810133P
Avanti
18:1-12:0 NBD PC
Avanti Research™ - A Croda Brand 810133P, powder
Synonym(s):
1-Oleoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-Glycero-3-Phosphocholine
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About This Item
Recommended Products
Assay
>99% (TLC)
form
powder
packaging
pkg of 1 × 1 mg (810133P-1mg)
pkg of 5 × 1 mg (810133P-5mg)
manufacturer/tradename
Avanti Research™ - A Croda Brand 810133P
shipped in
dry ice
storage temp.
−20°C
General description
Phosphocholine is considered as a precursor molecule. It is formed during the breakdown of phosphatidylcholine metabolism.
Application
18:1-12:0 NBD PC is suitable for use:
- as an optical probe of dynamics in the preparation of liposomes
- as the fluorophore in the formation of neuropathy target esterase (NTE) catalytic domain (NEST) proteoliposome
- as a component in bilayer membranes
- to prepare lipid vesicles
Packaging
5 mL Amber Glass Screw Cap Vial (810133P-1mg)
5 mL Amber Glass Screw Cap Vial (810133P-5mg)
Legal Information
Avanti Research is a trademark of Avanti Polar Lipids, LLC
Storage Class Code
11 - Combustible Solids
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’.
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Antimicrobial peptides temporins B and L induce formation of tubular lipid protrusions from supported phospholipid bilayers
Biophysical Journal, 91(12), 4427-4439 (2006)
Comparison of liposomes formed by sonication and extrusion: rotational and translational diffusion of an embedded chromophore
Langmuir, 23(23), 11677-11683 (2007)
Biology-cancer metabolic phenotype
NMR Metabolomics in Cancer Research, 15-138 (2013)
Influence of lysophospholipid hydrolysis by the catalytic domain of neuropathy target esterase on the fluidity of bilayer lipid membranes
Biochimica et Biophysica Acta - Biomembranes, 1798(8), 1533-1539 (2010)
Proceedings of the National Academy of Sciences of the United States of America, 113(16), 4362-4367 (2016-04-05)
Organelles are in constant communication with each other through exchange of proteins (mediated by trafficking vesicles) and lipids [mediated by both trafficking vesicles and lipid transfer proteins (LTPs)]. It has long been known that vesicle trafficking can be tightly regulated
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