1 2 dioleoyl sn glycero 3 phosphocholine dopc  (Avanti Polar)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    Avanti Polar 1 2 dioleoyl sn glycero 3 phosphocholine dopc
    <t>1,2-dioleoyl-</t> sn <t>-glycero-3-phosphocholine</t> <t>(DOPC)</t> vesicle (green), 1 min (left) and 10 min (right) after the incubation with nanoparticles ( r = 42 nm, magenta). Obviously, vesicle membrane is consumed while particles are internalized.
    1 2 Dioleoyl Sn Glycero 3 Phosphocholine Dopc, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 94/100, based on 151 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/1 2 dioleoyl sn glycero 3 phosphocholine dopc/product/Avanti Polar
    Average 94 stars, based on 151 article reviews
    Price from $9.99 to $1999.99
    1 2 dioleoyl sn glycero 3 phosphocholine dopc - by Bioz Stars, 2020-09
    94/100 stars

    Images

    1) Product Images from "Intake of silica nanoparticles by giant lipid vesicles: influence of particle size and thermodynamic membrane state"

    Article Title: Intake of silica nanoparticles by giant lipid vesicles: influence of particle size and thermodynamic membrane state

    Journal: Beilstein Journal of Nanotechnology

    doi: 10.3762/bjnano.5.256

    1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC) vesicle (green), 1 min (left) and 10 min (right) after the incubation with nanoparticles ( r = 42 nm, magenta). Obviously, vesicle membrane is consumed while particles are internalized.
    Figure Legend Snippet: 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC) vesicle (green), 1 min (left) and 10 min (right) after the incubation with nanoparticles ( r = 42 nm, magenta). Obviously, vesicle membrane is consumed while particles are internalized.

    Techniques Used: Incubation

    2) Product Images from "Interaction of a Polyarginine Peptide with Membranes of Different Mechanical Properties"

    Article Title: Interaction of a Polyarginine Peptide with Membranes of Different Mechanical Properties

    Journal: Biomolecules

    doi: 10.3390/biom9100625

    Insertion of KR 9 C into 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)/DOPG monolayers at 30 mN/m and 23 °C followed by fluorescence microscopy. Ten micrometers of the peptide were injected into the subphase at t = 0. ( a ) Representative images at the indicated times after peptide addition. ( b ) Percent of the area occupied by the darker regions, which corresponds to liquid-condensed phase state. ( c ) Number of domains in a 100 μm 2 region.
    Figure Legend Snippet: Insertion of KR 9 C into 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)/DOPG monolayers at 30 mN/m and 23 °C followed by fluorescence microscopy. Ten micrometers of the peptide were injected into the subphase at t = 0. ( a ) Representative images at the indicated times after peptide addition. ( b ) Percent of the area occupied by the darker regions, which corresponds to liquid-condensed phase state. ( c ) Number of domains in a 100 μm 2 region.

    Techniques Used: Fluorescence, Microscopy, Injection

    Increase in conductivity of black lipid membranes (BLMs) of the indicated compositions after addition of 1 µM KR 9 C. ANOVA test indicated that there is at least one different data with a 5% confidence (α = 0.05); the obtained * p -value was 0.01. The asterisk denotes a statistically significant difference between 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC)/ cholesterol (CHOL)/DOPG and DOPC/DOPG and DPPC/DOP, according to the Tukey test
    Figure Legend Snippet: Increase in conductivity of black lipid membranes (BLMs) of the indicated compositions after addition of 1 µM KR 9 C. ANOVA test indicated that there is at least one different data with a 5% confidence (α = 0.05); the obtained * p -value was 0.01. The asterisk denotes a statistically significant difference between 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC)/ cholesterol (CHOL)/DOPG and DOPC/DOPG and DPPC/DOP, according to the Tukey test

    Techniques Used:

    3) Product Images from "Enhanced efficacy of sublingual immunotherapy by liposome-mediated delivery of allergen"

    Article Title: Enhanced efficacy of sublingual immunotherapy by liposome-mediated delivery of allergen

    Journal: International Journal of Nanomedicine

    doi: 10.2147/IJN.S137033

    OVA dissociation and leakage from liposomes. Notes: OVA-liposomes were stored at 4°C and centrifuged at different time points using Amicon ultracel-100 membrane 100,000 MWCO filter units. The amount of OVA in the filtrate from both OVA-DOPC and OVA-POPC liposomes was quantified using amino acid analysis. Abbreviations: OVA, ovalbumin; POPC, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; DOPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine.
    Figure Legend Snippet: OVA dissociation and leakage from liposomes. Notes: OVA-liposomes were stored at 4°C and centrifuged at different time points using Amicon ultracel-100 membrane 100,000 MWCO filter units. The amount of OVA in the filtrate from both OVA-DOPC and OVA-POPC liposomes was quantified using amino acid analysis. Abbreviations: OVA, ovalbumin; POPC, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; DOPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine.

