700051P
Avanti
22(S)-hydroxycholesterol-d7
Avanti Research™ - A Croda Brand
Synonym(s):
25,26,26,26,27,27,27-heptadeuterocholest-5-ene-3β,22S-diol
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description
cholest-5-ene-3β,22(S)-diol-d7
Assay
>99% (TLC)
form
powder
packaging
pkg of 1 × 1 mg (700051P-1mg)
manufacturer/tradename
Avanti Research™ - A Croda Brand
shipped in
dry ice
storage temp.
−20°C
General description
22(S)-hydroxycholesterol is an enantiomer of 22(R)-hydroxycholesterol. 22(S)-hydroxycholesterol-d7 is a deuterated form of 22(S)-hydroxycholesterol.
Application
22(S)-hydroxycholesterol-d7 may be used as an internal standard in liquid chromatography with tandem mass spectrometry (LC-MS-MS) analysis of plasma low-density lipoprotein (LDL).
Biochem/physiol Actions
22(S)-hydroxycholesterol (22(S)-HC) promotes glucose catabolism and uptake and is regarded as a potential target to treat type 2 diabetes. 22(S)-HC also prevents the accumulation of lipids and lipid synthesis in hepatocytes and myotubes. Unlike 22(R)-hydroxycholesterol, 22(S)-HC is not estrogenic and is not a ligand for liver X receptor (LXR).
Packaging
5 mL Amber Glass Screw Cap Vial (700051P-1mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
Storage Class Code
11 - Combustible Solids
Certificates of Analysis (COA)
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Bioscience, biotechnology, and biochemistry, 68(8), 1790-1793 (2004-08-24)
In order to test the estrogenic activity of sterol oxidation products from cholesterol and phytosterols, an estrogen-dependent gene expression assay was performed in estrogen receptor alpha-stably transformed HeLa cells. The ranking of the estrogenic potency of these compounds was different:
The Journal of steroid biochemistry and molecular biology, 128(3-5), 154-164 (2011-11-05)
The aim of this study was to explore the effects of 22(S)-hydroxycholesterol (22(S)-HC) on lipid and glucose metabolism in human-derived cells from metabolic active tissues. Docking of T0901317 and 22(S)-HC showed that both substances fitted into the ligand binding domain
Journal of lipid research, 57(5), 791-808 (2016-03-19)
Endothelial biomechanics is emerging as a key factor in endothelial function. Here, we address the mechanisms of endothelial stiffening induced by oxidized LDL (oxLDL) and investigate the role of oxLDL in lumen formation. We show that oxLDL-induced endothelial stiffening is
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