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Merck

51060

Sigma-Aldrich

Guanosine 5′-diphosphate disodium salt

≥90% (HPLC)

Synonim(y):

5′-GDP-Na2

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About This Item

Wzór empiryczny (zapis Hilla):
C10H13N5Na2O11P2
Numer CAS:
Masa cząsteczkowa:
487.16
Numer WE:
Numer MDL:
Kod UNSPSC:
41106305
Identyfikator substancji w PubChem:
NACRES:
NA.51

pochodzenie biologiczne

Porcine brain
microbial (Corynebacterium sp)
synthetic

Próba

≥90% (HPLC)

Postać

powder

rozpuszczalność

H2O: 50 mg/mL, clear, colorless

Warunki transportu

dry ice

temp. przechowywania

−20°C

ciąg SMILES

[Na+].[Na+].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/C10H15N5O11P2.2Na/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;;/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18);;/q;2*+1/p-2/t3-,5-,6-,9-;;/m1../s1

Klucz InChI

LTZCGDIGAHOTKN-LGVAUZIVSA-L

Opis ogólny

Guanosine 5′-diphosphate (GDP) is a purine nucleotide and is interconvertible to guanosine by the action of ectonucleotidases and by nucleoside phosphorylase into guanine. GDP is majorly acted upon by 5′‐ectonucleotidases in neuronal cells.

Zastosowanie

Guanosine 5′-diphosphate (GDP) is used as a substrate of pyruvate kinase to produce GTP in support of RNA biosyntheis. GDP is used to study the kinetics and characteristics of GTPases such as those associated with G-protein coupled receptors (GPCR). GDP is also used to study cell signaling processes mediate by guanine nucleotide exchange factors.
Guanosine 5′-diphosphate disodium salt has been used:
  • in fluorescent metal nanoclusters selectivity of guanosine 3′-diphosphate-5′-di(tri)phosphate, ppGpp
  • in screening of fluorescence emission of hypocrellin A-zinc complex
  • as a component of assay buffers in the autoradiography of mice brain sections

Działania biochem./fizjol.

Guanosine based nucleosides play a key role in multiple cellular processes and generation growth factors. Elevated levels of guanosine 5′-diphosphate (GDP) is associated with the pathogenesis of neurological disorders. GDP is bound to G protein . G protein coupled receptors (GPCRs) activate G proteins by exchanging the bound GDP to GTP. GDP is potent inhibitor agent of hepcidin- ferroportin complex and may be effective for promoting erythropoiesis and treating anemia of inflammation(AI).
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Kod klasy składowania

11 - Combustible Solids

Klasa zagrożenia wodnego (WGK)

WGK 3

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable

Środki ochrony indywidualnej

Eyeshields, Gloves, type N95 (US)


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Michael P East et al.
Seminars in cell & developmental biology, 22(1), 3-9 (2010-07-20)
Arf GAPs (ADP-ribosylation factor GTPase-activating proteins) are essential components of Arf (ADP-ribosylation factor) signaling pathways. Arf GAPs stimulate the hydrolysis of GTP to GDP to transition Arf from the active, GTP bound, state to the inactive, GDP bound, state. Based
Alberto Fernández-Medarde et al.
Biochimica et biophysica acta, 1815(2), 170-188 (2010-11-30)
RasGrf1 and RasGrf2 are highly homologous mammalian guanine nucleotide exchange factors which are able to activate specific Ras or Rho GTPases. The RasGrf genes are preferentially expressed in the central nervous system, although specific expression of either locus may also
Highly selective detection of bacterial alarmone ppGpp with an off-on fluorescent probe of copper-mediated silver nanoclusters
Zhang P, et al.
Biosensors And Bioelectronics, 49, 433-437 (2013)
The guanylate-binding proteins: emerging insights into the biochemical properties and functions of this family of large interferon-induced guanosine triphosphatase.
Vestal DJ, Jeyaratnam JA.
Interferon Cytokine Res., 31, 89-97 (2011)
Identification of guanosine 5?-diphosphate as potential iron mobilizer: preventing the Hepcidin-Ferroportin interaction and modulating the interleukin-6/Stat-3 pathway
Angmo S, et al.
Scientific Reports, 7, 40097-40097 (2017)

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