    Techniques Used:

    Physical stability and characterization of OVA-liposomes. Notes: Neutral or cationic formulated OVA-POPC or OVA-DOPC liposomes were tested over a period of 4.5 months using DLS where the liposomes were stored at 4°C. ( A , C ) Diameter of OVA-POPC and OVA-DOPC liposomes, respectively, measured as replicates 5× for 30 seconds each. ( B , D ) Polydispersity index for OVA-POPC and OVA-DOPC liposomes, respectively. Each time point represents mean ± SD of two distinct samples. Abbreviations: OVA, ovalbumin; POPC, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; DOPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine; DLS, dynamic light scattering; SD, standard deviation.
    Figure Legend Snippet: Physical stability and characterization of OVA-liposomes. Notes: Neutral or cationic formulated OVA-POPC or OVA-DOPC liposomes were tested over a period of 4.5 months using DLS where the liposomes were stored at 4°C. ( A , C ) Diameter of OVA-POPC and OVA-DOPC liposomes, respectively, measured as replicates 5× for 30 seconds each. ( B , D ) Polydispersity index for OVA-POPC and OVA-DOPC liposomes, respectively. Each time point represents mean ± SD of two distinct samples. Abbreviations: OVA, ovalbumin; POPC, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine; DOPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine; DLS, dynamic light scattering; SD, standard deviation.

    Techniques Used: Standard Deviation

    4) Product Images from "Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2"

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2

    Journal: Journal of Lipid Research

    doi: 10.1194/jlr.M070730

    Hydrolysis of one medium-chain ox-PC by LPLA2 under neutral conditions. The reaction mixture contained 49 mM HEPES (pH 7.4), 10 μg/ml BSA, liposomes (130 μM PL), and 80 ng/ml of recombinant mouse LPLA2 in 500 μl of total volume. The liposomes consisted of DODPC/DOPC or one medium-chain ox-PC (PAzPC) (2.4:1, molar ratio). The reaction was initiated by the addition of recombinant LPLA2 and kept for 30 to 120 min at 37°C. The reaction products were extracted and separated with a HPTLC plate using a solvent system consisting of chloroform/methanol/pyridine (98:2:0.5, v/v) (A, B) or chloroform/methanol/water (60:35:8, v/v) (C), as described in the Materials and Methods. The reaction products produced by LPLA2 in (A–C) were quantified by scanning the plate, as described in the Materials and Methods, and were plotted against the incubation time (D). 1-Pal-2-LysoPC, 1-palmitoyl- sn -glycero-3-phosphocholine.
    Figure Legend Snippet: Hydrolysis of one medium-chain ox-PC by LPLA2 under neutral conditions. The reaction mixture contained 49 mM HEPES (pH 7.4), 10 μg/ml BSA, liposomes (130 μM PL), and 80 ng/ml of recombinant mouse LPLA2 in 500 μl of total volume. The liposomes consisted of DODPC/DOPC or one medium-chain ox-PC (PAzPC) (2.4:1, molar ratio). The reaction was initiated by the addition of recombinant LPLA2 and kept for 30 to 120 min at 37°C. The reaction products were extracted and separated with a HPTLC plate using a solvent system consisting of chloroform/methanol/pyridine (98:2:0.5, v/v) (A, B) or chloroform/methanol/water (60:35:8, v/v) (C), as described in the Materials and Methods. The reaction products produced by LPLA2 in (A–C) were quantified by scanning the plate, as described in the Materials and Methods, and were plotted against the incubation time (D). 1-Pal-2-LysoPC, 1-palmitoyl- sn -glycero-3-phosphocholine.

    Techniques Used: Recombinant, High Performance Thin Layer Chromatography, Produced, Incubation

    5) Product Images from "Ganglioside embedded in reconstituted lipoprotein binds cholera toxin with elevated affinity [S]"

    Article Title: Ganglioside embedded in reconstituted lipoprotein binds cholera toxin with elevated affinity [S]

    Journal: Journal of Lipid Research

    doi: 10.1194/jlr.M007401

    CTB-GM1 binding in surface-supported membranes. A: UV patterning enables a side-by-side comparison of Texas Red-labeled cholera toxin binding to 1 mol% GM1 supported in a fluid DMPC bilayer (outside squares) versus rHDL supports (inside squares). B: A plot of the fluorescence intensity along the line shown, indicates a 2-to 3-fold increase between the region inside and outside of the squares. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; GM1, monosialotetrahexosylganglioside.
    Figure Legend Snippet: CTB-GM1 binding in surface-supported membranes. A: UV patterning enables a side-by-side comparison of Texas Red-labeled cholera toxin binding to 1 mol% GM1 supported in a fluid DMPC bilayer (outside squares) versus rHDL supports (inside squares). B: A plot of the fluorescence intensity along the line shown, indicates a 2-to 3-fold increase between the region inside and outside of the squares. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; GM1, monosialotetrahexosylganglioside.

    Techniques Used: CtB Assay, Binding Assay, Labeling, Fluorescence

    Interaction of cells with vesicles and rHDL separately. Equal concentrations of fluorescently-labeled lipid particles are incubated for 4 h with RPE cells. POPC 100 nm diameter unilamellar vesicles with 2 mol% Texas Red-DHPE (A) and reconstituted HDL composed of apoA-I, DMPC, and 2 mol% Texas Red-DHPE (B) both show some association with cells. All images obtained at 10× magnification. ApoA-I, apolipoprotein A-I; DHPE, 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethyl-ammonium salt; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine.
    Figure Legend Snippet: Interaction of cells with vesicles and rHDL separately. Equal concentrations of fluorescently-labeled lipid particles are incubated for 4 h with RPE cells. POPC 100 nm diameter unilamellar vesicles with 2 mol% Texas Red-DHPE (A) and reconstituted HDL composed of apoA-I, DMPC, and 2 mol% Texas Red-DHPE (B) both show some association with cells. All images obtained at 10× magnification. ApoA-I, apolipoprotein A-I; DHPE, 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine, triethyl-ammonium salt; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine.

