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D7409

2′,3′-Dideoxyguanosine 5′-triphosphate sodium salt

Name: 2′,3′-Dideoxyguanosine 5′-triphosphate sodium salt
Brand: SIGMA

≥90% (HPLC)

Synonyma:

ddGTP

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen

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About This Item

Empirický vzorec (Hillův zápis):

C₁₀H₁₆N₅O₁₂P₃

Číslo CAS:

68726-28-3

Molekulová hmotnost:

491.18

MDL number:

MFCD00079152

UNSPSC Code:

41106305

PubChem Substance ID:

24894133

NACRES:

NA.51

Doporučené produkty

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Sigma-Aldrich

D4788

2′-Deoxyadenosine 5′-triphosphate sodium salt solution

Sigma-Aldrich

A1653

Albumin from human serum

Sigma-Aldrich

A9511

Albumin from human serum

Sigma-Aldrich

01905

Adenosine 5′-diphosphate

Sigma-Aldrich

D4010

2′-Deoxyguanosine 5′-triphosphate sodium salt hydrate

Sigma-Aldrich

D6500

2′-Deoxyadenosine 5′-triphosphate disodium salt

Sigma-Aldrich

D6920

2′-Deoxyadenosine 5′-triphosphate sodium salt solution

Roche

DNTP-RO

Deoxynucleoside Triphosphate Set

Roche

PMSF-RO

PMSF

Roche

DATP-RO

dATP

Quality Level

100

assay

≥90% (HPLC)

form

powder

solubility

water: 5 mg/mL, clear, colorless

storage temp.

−20°C

SMILES string

[Na+].OP([O-])(=O)OP(O)(=O)OP(O)(=O)OC[C@@H]1CC[C@@H](O1)n2cnc3C(=O)NC(=N)Nc23

InChI

1S/C10H16N5O12P3.Na/c11-10-13-8-7(9(16)14-10)12-4-15(8)6-2-1-5(25-6)3-24-29(20,21)27-30(22,23)26-28(17,18)19;/h4-6H,1-3H2,(H,20,21)(H,22,23)(H2,17,18,19)(H3,11,13,14,16);/q;+1/p-1/t5-,6+;/m0./s1

InChI key

XCOBCPBPAINELA-RIHPBJNCSA-M

Gene Information

human ... HRAS(3265)

Application

2′,3′-Dideoxyguanosine 5′-triphosphate (ddGTP) is use as a chain terminator inhibitor and a inhibitor of telomerase(s).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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A simple in vitro RNA editing assay for chloroplast transcripts using fluorescent dideoxynucleotides: distinct types of sequence elements required for editing of ndh transcripts.

Tadamasa Sasaki et al.

The Plant journal : for cell and molecular biology, 47(5), 802-810 (2006-07-22)

RNA editing is found in various transcripts from land plant chloroplasts. In tobacco chloroplasts, C-to-U conversion occurs at 36 specific sites including two sites identified in this work. Our RNA editing assay system using chloroplast extracts facilitated biochemical analyses of

Resistance of HIV-1 reverse transcriptase against [2',5'-bis-O-(tert-butyldimethylsilyl)-3'-spiro-5''-(4''-amino-1'',2''- oxathiole-2'',2''-dioxide)] (TSAO) derivatives is determined by the mutation Glu138-->Lys on the p51 subunit.

H Jonckheere et al.

The Journal of biological chemistry, 269(41), 25255-25258 (1994-10-14)

Determination of the three-dimensional structure of the human immunodeficiency virus type-1 (HIV-1) reverse transcriptase (RT) has indicated a totally different folding for the 51-kDa subunit (p51) than for the 66-kDa subunit (p66). The polymerase catalytic site is located on the

Enzymatic properties and sensitivity to inhibitors of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase with Glu-138-->Arg and Tyr-188-->His mutations.

H Zhang et al.

Antiviral research, 24(1), 43-57 (1994-05-01)

Two mutants of HIV-1 reverse transcriptase (RT), Tyr-188-->His and Glu-138-->Arg have been prepared and their catalytic properties and sensitivities to inhibitors studied. As compared to wild type RT, a reduction in catalytic efficiency and turn over number was observed, especially

Mutational analysis of trp-229 of human immunodeficiency virus type 1 reverse transcriptase (RT) identifies this amino acid residue as a prime target for the rational design of new non-nucleoside RT inhibitors.

H Pelemans et al.

Molecular pharmacology, 57(5), 954-960 (2000-04-25)

Trp-229 is part of the non-nucleoside reverse transcriptase inhibitor (NNRTI)-binding pocket of HIV type 1 (HIV-1) reverse transcriptase (RT), and is also part of the "primer grip" of HIV-1 RT. Using site-directed mutagenesis, seven RT mutants were constructed bearing the

A two plasmid co-expression system in Escherichia coli for the production of virion-like reverse transcriptase of the human immunodeficiency virus type 1.

H Jonckheere et al.

Journal of virological methods, 61(1-2), 113-125 (1996-09-01)

Many bacterial expression systems have been developed to study the reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1). This enzyme exists in the virions as a heterodimer of a 66 kDa (p66) subunit and a 51 kDa (p51)

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Hlavní dokumenty

2′,3′-Dideoxyguanosine 5′-triphosphate sodium salt

≥90% (HPLC)

About This Item

Doporučené produkty

Vlastnosti

Quality Level

assay

form

solubility

storage temp.

SMILES string

InChI

InChI key

Gene Information

Popis

Application

Bezpečnostní informace

Storage Class

wgk_germany

flash_point_f

flash_point_c

ppe

Dokumentace

Osvědčení o analýze (COA)

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