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10220647001

Roche

GTP-γ-S

Tetralithium salt

Synonyme(s) :

GTP-γ-S, GTP

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About This Item

Code UNSPSC :
12352204

Description

C10H12N5O13P3SLi4

Niveau de qualité

Pureté

87% (HPLC)

Forme

solid

Poids mol.

Mr 539.2 (GTP-γ-S)
Mr 563.0 (GTP-γ-S-Li4)

Composition

GDP, ≤12% HPLC
GMP, ≤1% HPLC
GTP, ≤2% HPLC

Conditionnement

pkg of 10 mg

Fabricant/nom de marque

Roche

Conditions de stockage

protect from light

Concentration

97%

Technique(s)

activity assay: suitable

Couleur

white

Solubilité

water: soluble

Température de stockage

−20°C (−15°C to −25°C)

Description générale

Guanosine 5′-O-(3-thiotriphosphate), tetralithium salt (GTP-γ-S) is a non-hydrolysable analog of GTP. It is an inhibitor of phosphodiesterase in photoreceptors.

Application

GTP-γ-S has been used:
  • in G-Protein activation assay to assess the functionality of protease-activated receptor 4 (PAR4)
  • in fluorimetric guanine nucleotide exchange assay of G protein alpha subunits (Gα)
  • to monitor the Rac family small guanosine triphosphatase (GTPase) 2 (Rac2)-stimulated activity of phospholipase Cγ2 mutants

Actions biochimiques/physiologiques

Guanosine 5′-O-(3-thiotriphosphate) (GTP-γ-S) activates guanine-nucleotide-binding proteins and is slowly hydrolyzed enzymatically. It inhibits guanosine triphosphatase (GTPases) more potently than guanosine triphosphate (GTP),

Stockage et stabilité

Store powder dry at -15 to -25 °C; aqueous solutions with pH approx. 7 should be stable for six months at -15 to -25 °C.

Remarque sur l'analyse

Absorption: Content is measured in aqueous solution by absorption at 254 nm.
Conditions:
  • approx. 10 mg/ml double-dist. water
  • dilution: 9.8 ml double-dist. water + 0.2 ml sample.

Autres remarques

For life science research only. Not for use in diagnostic procedures.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

does not flash

Point d'éclair (°C)

does not flash


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Consulter la Bibliothèque de documents

Gilbert Di Paolo, Markus R. Wenk
Lipids, 3-18 (2012)
Stephen R Sprang
Biopolymers, 105(8), 449-462 (2016-03-22)
This review addresses the regulatory consequences of the binding of GTP to the alpha subunits (Gα) of heterotrimeric G proteins, the reaction mechanism of GTP hydrolysis catalyzed by Gα and the means by which GTPase activating proteins (GAPs) stimulate the
S Nawy et al.
Neuron, 7(4), 677-683 (1991-10-01)
Transmitter release from photoreceptors is decreased by light, resulting in a conductance increase in depolarizing bipolar cells. Addition of exogenous cGMP through a patch pipette to depolarizing bipolar cells from slices of dark-adapted tiger salamander retina resulted in an enhancement
K Sasaki et al.
Nature, 325(6101), 259-262 (1987-01-15)
Recently, a GTP-binding protein sensitive to islet activating protein (IAP) has been suggested to be important in producing K+-currents when the muscarinic receptor of the atrial muscle is activated by acetylcholine (ACh). Here we confirm the blocking effects of IAP
Baisen Zeng et al.
Structure (London, England : 1993), 27(7), 1137-1147 (2019-06-04)
Ric-8A is a 530-amino acid cytoplasmic molecular chaperone and guanine nucleotide exchange factor (GEF) for i, q, and 12/13 classes of heterortrimeric G protein alpha subunits (Gα). We report the 2.2-Å crystal structure of the Ric-8A Gα-binding domain with GEF

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