D6920
2′-Deoxyadenosine 5′-triphosphate sodium salt solution
10 mM
Synonyme(s) :
dATP
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A propos de cet article
NACRES:
NA.52
UNSPSC Code:
41106305
EC Number:
217-662-3
Assay:
≥99%
Form:
liquid
Storage temp.:
−20°C
Service technique
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≥99%
Quality Level
form
liquid
concentration
10 mM
technique(s)
PCR: suitable
color
colorless
foreign activity
DNase, RNase, NICKase, none detected
shipped in
dry ice
storage temp.
−20°C
SMILES string
[Na+].Nc1ncnc2n(cnc12)[C@H]3C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)([O-])=O)O3
InChI
1S/C10H16N5O12P3.Na/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19;/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19);/q;+1/p-1/t5-,6+,7+;/m0./s1
InChI key
YJWCICGGRLOGEH-VWZUFWLJSA-M
General description
2′-Deoxyadenosine 5′-triphosphate (dATP) is made up of a nucleobase attached to deoxyribose and a 5′-hydroxyl on the sugar bound to a chain of three phosphate residues. dATP is used by cells for synthesis of DNA by DNA polymerases.
Application
2′-Deoxyadenosine 5′-triphosphate sodium salt solution has been used as a component of the dNTP mix for labelling of ribosomal 18s rDNA probe and telomeric (TTAGG)n probe.
2′-Deoxyadenosine 5′-triphosphate sodium salt solution is used in DNA sysnthesis reactions such as PCR, DNA sequencing and molecular cloning techniques.
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
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Contenu apparenté
Spittlebugs (Hemiptera)
Kuznetsova V G, et al.
Protocols for Cytogenetic Mapping of Arthropod Genomes., 351-380 (2015)
U C Halder et al.
Cell death & disease, 2, e197-e197 (2011-09-02)
During early infection, viruses activate cellular stress-response proteins such as heat-shock proteins (Hsps) to counteract apoptosis, but later on, they modulate these proteins to stimulate apoptosis for efficient viral dissemination. Hsp70 has been attributed to modulate viral entry, transcription, nuclear
Serdal Kirmizialtin et al.
Structure (London, England : 1993), 20(4), 618-627 (2012-04-10)
Nearly every enzyme undergoes a significant change in structure after binding it's substrate. Experimental and theoretical analyses of the role of changes in HIV reverse transcriptase structure in selecting a correct substrate are presented. Atomically detailed simulations using the Milestoning