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124029

Sigma-Aldrich

Akt Inhibitor XII, Isozyme-Selective, Akti-2

The Akt Inhibitor XII, Isozyme-Selective, Akti-2 controls the biological activity of Akt. This small molecule/inhibitor is primarily used for Phosphorylation & Dephosphorylation applications.

Sinónimos:

Akt Inhibitor XII, Isozyme-Selective, Akti-2, 1-((2-(4-((4-(2,3-Dihydro-2-oxo-1H-benzimidazol-1-yl)-1-piperidinyl)methyl)phenyl)-3-phenyl-6-quinoxalinyl)carbonyl)-4-methyl-piperazine, 3HCl and, 1-((3-(4-((4-(2,3-Dihydro-2-oxo-1H-benzimidazol-1-yl)-1-piperidinyl)methyl)phenyl)-2-phenyl-6-quinoxalinyl

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About This Item

Fórmula empírica (notación de Hill):
C39H39N7O2 · 3HCl
Peso molecular:
747.16
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

assay

≥97% (mixture of regioisomers, HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)
protect from light

color

yellow

solubility

DMSO: 25 mg/mL
water: 50 mg/mL

shipped in

ambient

storage temp.

2-8°C

General description

A cell-permeable Akti-1/2- (Cat. No. 124018) derived allosteric inhibitor pair (1:1 regioisomeric mixture) with much improved aqueous solubility (10 mg/ml in a pH 7.4 saline) and Akt2 selectivity (IC50 = 805 nM for Akt2, >10 µM for Akt1/3, and >50 µM for PKA/PKC/SGK). The inhibition is PH domain-dependent and non-competitive with ATP.
A cell-permeable Akti-1/2- (Cat. No. 124018) derived allosteric inhibitor pair (1:1 regioisomeric mixture) with much improved aqueous solubility (10 mg/ml in a pH 7.4 saline) and Akt2 selectivity (IC50 = 805 nM for Akt2, >10 µM for Akt1/3, and >50 µM for PKA/PKC/SGK). The inhibition is PH domain-dependent and non-competitive with ATP.

Packaging

Packaged under inert gas

Warning

Toxicity: Standard Handling (A)

Legal Information

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

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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Kenneth K Y Ting et al.
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The accumulation of lipid and the formation of macrophage foam cells is a hallmark of atherosclerosis, a chronic inflammatory disease. To better understand the role of macrophage lipid accumulation in inflammation during atherogenesis, we studied early molecular events that follow

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