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K1385

Sigma-Aldrich

KN-93

synthetic (organic), ≥98% (HPLC),  Ca2+/calmodulin-dependent protein kinase II inhibitor, powder

Synonym(s):

N-[2-[N-(4-Chlorocinnamyl)-N-methylaminomethyl]phenyl]-N-(2-hydroxyethyl)-4-methoxybenzenesulfonamide phosphate salt, N-[2-[[[3-(4′-Chlorophenyl)-2-propenyl]methylamino]methyl]phenyl]-N-(2-hydroxyethyl)-4′-methoxybenzenesulfonamide phosphate salt

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About This Item

Empirical Formula (Hill Notation):
C26H29ClN2O4S · H3PO4
CAS Number:
139298-40-1
Molecular Weight:
599.03
MDL number:
MFCD03788201
UNSPSC Code:
51111800
PubChem Substance ID:
329817125
NACRES:
NA.77

Key Documents

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Product Name

KN-93, ≥98% (HPLC)

biological source

synthetic (organic)

Quality Level

200

assay

≥98% (HPLC)

form

powder

color

white

solubility

DMSO: 1 mg/mL
H2O: soluble

storage temp.

2-8°C

SMILES string

OP(O)(O)=O.COc1ccc(cc1)S(=O)(=O)N(CCO)c2ccccc2CN(C)C\C=C\c3ccc(Cl)cc3

InChI

1S/C26H29ClN2O4S.H3O4P/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;1-5(2,3)4/h3-16,30H,17-20H2,1-2H3;(H3,1,2,3,4)/b6-5+;

InChI key

NNKJTPOXLIILMB-IPZCTEOASA-N

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Application

KN-93 has been used:
  • as an inhibitor to block αCaMKII (Ca2+/calmodulin-dependent protein kinase IIα)
  • as CaMKII inhibitor to pre-treat hippocampal slices
  • to treat the cells, to alter the cytoskeleton (CSK) structure and function during the experiment

Biochem/physiol Actions

KN-93 is a selective Ca2+/calmodulin-dependent protein kinase II inhibitor, which has been implicated in the regulation of smooth muscle contractility. CaM kinase II activation was inhibited by KN-93 pretreatment (IC50 ~1 μM). KN-93 inhibited histamine-induced tonic force maintenance, whereas early force development and MLC20 phosphorylation responses during the entire time course were unaffected. Both force development and maintenance in response to KCl were inhibited by KN-93. Rapid increases in KCl-induced MLC20 phosphorylation were also inhibited by KN-93, whereas steady-state MLC20 phosphorylation responses were unaffected. In contrast, phorbol 12,13-dibutyrate (PDBu) did not activate CaM kinase II and PDBu-stimulated force development was unaffected by KN-93. Thus KN-93 appears to target a step(s) essential for force maintenance in response to physiological stimuli, suggesting a role for CaM kinase II in regulating tonic contractile responses in arterial smooth muscle. Pharmacological activation of protein kinase C bypasses the KN-93 sensitive step.
KN-93 is a selective Ca2+/calmodulin-dependent protein kinase II inhibitor.

Features and Benefits

This compound is featured on the Ca/CaMKs page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.

Disclaimer

Photosensitive

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
SLCJ4451
SLCF5513
SLCD5365
SLCC3500
SLBW6003

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Thomas Hennig et al.
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Potentiation of Schaffer-Collateral CA1 Synaptic Transmission by eEF2K and p38 MAPK Mediated Mechanisms
Weng W, et al.
Frontiers in Cellular Neuroscience, 247-247 (2016)
S Tessier et al.
Circulation research, 85(9), 810-819 (1999-10-26)
Ca(2+)/calmodulin-dependent protein kinases II (CaMKII) have important functions in regulating cardiac excitability and contractility. In the present study, we examined whether CaMKII regulated the transient outward K(+) current (I(to)) in whole-cell patch-clamped human atrial myocytes. We found that a specific
Jing Xu et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 6(8), 1801233-1801233 (2019-04-25)
Fullerene C60 nanocrystals (nano-C60) possess various attractive bioactivities, including autophagy induction and calcium/calmodulin-dependent protein kinase IIα (CaMKIIα) activation. CaMKIIα is a multifunctional protein kinase involved in many cellular processes including tumor progression; however, the biological effects of CaMKIIα activity modulated
Differential Responses of Cultured MC3T3-E1 Cells to Dynamic and Static Stimulated Effect of Microgravity in Cell Morphology, Cytoskeleton Structure and Ca2+ Signaling
Luo M, et al.
mBio, 13(2), 137-157 (2016)
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