G7252
Guanosine 5′-diphosphate tris salt from Saccharomyces cerevisiae
Type VI, ≥92.5%
Synonym(s):
GDP
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About This Item
Empirical Formula (Hill Notation):
C10H15N5O11P2
CAS Number:
Molecular Weight:
443.20
NACRES:
NA.51
PubChem Substance ID:
UNSPSC Code:
41106305
MDL number:
Assay:
≥92.5%
Storage temp.:
−20°C
type
Type VI
Quality Level
assay
≥92.5%
shipped in
dry ice
storage temp.
−20°C
SMILES string
NC(CO)(CO)CO.NC1=Nc2c(ncn2[C@@H]3O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]3O)C(=O)N1
InChI
1S/C10H15N5O11P2.C4H11NO3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21;5-4(1-6,2-7)3-8/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18);6-8H,1-3,5H2/t3-,5-,6-,9-;/m1./s1
InChI key
YWMHXINREUQYRO-GWTDSMLYSA-N
Biochem/physiol Actions
Guanosine 5′-diphosphate (GDP) is the diphosphate nucleoside of the purine guanine. GDP and GTP are involved in and may be used to study cell signaling via G-coupled protein receptors (GCPR) and guanine nucleotide exchange factors (GEF) and a variety of GTPases.
Storage Class
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Nicola M Martucci et al.
Biochimie, 94(2), 503-509 (2011-09-20)
The effect of pulvomycin on the biochemical and fluorescence spectroscopic properties of the archaeal elongation factor 1α from Sulfolobus solfataricus (SsEF-1α), the functional analog of eubacterial EF-Tu, was investigated. The antibiotic was able to reduce in vitro the rate of protein
Antonio Castro-Castro et al.
The EMBO journal, 30(19), 3913-3927 (2011-08-30)
The activation of the Rac1 GTPase during cell signalling entails its translocation from the cytosol to membranes, release from sequestering Rho GDP dissociation inhibitors (RhoGDI), and GDP/GTP exchange. In addition to those steps, we show here that optimal Rac1 activation
Jason Lowery et al.
The Journal of biological chemistry, 286(42), 36898-36906 (2011-08-11)
ADP-ribosylation factors (ARFs) and their activating guanine nucleotide exchange factors (GEFs) play key roles in membrane traffic and signaling. All ARF GEFs share a ∼200-residue Sec7 domain (Sec7d) that alone catalyzes the GDP to GTP exchange that activates ARF. We