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422708

KN-93

Name: KN-93
Brand: MM

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

同義詞:

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

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About This Item

經驗公式（希爾表示法）:

C₂₆H₂₉ClN₂O₄S

CAS號碼:

139298-40-1

分子量：:

501.04

MDL號碼:

MFCD03788201

分類程式碼代碼:

12352200

NACRES:

NA.77

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product name

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

品質等級

100

化驗

≥95% (HPLC)

形狀

solid

製造商／商標名

Calbiochem^®

儲存條件

OK to freeze
protect from light

顏色

off-white

溶解度

DMSO: 5 mg/mL

運輸包裝

ambient

儲存溫度

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 密鑰

LLLQTDSSHZREGW-AATRIKPKSA-N

一般說明

A cell-permeable, reversible and competitive inhibitor of rat brain CaM kinase II (K_i = 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 (K_i = 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.

生化／生理作用

Cell permeable: yes

Primary Target
cam kinase 2

Product competes with ATP.

Reversible: yes

Target K_i: 370 nM against rat brain CaM kinase II

警告

Toxicity: Irritant (B)

重構

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

其他說明

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.

法律資訊

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

儲存類別代碼

11 - Combustible Solids

水污染物質分類（WGK）

WGK 3

閃點（°F）

Not applicable

閃點（°C）

Not applicable

分析證明 (COA)

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Electroacupuncture alleviates streptozotocin-induced diabetic neuropathic pain via suppressing phosphorylated CaMKIIα in rats.

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

Inhibition of phosphorylated calcium/calmodulin-dependent protein kinase IIα relieves streptozotocin-induced diabetic neuropathic pain through regulation of P2X3 receptor in dorsal root ganglia.

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

Spatial regulation of coordinated excitatory and inhibitory synaptic plasticity at dendritic synapses.

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

Suppression of CaMKIIβ Inhibits ANO1-Mediated Glioblastoma Progression.

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

Ser-2030, but not Ser-2808, is the major phosphorylation site in cardiac ryanodine receptors responding to protein kinase A activation upon beta-adrenergic stimulation in normal and failing hearts.

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

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KN-93