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Merck

422708

KN-93

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

Synonyme(s) :

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

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A propos de cet article

Formule empirique (notation de Hill) :
C26H29ClN2O4S
Numéro CAS:
139298-40-1
Poids moléculaire :
501.04
UNSPSC Code:
12352200
NACRES:
NA.77
MDL number:
MFCD03788201
Assay:
≥95% (HPLC)
Form:
solid
Quality level:
100
Storage condition:
OK to freeze, protect from light

Principaux documents

Voir toute la documentation
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Nom du produit

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

SMILES string

[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+

InChI key

LLLQTDSSHZREGW-AATRIKPKSA-N

assay

≥95% (HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze, protect from light

color

off-white

solubility

DMSO: 5 mg/mL

shipped in

ambient

storage temp.

2-8°C

Quality Level

100

Catégories apparentées

General description

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.

Biochem/physiol Actions

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

Preparation Note

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

Other Notes

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.

Legal Information

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

Disclaimer

Toxicity: Irritant (B)

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Siyi Li et al.
Neuroreport, 35(4), 258-268 (2024-02-02)
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
Xiao-Fen He et al.
Purinergic signalling (2022-01-02)
Diabetic neuropathic pain (DNP) is frequent among patients with diabetes. We previously showed that P2X3 upregulation in dorsal root ganglia (DRG) plays a role in streptozotocin (STZ)-induced DNP but the underlying mechanism is unclear. Here, a rat model of DNP
Tiziana Ravasenga et al.
Cell reports, 38(6), 110347-110347 (2022-02-10)
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
Kyoung Mi Sim et al.
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
Luyun Zou et al.
Frontiers in molecular biosciences, 8, 780865-780865 (2021-12-25)
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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