    Techniques Used: Labeling, Incubation

    Characterization of FRET pair and toxin-quencher titration. A: Excitation and emission spectra of DPH and FITC-CTB. Intensity of each spectrum is not to scale. Inset: schematic representation of DPH (green) embedded in the hydrophobic core of the lipoprotein (yellow) and its proximity to a receptor (purple) and fluorescently-labeled pentavalent ligand (red). B: Stern-Volmer plot of GM1-CTB binding for DMPC vesicles containing 1.0 mol% GM1. The independent axis is molarity of CTB (nM) and the dependent axis is the inverse normalized donor fluorescence ( I o / I) . Error bars are derived from instrument error. The entire collection of S-V plots are available in the supplementary data. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; DPH, diphenylhexatriene; FITC, fluorescein-isothiocyanate; FRET, Foerster Resonant Energy Transfer; GM1, monosialotetrahexosylganglioside.
    Figure Legend Snippet: Characterization of FRET pair and toxin-quencher titration. A: Excitation and emission spectra of DPH and FITC-CTB. Intensity of each spectrum is not to scale. Inset: schematic representation of DPH (green) embedded in the hydrophobic core of the lipoprotein (yellow) and its proximity to a receptor (purple) and fluorescently-labeled pentavalent ligand (red). B: Stern-Volmer plot of GM1-CTB binding for DMPC vesicles containing 1.0 mol% GM1. The independent axis is molarity of CTB (nM) and the dependent axis is the inverse normalized donor fluorescence ( I o / I) . Error bars are derived from instrument error. The entire collection of S-V plots are available in the supplementary data. CTB, cholera toxin subunit B; DMPC, 1,2-dimyristoyl-sn-glycero-3-phosphocholine; DPH, diphenylhexatriene; FITC, fluorescein-isothiocyanate; FRET, Foerster Resonant Energy Transfer; GM1, monosialotetrahexosylganglioside.

    Techniques Used: Titration, CtB Assay, Labeling, Binding Assay, Fluorescence, Derivative Assay

    6) Product Images from "Topical delivery of anti-TNFα siRNA and capsaicin via novel lipid-polymer hybrid nanoparticles efficiently inhibits skin inflammation in vivo"

    Article Title: Topical delivery of anti-TNFα siRNA and capsaicin via novel lipid-polymer hybrid nanoparticles efficiently inhibits skin inflammation in vivo

    Journal: Journal of controlled release : official journal of the Controlled Release Society

    doi: 10.1016/j.jconrel.2013.04.021

    Schematic illustration shows the formulation of CyLiPn. The CyLiPn comprises a hydrophobic PLGA core, a hydrophilic PEG shell and a lipid monolayer consisting of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and a new cationic cyclic-head lipid at the
    Figure Legend Snippet: Schematic illustration shows the formulation of CyLiPn. The CyLiPn comprises a hydrophobic PLGA core, a hydrophilic PEG shell and a lipid monolayer consisting of 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) and a new cationic cyclic-head lipid at the

    Techniques Used:

    7) Product Images from "New insight into the interaction of TRAF2 C-terminal domain with lipid rafts microdomains"

    Article Title: New insight into the interaction of TRAF2 C-terminal domain with lipid rafts microdomains

    Journal: Biochimica et biophysica acta

    doi: 10.1016/j.bbalip.2017.05.003

    Diffusion coefficients of labeled TRAF2 bound to GUVs. Vesicles were obtained from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), raft-like mixture (i.e. 1,2-dioleoyl-sn-glycero-3-phosphocholine/sphingomyelin/cholesterol (DOPC/SM/Cholesterol), BBM samples (Kidney Juxtamedullary Cortex (JMC), Kidney Superficial Cortex (SC), Intestinal Duodenum (ID), and Intestinal Jejunum (IJ)) and POPC + 1 % GM1. Data are expressed as mean ± SD values of three independent experiments; * and ** denote p
    Figure Legend Snippet: Diffusion coefficients of labeled TRAF2 bound to GUVs. Vesicles were obtained from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), raft-like mixture (i.e. 1,2-dioleoyl-sn-glycero-3-phosphocholine/sphingomyelin/cholesterol (DOPC/SM/Cholesterol), BBM samples (Kidney Juxtamedullary Cortex (JMC), Kidney Superficial Cortex (SC), Intestinal Duodenum (ID), and Intestinal Jejunum (IJ)) and POPC + 1 % GM1. Data are expressed as mean ± SD values of three independent experiments; * and ** denote p

    Techniques Used: Diffusion-based Assay, Labeling

    8) Product Images from "Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo"

    Article Title: Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo

    Journal: Nature Communications

    doi: 10.1038/s41467-020-17360-9

    Photoswitching the surface charge of a liposome – from neutral to cationic – requires photoactive lipids embedded within a liposome membrane. Prior to light activation, charge neutral, photoactive liposomes freely circulate throughout the vasculature of a zebrafish embryo and do not interact with RES cell types, or any other cell type, of the embryonic fish. Upon light irradiation and photolysis of photocaged, cholesterylamine lipids, rapid surface charge switching, from neutral to cationic, leads to non-specific adsorption of liposomes across the endothelium of the embryo, liposome uptake and intracellular delivery of liposome-encapsulated, membrane impermeable payloads. DOPC 1,2-dioleoyl- sn -glycero-3-phosphocholine.
    Figure Legend Snippet: Photoswitching the surface charge of a liposome – from neutral to cationic – requires photoactive lipids embedded within a liposome membrane. Prior to light activation, charge neutral, photoactive liposomes freely circulate throughout the vasculature of a zebrafish embryo and do not interact with RES cell types, or any other cell type, of the embryonic fish. Upon light irradiation and photolysis of photocaged, cholesterylamine lipids, rapid surface charge switching, from neutral to cationic, leads to non-specific adsorption of liposomes across the endothelium of the embryo, liposome uptake and intracellular delivery of liposome-encapsulated, membrane impermeable payloads. DOPC 1,2-dioleoyl- sn -glycero-3-phosphocholine.

