Substance
ID:184498
Names and Identifiers
IUPAC name
N-[2-({[(2E)-3-(4-chlorophenyl)prop-2-en-1-yl](methyl)amino}methyl)phenyl]-2-hydroxy-S'-(4-methoxyphenyl)ethane-1-sulfonamido; phosphoric acid
Synonyms
N-[2-[[[3-(4′-Chlorophenyl)-2-propenyl]methylamino]methyl]phenyl]-N-(2-hydroxyethyl)-4′-methoxybenzenesulfonamide phosphate saltN-[2-[N-(4-Chlorocinnamyl)-N-methylaminomethyl]phenyl]-N-(2-hydroxyethyl)-4-methoxybenzenesulfonamide phosphate saltKN-93
IUPAC Traditional name
N-[2-({[(2E)-3-(4-chlorophenyl)prop-2-en-1-yl](methyl)amino}methyl)phenyl]-2-hydroxy-S'-(4-methoxyphenyl)ethanesulfonamido; phosphoric acid
Properties
Product Information
Purity
≥98% (HPLC)
Safety Information
Storage Temperature
2-8°C
German water hazard class
3
Personal Protective Equipment
Eyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
Physical Property
Solubility
DMSO: soluble1 mg/mL
H2O: soluble
Apperance
white
Molecule Details
Frequently Asked Questions
Live Chat and Frequently Asked Questions are available for this Product.
Caution
Photosensitive
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.
Live Chat and Frequently Asked Questions are available for this Product.
Caution
Photosensitive
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.
Molecular Spectra
No Data Available
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References
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