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Key Documents

A5156

Sigma-Aldrich

Actinomycin D–Mannitol

lyophilized powder

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About This Item

Numéro MDL:
Code UNSPSC :
51102829
ID de substance PubChem :
Nomenclature NACRES :
NA.85

Source biologique

Streptomyces sp.

Niveau de qualité

Forme

lyophilized powder

Couleur

yellow to orange

Solubilité

H2O: 20 mg/mL

Spectre d'activité de l'antibiotique

neoplastics

Mode d’action

DNA synthesis | interferes

Température de stockage

2-8°C

Chaîne SMILES 

OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO.CC(C)[C@H]1NC(=O)[C@@H](NC(=O)c2ccc(C)c3OC4=CC(=O)C(N)=C(C(=O)N[C@H]5[C@@H](C)OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]6CCCN6C(=O)[C@H](NC5=O)C(C)C)C4=Nc23)[C@@H](C)OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]7CCCN7C1=O

InChI

1S/C61H84N12O16.C6H14O6/c1-27(2)43-58(83)72-22-16-18-35(72)56(81)68(12)25-39(75)70(14)49(29(5)6)60(85)87-32(10)45(54(79)64-43)66-52(77)34-21-20-31(9)51-47(34)63-48-38(89-51)24-37(74)42(62)41(48)53(78)67-46-33(11)88-61(86)50(30(7)8)71(15)40(76)26-69(13)57(82)36-19-17-23-73(36)59(84)44(28(3)4)65-55(46)80;7-1-3(9)5(11)6(12)4(10)2-8/h20-21,24,27-30,32-33,35-36,43-46,49-50H,16-19,22-23,25-26,62H2,1-15H3,(H,64,79)(H,65,80)(H,66,77)(H,67,78);3-12H,1-2H2/t32-,33-,35+,36+,43-,44-,45+,46+,49+,50+;3-,4-,5-,6-/m11/s1

Clé InChI

AURFRHZIDSMTRK-CSXPNASWSA-N

Description générale

Chemical structure: peptide

Application

Actinomycin D is used as a selection agent and is used in banding techniques to differentiate between different regions of chromosomes. Actinomycin induces apoptosis and is used as a potent antitumor agent .

Actions biochimiques/physiologiques

An antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces apoptosis. Potent antitumor agent. For cell culture applications, actinomycin D is used as a selection agent and in banding techniques to differentiate between different regions of chromosomes.
Actinomycin D is an antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces apoptosis. Potent antitumor agent.
An antineoplastic antibiotic that inhibits cell proliferation by forming a stable complex with DNA and blocking the movement of RNA polymerase which interferes with DNA-dependent RNA synthesis. Induces apoptosis. Potent antitumor agent. For cell culture applications, actinomycin D is used as a selection agent and is used in banding techniques to differentiate between different regions of chromosomes.

Composants

1 mg actinomycin D and 49 mg mannitol per vial

Autres remarques

The powder is hygroscopic and sensitive to light.

Pictogrammes

Skull and crossbonesHealth hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Acute Tox. 2 Oral - Carc. 2 - Resp. Sens. 1

Code de la classe de stockage

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges


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Les clients ont également consulté

G S Ridge et al.
Nucleic acids research, 22(24), 5241-5246 (1994-12-11)
The antitumour antibiotic actinomycin D normally binds to DNA by intercalation at sequences containing the CpG step, but in the presence of daunomycin it has been reported to interact with poly(dA-dT). This observation has neither been confirmed nor explained. Here
Haishan Xu et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 16(17), 4392-4400 (2010-08-25)
ABT-737, which blocks the function of Bcl-2 and Bcl-X(L) but not Mcl-1, has shown single-agent activity in preclinical models of small cell lung cancer (SCLC). Elevated expression of Mcl-1 induces resistance to ABT-737 in SCLC. Based on the short half-life
Louis-Marie Bloyet et al.
Journal of virology, 94(13) (2020-04-24)
Nonsegmented negative-strand (NNS) RNA viruses possess a ribonucleoprotein template in which the genomic RNA is sequestered within a homopolymer of nucleocapsid protein (N). The viral RNA-dependent RNA polymerase (RdRP) resides within an approximately 250-kDa large protein (L), along with unconventional
William J Neidermyer et al.
PLoS pathogens, 15(6), e1007875-e1007875 (2019-06-22)
Infection of mammalian cells with vesicular stomatitis virus (VSV) results in the inhibition of cellular translation while viral translation proceeds efficiently. VSV RNA synthesis occurs entirely within the cytoplasm, where during transcription the viral polymerase produces 5 mRNAs that are

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