    Techniques Used: Activation Assay, Fluorescence In Situ Hybridization, Irradiation, Adsorption

    9) Product Images from "Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer Cells"

    Article Title: Phosphatidic Acid (PA) can Displace PPARα/LXRα Binding to The EGFR Promoter Causing its Transrepression in Luminal Cancer Cells

    Journal: Scientific Reports

    doi: 10.1038/srep15379

    Binding and circular dichroism of PPARα in the presence of PA. ( A ) Phospholipase assay was performed using recombinant PLD2 and cells overexpressing PLD2 in the presence of several phospholipids: potential PLD substrates, 1,2-dioctanoyl-sn-glycero-3-phosphocholine (DOPC); 1,2-dimirystoyl-sn-glycero-3-phosphocholine (DMPC); 1,2-diarachidonoyl-sn-glycero-3-phosphocholine (AraPC); 1-oleoyl-2 -hydroxy-sn-glycero-3-phosphatidic acid (lyso-PC) and oxidized 1-palimitoyl, 2-arachidonoyl—sn-glycero-3-phosphocholine (OxPAPC). DOPC is considered the best substrate (positive control). ( B ) Protein-lipid overlay assays to PVDF membranes were performed with recombinant PPARα. PIP 2 was used as a positive control for biding to PPARα and cholesterol was used as a negative control. ( C–E ) Protein-lipid binding by quenching of intrinsic aromatic amino acid fluorescence using the lipids: PC ( C ), DOPA ( D ) or AraPA ( E ) with recombinant PPARα in vitro . ( F,G ) Circular dichroism of PPARα upon binding to ( F ) AraPA (yellow circles) or lysoPA (blue circles), or ( G ) DOPA (red circles) or DMPA (green circles). ( H ) Positive control for Circular Dichroism; PPAR bound to C18:0-CoA, its strongest lignad. ( I ) Secondary structure analysis to ascertain the percentage of alpha helices, beta sheets, turns and undetermined structures in PPAR in the presence of PC or PA. C18:0-CoA was used as a positive control.
    Figure Legend Snippet: Binding and circular dichroism of PPARα in the presence of PA. ( A ) Phospholipase assay was performed using recombinant PLD2 and cells overexpressing PLD2 in the presence of several phospholipids: potential PLD substrates, 1,2-dioctanoyl-sn-glycero-3-phosphocholine (DOPC); 1,2-dimirystoyl-sn-glycero-3-phosphocholine (DMPC); 1,2-diarachidonoyl-sn-glycero-3-phosphocholine (AraPC); 1-oleoyl-2 -hydroxy-sn-glycero-3-phosphatidic acid (lyso-PC) and oxidized 1-palimitoyl, 2-arachidonoyl—sn-glycero-3-phosphocholine (OxPAPC). DOPC is considered the best substrate (positive control). ( B ) Protein-lipid overlay assays to PVDF membranes were performed with recombinant PPARα. PIP 2 was used as a positive control for biding to PPARα and cholesterol was used as a negative control. ( C–E ) Protein-lipid binding by quenching of intrinsic aromatic amino acid fluorescence using the lipids: PC ( C ), DOPA ( D ) or AraPA ( E ) with recombinant PPARα in vitro . ( F,G ) Circular dichroism of PPARα upon binding to ( F ) AraPA (yellow circles) or lysoPA (blue circles), or ( G ) DOPA (red circles) or DMPA (green circles). ( H ) Positive control for Circular Dichroism; PPAR bound to C18:0-CoA, its strongest lignad. ( I ) Secondary structure analysis to ascertain the percentage of alpha helices, beta sheets, turns and undetermined structures in PPAR in the presence of PC or PA. C18:0-CoA was used as a positive control.

    Techniques Used: Binding Assay, Recombinant, Positive Control, Negative Control, Fluorescence, In Vitro

    10) Product Images from "Unveiling the Mechanism of Action of 7α-acetoxy-6β-hydroxyroyleanone on an MRSA/VISA Strain: Membrane and Cell Wall Interactions"

    Article Title: Unveiling the Mechanism of Action of 7α-acetoxy-6β-hydroxyroyleanone on an MRSA/VISA Strain: Membrane and Cell Wall Interactions

