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114666

Sigma-Aldrich

Actinomycin D, Streptomyces sp.

Anti-neoplastic antibiotic. Inhibits DNA-primed RNA polymerase by complexing with DNA via deoxyguanosine residues.

Synonyme(s) :

Actinomycin D, Streptomyces sp., Dactinomycin, RNA Polymerase I Inhibitor I, Pol I Inhibitor I

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About This Item

Formule empirique (notation de Hill) :
C62H86N12O16
Numéro CAS:
50-76-0
Poids moléculaire :
1255.42
Numéro MDL:
MFCD00005033
Code UNSPSC :
12352200

Niveau de qualité

100

Essai

≥98% (HPLC)

Forme

crystalline solid

Fabricant/nom de marque

Calbiochem®

Conditions de stockage

OK to freeze
desiccated (hygroscopic)
protect from light

Couleur

red

Solubilité

DMSO: 1 mg/mL
chloroform: soluble
methanol: soluble

Conditions d'expédition

ambient

Température de stockage

2-8°C

InChI

1S/C62H86N12O16/c1-27(2)42-59(84)73-23-17-19-36(73)57(82)69(13)25-38(75)71(15)48(29(5)6)61(86)88-33(11)44(55(80)65-42)67-53(78)35-22-21-31(9)51-46(35)64-47-40(41(63)50(77)32(10)52(47)90-51)54(79)68-45-34(12)89-62(87)49(30(7)8)72(16)39(76)26-70(14)58(83)37-20-18-24-74(37)60(85)43(28(3)4)66-56(45)81/h21-22,27-30,33-34,36-37,42-45,48-49H,17-20,23-26,63H2,1-16H3,(H,65,80)(H,66,81)(H,67,78)(H,68,79)

Clé InChI

RJURFGZVJUQBHK-UHFFFAOYSA-N

Description générale

Anti-neoplastic antibiotic. Inhibits DNA-primed RNA polymerase by complexing with DNA via deoxyguanosine residues. At higher concentrations, DNA polymerase is inhibited. Also acts as a competitive inhibitor of serine proteases. Inhibits cell growth and colony formation in synchronized HeLa cells. Induces apoptosis in many cell lines. However, actinomycin D has also been shown to suppress etoposide-induced apoptosis in PC12 cells. Note: 1 set = 20 x 200 µg.
Antineoplastic antibiotic. Inhibits DNA-primed RNA polymerase by complexing with DNA via deoxyguanosine residues. A DNA-intercalator with growth inhibitory activity against certain leukemias and sarcomas. At higher concentrations, DNA polymerase is inhibited. Inhibits cell growth and colony formation in synchronized HeLa cells. A potent inducer of apoptosis in many cell lines; however, actinomycin D has also been shown to suppress programmed cell death of PC12 cells induced by etoposide, an inhibitor of topoisomerase II. Acts as a competitive inhibitor of serine protease from microorganisms. The growth of S. aureus is inhibited by 0.25-0.75 µg/ml, whereas a concentration of 100 µg/ml is required to inhibit E. coli due to permeability differences. Heat resistant and stable between pH 2 and 11; decomposed by strong acids and bases. λmax 441 nm ±2 nm. Note: 1 set = 20 vials x 200 µg.
Stability: heat resistant and stable between pH 2 and 11. Decomposed by strong acids and bases.

Actions biochimiques/physiologiques

Primary Target
serine proteases
Secondary Target
cell growth and colony formation in synchronized HeLa cells

Avertissement

Toxicity: Highly Toxic & Carcinogenic / Teratogenic (I)

Reconstitution

Following reconstitution, aliquot and freeze (-20°C) for long term storage or refrigerate (4°C) for short term storage. Stock solutions are stable for up to 3 months at -20°C.

Autres remarques

Due to the nature of the Hazardous Materials in this shipment, additional shipping charges may be applied to your order. Certain sizes may be exempt from the additional hazardous materials shipping charges. Please contact your local sales office for more information regarding these charges.
Nakajima, M., et al. 1994. Neurosci. Lett.176, 161.
Wu, M.H., and Yung, B.Y. 1994. Eur. J. Pharmacol. 270, 203.
Betzel, C., et al. 1993. Biochim. Biophys. Acta 1161, 47.
Yung, B.Y., et al. 1992. Int. J. Cancer52, 317.
Martin, S.J., et al. 1990. J. Immunol.145, 1859.
Yung, B.Y., et al. 1990. Cancer Res.50, 5987.
White, R.J., and Phillips, D.R. 1985. Biochemistry27, 9122.
Madharavao, M., et al. 1978. J. Med. Chem.21, 958.
Sengupta, S.K., et al. 1975. J. Med. Chem.18, 1175.

Informations légales

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Pictogrammes

Skull and crossbonesHealth hazard
GHS06,GHS08

Mention d'avertissement

Danger

Mentions de danger

H300,H350,H360FD

Classification des risques

Acute Tox. 2 Oral - Carc. 1B - Repr. 1B

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

Certificats d'analyse (COA)

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Azam Asgarihafshejani et al.
iScience, 25(5), 104259-104259 (2022-05-07)
Hippocampal somatostatin (SOM) cells are dendrite-projecting inhibitory interneurons. CA1 SOM cells receive major excitatory inputs from pyramidal cells (PC-SOM synapses) which show mGluR1a- and mTORC1-mediated long-term potentiation (LTP). PC-SOM synapse LTP contributes to CA1 network metaplasticity and memory consolidation, but
Viana Manrique-Suárez et al.
Proteins, 89(11), 1508-1521 (2021-07-06)
Tumor necrosis factor-alpha (TNFα) inhibitors could prevent neurological disorders systemically, but their design generally relies on molecules unable to cross the blood-brain barrier (BBB). This research was aimed to design and characterize a novel TNFα inhibitor based on the angiopeptide-2
Victor L Bass et al.
Molecular systems biology, 17(7), e10127-e10127 (2021-07-22)
Cell-to-cell heterogeneity is a feature of the tumor necrosis factor (TNF)-stimulated inflammatory response mediated by the transcription factor NF-κB, motivating an exploration of the underlying sources of this noise. Here, we combined single-transcript measurements with computational models to study transcriptional
Edward J Morris et al.
Cell reports, 30(11), 3605-3615 (2020-03-19)
Multiple cancer-related genes both promote and paradoxically suppress growth initiation, depending on the cell context. We discover an explanation for how this occurs for one such protein, Stat3, based on asymmetric cell division. Here, we show that Stat3, by Stathmin/PLK-1
Janaki N Sudhakar et al.
Biology of the cell, 106(10), 359-376 (2014-07-25)
During the initiation of cell death, mitochondrial protein, apoptosis-inducing factor (AIF), is transported to the nucleus. The mechanism of AIF nuclear translocation, however, is not clear. After protein synthesis, the AIF is originally targetted to the mitochondria, and the nuclear

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