Skip to Content
MilliporeSigma

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)

Slide 1 of 1
Sign In to View Organizational & Contract Pricing.

Select a Size

1 MG

$205.00

5 MG

$665.00

$205.00

Check Cart for Availability

About This Item

Empirical Formula (Hill Notation):
C26H29ClN2O4S
CAS Number:
139298-40-1
Molecular Weight:
501.04
UNSPSC Code:
12352200
NACRES:
NA.77
MDL number:
MFCD03788201

Key Documents

View All Documentation

Skip To

Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

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

Related Categories

Compare Similar Items

View Full Comparison

Show Differences

1 of 4

This Item
K1385422709422712
KN-93 A cell-permeable, reversible and competitive inhibitor of rat brain CaM kinase II (Ki = 370 nM).

Sigma-Aldrich

422708

KN-93

KN-93 ≥98% (HPLC)

Sigma-Aldrich

K1385

KN-93

KN-92 KN-92, CAS 1135280-28-2, is useful as a negative control for KN-93 (Cat. No. 422708), a Ca2+/CaM Kinase II inhibitor.

Sigma-Aldrich

422709

KN-92

KN-93 InSolution, ≥95%, A cell-permeable, competitive inhibitor of Ca2+/calmodulin-dependent protein kinase II

Sigma-Aldrich

422712

KN-93

form

solid

form

powder

form

viscous liquid

form

liquid

assay

≥95% (HPLC)

assay

≥98% (HPLC)

assay

≥95% (HPLC)

assay

≥95% (HPLC)

Quality Level

100

Quality Level

200

Quality Level

100

Quality Level

100

manufacturer/tradename

Calbiochem®

manufacturer/tradename

-

manufacturer/tradename

Calbiochem®

manufacturer/tradename

Calbiochem®

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

solubility

DMSO: 5 mg/mL

solubility

DMSO: 1 mg/mL, H2O: soluble

solubility

DMSO: 5 mg/mL

solubility

-

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

Disclaimer

Toxicity: Irritant (B)

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.

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.

Preparation Note

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

Legal Information

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

Storage Class

11 - Combustible Solids

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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
Bailong Xiao et al.
The Biochemical journal, 396(1), 7-16 (2006-02-18)
We have recently shown that RyR2 (cardiac ryanodine receptor) is phosphorylated by PKA (protein kinase A/cAMP-dependent protein kinase) at two major sites, Ser-2030 and Ser-2808. In the present study, we examined the properties and physiological relevance of phosphorylation of these
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
View All Related Papers

Related Content

Questions

Reviews

No rating value

Active Filters

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service