    Journal: Biomolecules

    doi: 10.3390/biom10070983

    AHR at relevant antimicrobial concentrations interacts with phospholipid bilayers without compromising their integrity. ( A ) Electronic absorption spectrum of AHR at 20 µM in buffer Tris-HCl, pH 7.4 in the absence and presence of 1mM 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC) large unilamellar vesicles (LUV) suspension. ( B ) Representative curves (median behavior from 6 independent experiments) of the effect of AHR on CF leakage from DOPC LUVs in suspensions, with a total lipid concentration of 0.5 mM, in the presence of different AHR concentrations: 15.6 mg/L (2 MIC, 40 µM), 7.8 mg/L (MIC, 20 µM) and 3.9 mg/L (MIC/2, 10 µM). These experiments were performed at 25 °C.
    Figure Legend Snippet: AHR at relevant antimicrobial concentrations interacts with phospholipid bilayers without compromising their integrity. ( A ) Electronic absorption spectrum of AHR at 20 µM in buffer Tris-HCl, pH 7.4 in the absence and presence of 1mM 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC) large unilamellar vesicles (LUV) suspension. ( B ) Representative curves (median behavior from 6 independent experiments) of the effect of AHR on CF leakage from DOPC LUVs in suspensions, with a total lipid concentration of 0.5 mM, in the presence of different AHR concentrations: 15.6 mg/L (2 MIC, 40 µM), 7.8 mg/L (MIC, 20 µM) and 3.9 mg/L (MIC/2, 10 µM). These experiments were performed at 25 °C.

    Techniques Used: Concentration Assay

    11) Product Images from "A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src"

    Article Title: A non-mitotic role for Aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src

    Journal: Journal of Cell Science

    doi: 10.1242/jcs.157339

    Phosphatidic acid binds to and activates AURA and positively affects tubulin polymerization. (A) Protein–lipid overlay assays using 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPA) and lysates from cells overexpressing AURA. DOPC was used as a negative control. (B) Positive effect of increasing concentrations of phosphatidic acid (PA) on catalytic activity of recombinant purified AURA. Experiments were performed in triplicate and are expressed as the mean±s.e.m. percentage of control. * P
    Figure Legend Snippet: Phosphatidic acid binds to and activates AURA and positively affects tubulin polymerization. (A) Protein–lipid overlay assays using 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPA) and lysates from cells overexpressing AURA. DOPC was used as a negative control. (B) Positive effect of increasing concentrations of phosphatidic acid (PA) on catalytic activity of recombinant purified AURA. Experiments were performed in triplicate and are expressed as the mean±s.e.m. percentage of control. * P

    Techniques Used: Negative Control, Activity Assay, Recombinant, Purification

    Related Articles

    Thin Layer Chromatography:

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2
    Article Snippet: .. The 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2- O -octadecenyl- sn -glycero-3-phosphocholine (DODPC), N -acetylsphingosine (NAS), N -oleoyl-sphingosine, POVPC, PGPC, PONPC, PAzPC, 1-palmitoyl-2-acetyl- sn -glycero-3-phosphocholine (PAcPC), and 1-nonanoyl- sn -glycero-3-phosphocholine were obtained from Avanti Polar Lipids Corp. (Alabaster, AL); recombinant mouse LPLA2 was from Proteos (Kalamazoo, MI); high-performance TLC (HPTLC) silica gel plates (10 × 20 cm) were from Merck (Darmstadt, Germany). .. A HPTLC plate was immersed into 100 mM AgNO3 in acetonitrile and incubated for 10 min.

    Recombinant:

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2
    Article Snippet: .. The 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2- O -octadecenyl- sn -glycero-3-phosphocholine (DODPC), N -acetylsphingosine (NAS), N -oleoyl-sphingosine, POVPC, PGPC, PONPC, PAzPC, 1-palmitoyl-2-acetyl- sn -glycero-3-phosphocholine (PAcPC), and 1-nonanoyl- sn -glycero-3-phosphocholine were obtained from Avanti Polar Lipids Corp. (Alabaster, AL); recombinant mouse LPLA2 was from Proteos (Kalamazoo, MI); high-performance TLC (HPTLC) silica gel plates (10 × 20 cm) were from Merck (Darmstadt, Germany). .. A HPTLC plate was immersed into 100 mM AgNO3 in acetonitrile and incubated for 10 min.

    other:

    Article Title: Enhanced efficacy of sublingual immunotherapy by liposome-mediated delivery of allergen
    Article Snippet: Chemicals 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP), 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(methoxy[PEG]-1000) (ammonium salt) (DOPE-PEG1000), and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-(methoxy[PEG]-2000) (ammonium salt) (DOPE-PEG2000) were purchased from Avanti Polar Lipids (Alabaster, AL, USA).

    Article Title: Interaction of a Polyarginine Peptide with Membranes of Different Mechanical Properties
    Article Snippet: Cholesterol (CHOL), 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dioleoyl-sn-glycero-3-phospho-(1’-rac-glycerol) sodium salt (DOPG), 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-[biotinyl(polyethylene glycol)-2000] ammonium salt (DSPE-PEG(2000) Biotin), and the lipophilic fluorescent probe L-a-phosphatidylethanolamine-N-(lissamine rhodamine B sulfonyl) (ammonium salt) (egg-transphosphatidylated chicken) (Rho-PE) were obtained from Avanti Polar Lipids (Alabaster, AL, USA).

    Article Title: Light-triggered switching of liposome surface charge directs delivery of membrane impermeable payloads in vivo
    Article Snippet: Materials and reagents 1,2-dioleoyl-sn -glycero-3-phosphocholine (DOPC), 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP), 1,2-dioleoyl-sn -glycero-3-phosphoethanolamine-N-(lissamine rhodamine B sulfonyl) (Rhodamine-PE) were purchased from Avanti Polar Lipids (Alabaster, AL, US).

