400090
IC261
A cell-permeable, reversible, potent and selective inhibitor of casein kinase (CK1) that inhibits CK1δ (IC₅₀ = 0.7-1.3 µM) and CK1ε (IC₅₀ = 0.6-1.4 µM) isozymes.
Sinónimos:
IC261, 3-[(2,4,6-Trimethoxyphenyl)methylidenyl]-indolin-2-one, SU5607, Casein Kinase I Inhibitor VI
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About This Item
Fórmula empírica (notación de Hill):
C18H17NO4
Número de CAS:
Peso molecular:
311.33
Número MDL:
Código UNSPSC:
12352200
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Nivel de calidad
Ensayo
≥95% (sum of two isomers, HPLC)
Formulario
solid
fabricante / nombre comercial
Calbiochem®
condiciones de almacenamiento
OK to freeze
protect from light
color
yellow
solubilidad
DMSO: 100 mg/mL
Condiciones de envío
ambient
temp. de almacenamiento
−20°C
Descripción general
A cell-permeable, reversible, potent and selective inhibitor of Casein Kinase (CK1) that inhibits the CK1δ (IC50 = 0.7-1.3 µM) and CK1ε (IC50 = 0.6-1.4 µM) isozymes. Also inhibits CK1α1 at much higher concentrations (IC50 = 11-21 µM). The inhibition is competitive with respect to ATP. Has only a trivial effect on p34cdc2 and p55fyn (IC50s >100 µM). Blocks the phosphorylation of p53 by CK1δ and CK1ε, thereby modulating p53′s effect on the cell cycle. At low micromolar concentrations, IC261 inhibits cytokinesis causing a transient mitotic arrest.
A cell-permeable, reversible, potent and selective inhibitor of casein kinase (CK1) that inhibits CK1δ (IC50 = 0.7-1.3 µM) and CK1ε (IC50 = 0.6-1.4 µM) isozymes. Also inhibits CK1α1 at much higher concentrations (IC50 = 11-21 µM). The inhibition is competitive with respect to ATP. Only weakly inhibits PKA, p34cdc2, and p55fyn (IC50s >100 µM). At low micromolar concentrations, IC261 inhibits cytokinesis causing a transient mitotic arrest.
Acciones bioquímicas o fisiológicas
Cell permeable: yes
Primary Target
CK1δ
CK1δ
Product competes with ATP.
Reversible: yes
Target IC50: 0.7-1.3 µM, 0.6-1.4 µM, against CK1δ and CK1ε isozymes, respectively
Envase
Packaged under inert gas
Advertencia
Toxicity: Standard Handling (A)
Reconstitución
Following reconstitution, aliquot, purge with inert gas, and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C when stored under an inert gas.
Otras notas
Behrend, L., et al. 2000. Oncogene19, 5303.
Mashhoon, N., et al. 2000. J. Biol. Chem.275, 20052.
Knippschild, U., et al. 1997. Oncogene15, 1727.
Mashhoon, N., et al. 2000. J. Biol. Chem.275, 20052.
Knippschild, U., et al. 1997. Oncogene15, 1727.
Información legal
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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L Behrend et al.
Oncogene, 19(47), 5303-5313 (2000-12-05)
The p53-targeted kinases casein kinase 1delta (CK1delta) and casein kinase 1epsilon (CK1epsilon) have been proposed to be involved in regulating DNA repair and chromosomal segregation. Recently, we showed that CK1delta localizes to the spindle apparatus and the centrosomes in cells
U Knippschild et al.
Oncogene, 15(14), 1727-1736 (1998-02-12)
The p53 tumour suppressor protein plays a key role in the integration of stress signals. Multi-site phosphorylation of p53 may play an integral part in the transmission of these signals and is catalysed by many different protein kinases including an
Qiwei Jiang et al.
Molecular cancer, 20(1), 100-100 (2021-08-07)
3-phosphoinositide-dependent protein kinase-1 (PDK1) acts as a master kinase of protein kinase A, G, and C family (AGC) kinase to predominantly govern cell survival, proliferation, and metabolic homeostasis. Although the regulations to PDK1 downstream substrates such as protein kinase B
N Mashhoon et al.
The Journal of biological chemistry, 275(26), 20052-20060 (2000-04-06)
Members of the casein kinase-1 family of protein kinases play an essential role in cell regulation and disease pathogenesis. Unlike most protein kinases, they appear to function as constitutively active enzymes. As a result, selective pharmacological inhibitors can play an
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