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P4512

Sigma-Aldrich

Puromycin

liquid, suitable for cell culture, BioReagent

Sinónimos:

Achromycin, PDH, Stillomycin, Stylomycin

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10 X 1 ML
$204.00

$204.00


Disponible para envío el09 de abril de 2025Detalles


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10 X 1 ML
$204.00

About This Item

Código UNSPSC:
12352207
NACRES:
NA.76

$204.00


Disponible para envío el09 de abril de 2025Detalles


Solicitar un pedido a granel

Nombre del producto

Puromycin ready made solution, 10 mg/mL in H2O, ≥98% (HPLC), Cell culture tested

Nivel de calidad

Ensayo

≥98% (HPLC)

Formulario

liquid

concentración

10 mg/mL in H2O

temp. de almacenamiento

2-8°C

Descripción general

Puromycin is an aminonucleoside antibiotic naturally produced by Streptomyces alboniger as a tyrosyl tRNA analog. It inhibits ribosomal protein synthesis process by causing premature chain termination acting as an analog of the 3′-terminal end of the aminoacyl-tRNA. Puromycin also acts as a reversible inhibitor of dipeptidyl-peptidase II (serine peptidase) and cytosol alanyl aminopeptidase (100μM, IC50=0.6μM). Puromycin is used as a selection marker gene (puromycin-N-acetyltransferase gene, pac) in eukaryotic/mammalian cells.
Puromycin has a wide variety of biological activities with inhibitory effect against bacteria, protozoa, parasitic worms, algae, plants, and mammalian cells.
Puromycin shows broad spectrum activity, particularly strong activity against gram positive microorganisms but weak activity against acid-fast bacilli and even weaker activity against gram negative microorganisms.
Puromycin has anti-cancer properties, inducing apoptosis in breast cancer cells. It has been shown that Puromycin induces apoptosis in MCF-7 breast cancer cells using an immunological assay to study apoptosis (the modulating effect of insulin-like growth factor-1 (IGF-1)). Puromycin at 0.5 microg/ml induced a high level of apoptosis in MCF-7 breast cancer cells, although there was still a non-negligible amount of synthesized protein. The activity of Puromycin was compared to 2 other protein synthesis inhibitors (cycloheximide and emetine), in which apoptosis occurred when protein synthesis was almost completely blocked.
Puromycin also showed antitumor activity in MDA-MB-231 breast cancer cells, causing suppression of 45S pre-ribosomal RNA and upstream binding factor (UBF).
Furthermore, Puromycin was used to study the vascular smooth muscle cell viability after treatment in rabbit model.

Technical information
The suggested concentration of Puromycin in cell culture assays is 0.2-10-μg/mL. Therefore, it is recommended to dilute the ready made solution 1:1000-50,000.

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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J A Vara et al.
Nucleic acids research, 14(11), 4617-4624 (1986-06-11)
The gene encoding a puromycin N-acetyl transferase from Streptomyces alboniger has been cloned next to the SV40 early promoter in a mammalian cells-Escherichia coli shuttle vector. When this construction was introduced into VERO cells it expressed the relevant enzymic activity.
Y Yamamoto et al.
Forensic science international, 113(1-3), 143-146 (2000-09-09)
A cytosolic alanyl aminopeptidase (AAP-S) was purified to homogeneity from human liver cytosol. The molecular weight of the purified enzyme was calculated to be approximately 98,000 on TOF-MS and 90,000 on SDS-PAGE in the presence of beta-ME. These findings suggest
Inhibitors of protein biosynthesis.
D Vázquez
Molecular biology, biochemistry, and biophysics, 30, i-x (1979-01-01)
Masaaki Iwamoto et al.
Gene, 534(2), 249-255 (2013-11-05)
A puromycin-N-acetyltransferase gene (pac) is widely used as a selection marker for eukaryotic gene manipulation. However, it has never been utilized for molecular studies in the ciliate Tetrahymena thermophila, in spite of the limited number of selection markers available for
R Giegé et al.
Current opinion in structural biology, 8(3), 286-293 (1998-07-17)
Mimics recapitulating the structural features of tRNAs are involved in biological processes other than ribosome-dependent protein synthesis. A knowledge of the rules underlying the architecture and function of tRNAs allows the design of non-natural mimics. The study of these mimics

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