    High Performance Thin Layer Chromatography:

    Article Title: Preferential hydrolysis of truncated oxidized glycerophospholipids by lysosomal phospholipase A2
    Article Snippet: .. The 1,2-dioleoyl- sn -glycero-3-phosphocholine (DOPC), 1,2- O -octadecenyl- sn -glycero-3-phosphocholine (DODPC), N -acetylsphingosine (NAS), N -oleoyl-sphingosine, POVPC, PGPC, PONPC, PAzPC, 1-palmitoyl-2-acetyl- sn -glycero-3-phosphocholine (PAcPC), and 1-nonanoyl- sn -glycero-3-phosphocholine were obtained from Avanti Polar Lipids Corp. (Alabaster, AL); recombinant mouse LPLA2 was from Proteos (Kalamazoo, MI); high-performance TLC (HPTLC) silica gel plates (10 × 20 cm) were from Merck (Darmstadt, Germany). .. A HPTLC plate was immersed into 100 mM AgNO3 in acetonitrile and incubated for 10 min.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 92
    Avanti Polar dopc
    Characterization of <t>SthK</t> channel activity. (A) Normalized 86 Rb + flux through SthK (reconstituted in 5:3:2 <t>DOPC:POPG:cardiolipin)</t> in the presence of 200 µM cAMP (red squares), cGMP (blue circles), both cAMP and cGMP (black triangles), and without cyclic nucleotides (open triangles). Flux through empty liposomes (open circles) is shown as a reference. All flux values are normalized to the maximum uptake recorded in the presence of valinomycin. Bars represent means ± SEM for three separate experiments. (B) SthK channel activity represented by the maximum achieved 86 Rb + uptake through SthK reconstituted in liposomes made from 3:1 POPE:POPG (PE:PG) or 5:3:2 DOPC:POPG:cardiolipin (PC:PG:CA), as indicated, in the presence of 200 µM cAMP. Bars represent means ± SEM for three separate experiments. (C) Representative single-channel recordings of SthK in 0.1 mM intracellular cAMP. (D) I-V relationship of SthK single-channel current amplitude at 100 µM cAMP. (E) Open probability of SthK at 100 mV as a function of the cAMP concentration. Fitting the data with Eq. 10 yields an apparent activation constant of EC 50 = 17 µM and a Hill coefficient of n H = 3. The number of repeats is indicated beside each data point. (F) Open probability of SthK in the presence of 500 µM cAMP as function of the membrane potential. The line indicates the fit according to Eq. 13 , leading to z = 0.8 and V half = 87 mV, Po max = 0.65, and Po min = 0.05. Symbols and error bars in D–F represent means ± SEM from at least three separate bilayers.
    Dopc, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 92/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dopc/product/Avanti Polar
    Average 92 stars, based on 14 article reviews
    Price from $9.99 to $1999.99
    dopc - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    Image Search Results


    Characterization of SthK channel activity. (A) Normalized 86 Rb + flux through SthK (reconstituted in 5:3:2 DOPC:POPG:cardiolipin) in the presence of 200 µM cAMP (red squares), cGMP (blue circles), both cAMP and cGMP (black triangles), and without cyclic nucleotides (open triangles). Flux through empty liposomes (open circles) is shown as a reference. All flux values are normalized to the maximum uptake recorded in the presence of valinomycin. Bars represent means ± SEM for three separate experiments. (B) SthK channel activity represented by the maximum achieved 86 Rb + uptake through SthK reconstituted in liposomes made from 3:1 POPE:POPG (PE:PG) or 5:3:2 DOPC:POPG:cardiolipin (PC:PG:CA), as indicated, in the presence of 200 µM cAMP. Bars represent means ± SEM for three separate experiments. (C) Representative single-channel recordings of SthK in 0.1 mM intracellular cAMP. (D) I-V relationship of SthK single-channel current amplitude at 100 µM cAMP. (E) Open probability of SthK at 100 mV as a function of the cAMP concentration. Fitting the data with Eq. 10 yields an apparent activation constant of EC 50 = 17 µM and a Hill coefficient of n H = 3. The number of repeats is indicated beside each data point. (F) Open probability of SthK in the presence of 500 µM cAMP as function of the membrane potential. The line indicates the fit according to Eq. 13 , leading to z = 0.8 and V half = 87 mV, Po max = 0.65, and Po min = 0.05. Symbols and error bars in D–F represent means ± SEM from at least three separate bilayers.

    Journal: The Journal of General Physiology

    Article Title: Ligand binding and activation properties of the purified bacterial cyclic nucleotide–gated channel SthK

    doi: 10.1085/jgp.201812023

    Figure Lengend Snippet: Characterization of SthK channel activity. (A) Normalized 86 Rb + flux through SthK (reconstituted in 5:3:2 DOPC:POPG:cardiolipin) in the presence of 200 µM cAMP (red squares), cGMP (blue circles), both cAMP and cGMP (black triangles), and without cyclic nucleotides (open triangles). Flux through empty liposomes (open circles) is shown as a reference. All flux values are normalized to the maximum uptake recorded in the presence of valinomycin. Bars represent means ± SEM for three separate experiments. (B) SthK channel activity represented by the maximum achieved 86 Rb + uptake through SthK reconstituted in liposomes made from 3:1 POPE:POPG (PE:PG) or 5:3:2 DOPC:POPG:cardiolipin (PC:PG:CA), as indicated, in the presence of 200 µM cAMP. Bars represent means ± SEM for three separate experiments. (C) Representative single-channel recordings of SthK in 0.1 mM intracellular cAMP. (D) I-V relationship of SthK single-channel current amplitude at 100 µM cAMP. (E) Open probability of SthK at 100 mV as a function of the cAMP concentration. Fitting the data with Eq. 10 yields an apparent activation constant of EC 50 = 17 µM and a Hill coefficient of n H = 3. The number of repeats is indicated beside each data point. (F) Open probability of SthK in the presence of 500 µM cAMP as function of the membrane potential. The line indicates the fit according to Eq. 13 , leading to z = 0.8 and V half = 87 mV, Po max = 0.65, and Po min = 0.05. Symbols and error bars in D–F represent means ± SEM from at least three separate bilayers.

