422708
KN-93
≥95% (HPLC), solid, CAM kinase II inhibitor, Calbiochem®
Synonym(s):
2-[N-(2-hydroxyethyl)]-N-(4-methoxybenzenesulfonyl)]amino-N-(4-chlorocinnamyl)-N-methylbenzylamine)
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About This Item
Empirical Formula (Hill Notation):
C26H29ClN2O4S
CAS Number:
Molecular Weight:
501.04
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.77
product name
KN-93, A cell-permeable, reversible and competitive inhibitor of rat brain CaM kinase II (Ki = 370 nM).
Quality Level
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
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
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
cam kinase 2
Product competes with ATP.
Reversible: yes
Target Ki: 370 nM against rat brain CaM kinase II
Warning
Toxicity: Irritant (B)
Reconstitution
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.
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
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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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