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Merck

G3776

Guanosine 5′-triphosphate sodium salt solution

HPLC purified, aqueous solution for RNA polymerase transcription

Synonym(s):

GTP

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25 μMOL

€ 287,00

€ 287,00


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About This Item

CAS Number:
NACRES:
NA.52
PubChem Substance ID:
UNSPSC Code:
41106305
MDL number:
Assay:
≥95% (HPLC)
Biological source:
Porcine brain, bacterial (Corynebacterium), yeast
Form:
liquid
Storage temp.:
−20°C

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InChI

1S/C10H16N5O14P3.3Na/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21;;;/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18);;;/q;3*+1/p-3/t3-,5-,6-,9-;;;/m1.../s1

SMILES string

[Na+].[Na+].[Na+].NC1=Nc2c(ncn2[C@@H]3O[C@H](COP(O)(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]3O)C(=O)N1

InChI key

KZRMTEVIDYXWQW-CYCLDIHTSA-K

biological source

Porcine brain, bacterial (Corynebacterium), yeast

assay

≥95% (HPLC)

form

liquid

Quality Level

Gene Information

human ... HRAS(3265)

feature

PCR Additives

concentration

100 mM in H2O (adjusted to pH 7)

technique(s)

PCR: suitable

color

colorless

foreign activity

DNase, RNase and Nickase, none detected

shipped in

dry ice

storage temp.

−20°C

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Show Differences

1 of 4

This Item
U1006D5038D7170
biological source

Porcine brain, yeast, bacterial (Corynebacterium)

biological source

yeast (Candida Utilis)

biological source

-

biological source

-

Quality Level

300

Quality Level

300

Quality Level

200

Quality Level

200

form

liquid

form

liquid

form

liquid

form

liquid

assay

≥95% (HPLC)

assay

≥95 (HPLC)

assay

≥99%

assay

≥99%

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

concentration

100 mM in H2O (adjusted to pH 7)

concentration

100 mM in H2O (adjusted to pH 7 with Trizma®
base)

concentration

100 mM (pH 7)

concentration

10 mM in H2O

Application

Guanosine 5′-triphosphate sodium salt solution has been used:

  • for reconstituting transducin during purification of transducin.[1]
  • as a compnent of the 3.3X loading buffer to assemble 32P-miR-31—3xFLAG-AGO2 complexes[2]
  • as a component of the nucleotide substrate mix to evaluate the hydrolytic activity of MutT homolog 1 (MTH1) on methylated nucleoside triphosphates[3]
  • in DNA-dependent RNA polymerase transcription

Biochem/physiol Actions

Guanosine 5′-triphosphate (GTP) forms nearly 25% of the total nucleotide triphosphate pool and is a nucleotide anion.[4] It participates in several biological functions such as cell signaling by activation of GTP-binding proteins, RNA and protein synthesis[4], and production of cyclic guanosine monophosphate (cGMP), a secondary messenger. GTP also participates in the production of stringent alarmone.[4]

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type N95 (US)


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Reyad A Elbarbary et al.
Methods (San Diego, Calif.), 152, 18-22 (2018-05-20)
MicroRNAs (miRNAs) comprise a class of small non-coding RNAs that regulate the stability and/or translatability of most protein-coding transcripts. Steady-state levels of mature miRNAs can be controlled through mechanisms that influence their biogenesis and/or decay rates. Pathways that mediate mature
Giselle Cerchiaro et al.
Redox report : communications in free radical research, 14(2), 82-92 (2009-04-25)
Levels of oxidized guanosine base in DNA have become a hallmark biomarker in assessing oxidative stress implicated in a variety of disease and toxin-induced states. However, there is evidence that the guanosine in the nucleotide triphosphate pool (GTP) is more
In vitro biochemical assays to monitor rhodopsin function.
Sammons J and Gross AK
Methods in Molecular Biology, 884, 167-181 (2012)
Water-soluble luminescent copper nanoclusters reduced and protected by histidine for sensing of guanosine 5'-triphosphate
Zhao X J and Huang, C Z
New. J. Chem., 38(8), 3673-3677 (2014)
A L Menon et al.
Journal of bacteriology, 176(2), 291-295 (1994-01-01)
H2 oxidation in Azotobacter vinelandii is catalyzed by a membrane-bound, alpha beta dimeric [NiFe] hydrogenase. Maturation of the enzyme involves cleavage of a putative N-terminal signal sequence in the beta subunit and removal of 15 amino acids from the C

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