    Article Snippet: To reconstitute SthK into liposomes, DOPC, POPG, and cardiolipin (Avanti Polar Lipids), dissolved in chloroform, were mixed in a 5:3:2 (wt/wt/wt) ratio and dried under constant N2 flow in disposable glass tubes to a thin layer.

    Techniques: Activity Assay, Concentration Assay, Activation Assay

    Raman spectra in the region of 1620–1700 cm −1 for CerPE ( red ) and three mixtures of CerPE/DOPC (1:1) ( blue ), CerPE /DPPC (1:1) ( green ), and CerPE/Chol (1:1) ( black ). The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Journal: Biophysical Journal

    Article Title: Detection of Sphingomyelin Clusters by Raman Spectroscopy

    doi: 10.1016/j.bpj.2016.07.035

    Figure Lengend Snippet: Raman spectra in the region of 1620–1700 cm −1 for CerPE ( red ) and three mixtures of CerPE/DOPC (1:1) ( blue ), CerPE /DPPC (1:1) ( green ), and CerPE/Chol (1:1) ( black ). The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Article Snippet: We purchased SM (egg, chicken; egg SM; > 80% of the amide-linked fatty acid of egg SM is palmitic acid according to the manufacturer), DPPC, DOPC, N -lauroyl-D- erythro -sphingosylphosphorylcholine (lauroyl SM), N -stearoyl-D- erythro -sphingosylphosphorylcholine (stearoyl SM), and N -palmitoyl-d31-D- erythro -sphingosylphosphorylcholine (d31 SM) from Avanti Polar Lipids (Alabaster, AL); Chol from Sigma (St. Louis, MO); and N -Acyl-sphingosylphosphorylethanolamine (CerPE) from Matreya LLC (Pleasant Gap, PA).

    Techniques:

    Raman spectra of various lipid suspensions. ( A ) Raman spectra of egg SM, egg SM/DOPC (1:1), egg SM/DPPC (1:1), DOPC, and DPPC. ( B ) Raman spectra of the 1620–1720 cm −1 region for egg SM ( red ), egg SM/DOPC (1:1) ( blue ), and egg SM/DPPC (1:1) ( black ). ( C ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DOPC. ( D ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DPPC. The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Journal: Biophysical Journal

    Article Title: Detection of Sphingomyelin Clusters by Raman Spectroscopy

    doi: 10.1016/j.bpj.2016.07.035

    Figure Lengend Snippet: Raman spectra of various lipid suspensions. ( A ) Raman spectra of egg SM, egg SM/DOPC (1:1), egg SM/DPPC (1:1), DOPC, and DPPC. ( B ) Raman spectra of the 1620–1720 cm −1 region for egg SM ( red ), egg SM/DOPC (1:1) ( blue ), and egg SM/DPPC (1:1) ( black ). ( C ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DOPC. ( D ) Concentration dependence of the relative intensities of the trans C=C stretching band ( circle ) and the amide I band ( square ) for a 1:1 mixture of egg SM and DPPC. The Raman spectrum was collected 25 h after sample deposition at 23°C.

    Article Snippet: We purchased SM (egg, chicken; egg SM; > 80% of the amide-linked fatty acid of egg SM is palmitic acid according to the manufacturer), DPPC, DOPC, N -lauroyl-D- erythro -sphingosylphosphorylcholine (lauroyl SM), N -stearoyl-D- erythro -sphingosylphosphorylcholine (stearoyl SM), and N -palmitoyl-d31-D- erythro -sphingosylphosphorylcholine (d31 SM) from Avanti Polar Lipids (Alabaster, AL); Chol from Sigma (St. Louis, MO); and N -Acyl-sphingosylphosphorylethanolamine (CerPE) from Matreya LLC (Pleasant Gap, PA).

    Techniques: Concentration Assay

    Pre-proccesing of spectra and selection of appropriate wavelengths . A) Raw fluorescence emission spectra of various AChR-free liposomes with varying molar ratios of DOPA/DOPC (ranging from 0 to 60%) and two AChR-containing liposomes with DOPA/DOPC (20:40). Two replicas from independent experiments are shown. In all samples, NBD-Chol and PyPC concentrations were kept at 40 and 5%, respectively. The final lipid concentration and the lipid to protein molar ratio in the AChR-containing liposomes were 40 μM and 500:1, respectively. Excitation wavelength = 340 nm. Temperature = 25°C. B) Pre-processed spectra obtained by smoothing throughout the Savitsky-Golay procedure (with a window width of 8 points and a second order polynomial fit) and normalizing to the highest value of each spectrum (corresponding to the first PyPC emission band at 374 nm). The wavelengths further employed for the multivariate analysis are outlined in the dotted rectangle. It is clear that the sixteen spectra in each panel are difficult to identify due to their high degree of overlap; this is precisely what multivariate analysis dissects so effectively. Where possible, spectra have been identified with the sample numbers appearing in Table 1 .

