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422708

Sigma-Aldrich

KN-93

≥95% (HPLC), solid, CAM kinase II inhibitor, Calbiochem®

Sinónimos:

2-[N-(2-hydroxyethyl)]-N-(4-methoxybenzenesulfonyl)]amino-N-(4-chlorocinnamyl)-N-methylbenzylamine)

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About This Item

Fórmula empírica (notación de Hill):
C26H29ClN2O4S
Número de CAS:
139298-40-1
Peso molecular:
501.04
Número MDL:
MFCD03788201
Código UNSPSC:
12352200
NACRES:
NA.77

Nombre del producto

KN-93, A cell-permeable, reversible and competitive inhibitor of rat brain CaM kinase II (Ki = 370 nM).

Nivel de calidad

100

Ensayo

≥95% (HPLC)

Formulario

solid

fabricante / nombre comercial

Calbiochem®

condiciones de almacenamiento

OK to freeze
protect from light

color

off-white

solubilidad

DMSO: 5 mg/mL

Condiciones de envío

ambient

temp. de almacenamiento

2-8°C

cadena SMILES

[S](=O)(=O)(N(CCO)c2c(cccc2)CN(C\C=C\c3ccc(cc3)Cl)C)c1ccc(cc1)OC

InChI

1S/C26H29ClN2O4S/c1-28(17-5-6-21-9-11-23(27)12-10-21)20-22-7-3-4-8-26(22)29(18-19-30)34(31,32)25-15-13-24(33-2)14-16-25/h3-16,30H,17-20H2,1-2H3/b6-5+

Clave InChI

LLLQTDSSHZREGW-AATRIKPKSA-N

Descripción general

A cell-permeable, reversible and competitive inhibitor of rat brain CaM kinase II (Ki = 370 nM). Selectively binds to the CaM binding site of the enzyme and prevents the association of CaM with CaMKII. Has no significant effects on protein kinase A activity. Induces G1 cell cycle arrest and apoptosis in NIH/3T3 cells. A 5 mM (1 mg/399 µl) solution of KN-93 (Cat. No. 422712) in DMSO is also available.
Cell-permeable, reversible, and competitive inhibitor of rat brain Ca+2/calmodulin-dependent protein kinase II (Ki = 370 nM). KN-93 selectively binds to the Calmodulin (CaM) binding site of the enzyme and prevents the association of CaM with CaM Kinase II. Selectively binds to the CaM binding site of the enzyme and prevents the association of CaM with CaMKII. Has no significant effect on protein kinase A activity. Induces G1 cell cycle arrest and apoptosis in NIH 3T3 cells.

Acciones bioquímicas o fisiológicas

Cell permeable: yes
Primary Target
cam kinase 2
Product competes with ATP.
Reversible: yes
Target Ki: 370 nM against rat brain CaM kinase II

Advertencia

Toxicity: Irritant (B)

Reconstitución

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 4 months at -20°C.

Otras notas

Fan, G.H., et al. 1999. Mol. Pharmacol.56, 39.
Tombes, R.M., et al. 1995. Cell Growth Differ.6, 1063.
Mamiya, N., et al. 1993. Biochem. Biophys. Res. Commun. 195, 608.
Nicki, I., et al. 1993. Biochem. Biophys. Res. Commun.191, 255.
Sumi, M., et al. 1991. Biochem. Biophys. Res. Commun.181, 968.
Tokumitsu, H., et al. 1990. J. Biol. Chem.265, 4315.

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

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

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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Diabetic neuropathic pain (DNP) is a frequent complication of diabetes. Calcium/calmodulin-dependent protein kinase II α (CaMKIIα), a multi-functional serine/threonine kinase subunit, is mainly located in the surface layer of the spinal cord dorsal horn (SCDH) and the primary sensory neurons
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The induction of synaptic plasticity at an individual dendritic glutamatergic spine can affect neighboring spines. This local modulation generates dendritic plasticity microdomains believed to expand the neuronal computational capacity. Here, we investigate whether local modulation of plasticity can also occur
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Cells, 9(5) (2020-05-03)
ANO1, a Ca2+-activated chloride channel, is highly expressed in glioblastoma cells and its surface expression is involved in their migration and invasion. However, the regulation of ANO1 surface expression in glioblastoma cells is largely unknown. In this study, we found
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The modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is associated with the regulation of numerous cellular processes. Despite the importance of O-GlcNAc in mediating cellular function our understanding of the mechanisms that regulate O-GlcNAc levels is limited. One factor known
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