is Critical for Dynamin-catalyzed Vesicle Scission. Molecular Biology of the Cell 20 (22):4630.