810590O
Avanti
10-Doxyl Nonadecane
Avanti Polar Lipids 810590O
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10-doxyl nonadecane
C23H46NO2
Recommended Products
Assay
>99% (TLC)
form
liquid
packaging
pkg of 1 × 1 mg (810590O-1mg)
manufacturer/tradename
Avanti Polar Lipids 810590O
shipped in
dry ice
storage temp.
−20°C
InChI
1S/C23H46NO2/c1-5-7-9-11-13-15-17-19-23(24(25)22(3,4)21-26-23)20-18-16-14-12-10-8-6-2/h5-21H2,1-4H3
InChI key
LMFAKDOCBCXKIK-UHFFFAOYSA-N
General description
Quenching of tryptophan (Trp) by 10-docylnonadecane can be used to measure Trp depth in the lipid membrane.
Packaging
5 mL Clear Glass Sealed Ampule (810590O-1mg)
WGK
WGK 3
Flash Point(F)
235.4 °F
Flash Point(C)
113 °C
Regulatory Information
新产品
Certificates of Analysis (COA)
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Biochemical and biophysical research communications, 343(2), 483-488 (2006-03-21)
The linear peptide gramicidin forms prototypical ion channels specific for monovalent cations and has been extensively used to study the organization, dynamics, and function of membrane-spanning channels. We have analyzed the localization of the functionally important tryptophan residues of the
International journal of pharmaceutics, 200(1), 27-39 (2000-06-14)
The development of stable spherical lipid-coated drug particles that are termed 'lipocores' is reported here. Unlike conventional lipid-based particles (i.e. liposomes, emulsions, micelles), these particles are comprised solely of a core of a poorly water soluble drug surrounded by polyethyleneglycol
Biochemistry, 42(11), 3265-3274 (2003-03-19)
A novel fluorescence method for determining the depth of Trp residues in membrane-inserted polypeptides is introduced. Quenching of Trp by acrylamide and 10-doxylnonadecane (10-DN) was used to measure Trp depth. Transmembrane helices with Trp residues at varying positions (and thus
Peptide science (Hoboken, N.J.), 110(4) (2019-01-15)
Amphiphilic alpha-helices are common motifs used in numerous biological systems including membrane channels/pores and antimicrobial peptides (AMPs), and binding proteins, and a variety of synthetic biomaterials. Previously, an amphiphilic peptide with lysine-containing motifs was shown to reversibly bind the anionic
The Journal of biological chemistry, 290(42), 25579-25594 (2015-09-02)
Enterohemorrhagic Escherichia coli is a causative agent of gastrointestinal and diarrheal diseases. Pathogenesis associated with enterohemorrhagic E. coli involves direct delivery of virulence factors from the bacteria into epithelial cell cytosol via a syringe-like organelle known as the type III
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