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Merck
CN

21376

(S)-(+)-喜树碱

≥90% (sum of enantiomers, HPLC)

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经验公式(希尔记法):
C20H16N2O4
化学文摘社编号:
分子量:
348.35
UNSPSC Code:
12352200
Beilstein/REAXYS Number:
631069
MDL number:
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assay

≥90% (sum of enantiomers, HPLC)

mp

260 °C (dec.) (lit.)

mode of action

DNA synthesis | interferes, enzyme | inhibits

SMILES string

CC[C@@]1(O)C(=O)OCC2=C1C=C3N(Cc4cc5ccccc5nc34)C2=O

InChI

1S/C20H16N2O4/c1-2-20(25)14-8-16-17-12(7-11-5-3-4-6-15(11)21-17)9-22(16)18(23)13(14)10-26-19(20)24/h3-8,25H,2,9-10H2,1H3/t20-/m0/s1

InChI key

VSJKWCGYPAHWDS-FQEVSTJZSA-N

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Other Notes

Eukaryotic DNA topoisomerase I poison. Used to study the interaction of topo I with DNA; DNA topoisomerases, review

pictograms

Skull and crossbonesHealth hazard

signalword

Danger

hcodes

Hazard Classifications

Acute Tox. 3 Oral - Muta. 1B

存储类别

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges

法规信息

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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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M.-A. Bjornsti
Current Opinion in Structural Biology, 1, 99-99 (1991)
S E Porter et al.
Nucleic acids research, 17(21), 8521-8532 (1989-11-11)
The eukaryotic topoisomerase I (topo I) is the target of the cytotoxic alkaloid camptothecin (CTT). In vitro, CTT enhances the breakage of DNA by topo I when the reaction is stopped with detergent. Although breakage at some sites is enhanced
DNA topoisomerase poisons as antitumor drugs.
L F Liu
Annual review of biochemistry, 58, 351-375 (1989-01-01)
Carmen Losasso et al.
Nucleic acids research, 36(17), 5635-5644 (2008-09-06)
Human DNA topoisomerase I (hTop1p) catalyzes the relaxation of supercoiled DNA and constitutes the cellular target of the antitumor drug camptothecin (CPT). The X-ray crystal structure of the enzyme covalently joined to DNA and bound to the CPT analog Topotecan
Andrea K McCollum et al.
Molecular cancer therapeutics, 7(10), 3256-3264 (2008-10-15)
Benzoquinone ansamycin antibiotics such as geldanamycin (GA) bind to the NH(2)-terminal ATP-binding domain of heat shock protein (Hsp) 90 and inhibit its chaperone functions. Despite in vitro and in vivo studies indicating promising antitumor activity, derivatives of GA, including 17-allylaminogeldanamycin

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