810607P
Avanti
18:1 TEMPO Lyso PC
Avanti Research™ - A Croda Brand 810607P, powder
Synonym(s):
1-oleoyl-2-hydroxy-sn-glycero-3-phospho(tempo)choline
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About This Item
Empirical Formula (Hill Notation):
C34H66N2O8P
CAS Number:
Molecular Weight:
661.87
UNSPSC Code:
41141825
NACRES:
NA.25
assay
>99% (TLC)
form
powder
packaging
pkg of 1 × 1 mg (810607P-1mg)
manufacturer/tradename
Avanti Research™ - A Croda Brand 810607P
shipped in
dry ice
storage temp.
−20°C
General description
Lysophosphatidylcholine (LPC) is one of the important constituent of oxidized low-density lipoprotein (Ox-LDL). 1-oleoyl-2-hydroxy-sn-glycero-3-phospho(tempo)choline (18:1 TEMPO Lyso PC), a lipoxygenase substrate analog is a lysooleoyllecithin which carries a spin label instead of a choline methyl. It is a paramagnetic lysolipid.
TEMPO and DOXYL spin probes penetrate liposome membranes. This may reveal new components with increased ordering of the lipids associated with peptides or proteins.
Application
1-oleoyl-2-hydroxy-sn-glycero-3-phospho(tempo)choline (18:1 TEMPO Lyso PC) may be used as a spin-labeled lysolecithin (LOPTC) in micelles to study the nature of lipoxygenase interaction by electron paramagnetic resonance spectroscopy.
Biochem/physiol Actions
Lysophosphatidylcholine (LPC) is known to play a vital role in the atherogenic activity of oxidized low-density lipoprotein (Ox-LDL). 1-oleoyl-2-hydroxy-sn-glycero-3-phospho(tempo)choline (18:1 TEMPO Lyso PC) can form micelles in solution.
Packaging
5 mL Clear Glass Sealed Ampule (810607P-1mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
Storage Class
11 - Combustible Solids
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Takayuki Matsumoto et al.
Current medicinal chemistry, 14(30), 3209-3220 (2008-01-29)
Lysophosphatidylcholine (LPC) is a bioactive proinflammatory lipid generated by pathological activities. LPC is also a major phospholipid component of oxidized low-density lipoprotein (Ox-LDL) and is implicated as a critical factor in the atherogenic activity of Ox-LDL. LPC is believed to
Betty J Gaffney et al.
Biophysical journal, 103(10), 2134-2144 (2012-12-04)
Lipoxygenase enzymes initiate diverse signaling pathways by specifically directing oxygen to different carbons of arachidonate and other polyunsaturated acyl chains, but structural origins of this specificity have remained unclear. We therefore determined the nature of the lipoxygenase interaction with the
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