    Journal: PMC Biophysics

    Article Title: Resolution of complex fluorescence spectra of lipids and nicotinic acetylcholine receptor by multivariate analysis reveals protein-mediated effects on the receptor's immediate lipid microenvironment

    doi: 10.1186/1757-5036-1-6

    Figure Lengend Snippet: Pre-proccesing of spectra and selection of appropriate wavelengths . A) Raw fluorescence emission spectra of various AChR-free liposomes with varying molar ratios of DOPA/DOPC (ranging from 0 to 60%) and two AChR-containing liposomes with DOPA/DOPC (20:40). Two replicas from independent experiments are shown. In all samples, NBD-Chol and PyPC concentrations were kept at 40 and 5%, respectively. The final lipid concentration and the lipid to protein molar ratio in the AChR-containing liposomes were 40 μM and 500:1, respectively. Excitation wavelength = 340 nm. Temperature = 25°C. B) Pre-processed spectra obtained by smoothing throughout the Savitsky-Golay procedure (with a window width of 8 points and a second order polynomial fit) and normalizing to the highest value of each spectrum (corresponding to the first PyPC emission band at 374 nm). The wavelengths further employed for the multivariate analysis are outlined in the dotted rectangle. It is clear that the sixteen spectra in each panel are difficult to identify due to their high degree of overlap; this is precisely what multivariate analysis dissects so effectively. Where possible, spectra have been identified with the sample numbers appearing in Table 1 .

    Article Snippet: DOPA, DOPC and Chol were obtained from Avanti Polar Lipids, Inc (Alabaster, AL).

    Techniques: Selection, Fluorescence, Concentration Assay

    Förster resonance energy transfer (FRET) from the AChR . Smoothened fluorescence emission spectrum of an AChR PyPC-containing sample at 25°C showing the areas (A1 and A2) used to evaluate FRET. The dotted line indicates the average boundary wavelength at which the absolute value of the first derivative of the spectrum passed through a minimum. Excitation wavelength = 290 nm. Inset: FRET from AChR to PyPC as a function of temperature. FRET was calculated according to [1-(A 1 /A 2 )]. Liposomes contained DOPA/DOPC/NBD-Chol at a molar fraction 20/40/40 and a lipid to protein molar ratio of 500:1. PyPC concentration was 5 mol%. Error bars represent the S.D. of two independent samples.

    Journal: PMC Biophysics

    Article Title: Resolution of complex fluorescence spectra of lipids and nicotinic acetylcholine receptor by multivariate analysis reveals protein-mediated effects on the receptor's immediate lipid microenvironment

    doi: 10.1186/1757-5036-1-6

    Figure Lengend Snippet: Förster resonance energy transfer (FRET) from the AChR . Smoothened fluorescence emission spectrum of an AChR PyPC-containing sample at 25°C showing the areas (A1 and A2) used to evaluate FRET. The dotted line indicates the average boundary wavelength at which the absolute value of the first derivative of the spectrum passed through a minimum. Excitation wavelength = 290 nm. Inset: FRET from AChR to PyPC as a function of temperature. FRET was calculated according to [1-(A 1 /A 2 )]. Liposomes contained DOPA/DOPC/NBD-Chol at a molar fraction 20/40/40 and a lipid to protein molar ratio of 500:1. PyPC concentration was 5 mol%. Error bars represent the S.D. of two independent samples.

    Article Snippet: DOPA, DOPC and Chol were obtained from Avanti Polar Lipids, Inc (Alabaster, AL).

    Techniques: Förster Resonance Energy Transfer, Fluorescence, Concentration Assay

    The effect of cholesterol content on DNA-liposome concentration. Colocalisation scores and standard deviations are shown for Alexa647-labelled cholesterol-tagged ssDNA (pink), cholesterol-tagged dsDNA (blue) and cholesterol-tagged dsDNA with a 6 nt overhang (green) as well as dsDNA with no cholesterol tag (yellow) and ssDNA with no cholesterol tag (orange) and rhodamine-labelled DOPE/DOPC liposomes (a) or DPhPC liposomes (b) prepared from lipid stocks containing 0, 10, 20, 30 or 40% cholesterol.

    Journal: bioRxiv

    Article Title: Optimised assembly of DNA-lipid nanostructures

    doi: 10.1101/2020.06.01.128686

    Figure Lengend Snippet: The effect of cholesterol content on DNA-liposome concentration. Colocalisation scores and standard deviations are shown for Alexa647-labelled cholesterol-tagged ssDNA (pink), cholesterol-tagged dsDNA (blue) and cholesterol-tagged dsDNA with a 6 nt overhang (green) as well as dsDNA with no cholesterol tag (yellow) and ssDNA with no cholesterol tag (orange) and rhodamine-labelled DOPE/DOPC liposomes (a) or DPhPC liposomes (b) prepared from lipid stocks containing 0, 10, 20, 30 or 40% cholesterol.

    Article Snippet: Liposomes with cholesterol were prepared by replacing either DPhPC or equal parts of DOPE and DOPC with cholesterol [700000P Avanti Polar Lipids].

    Techniques: Concentration Assay

    The effect of NaCl, MgCl 2 and pH on DNA-liposome colocalisation. Colocalisation scores and standard deviations are shown for Alexa647-labelled cholesterol-tagged single stranded DNA (ssDNA, pink), cholesterol-tagged double stranded DNA (dsDNA, blue) and cholesterol-tagged double stranded DNA with a 6 nt overhang (dsDNA-6nt, green) as well as dsDNA with no cholesterol tag (yellow) and ssDNA with no cholesterol tag (orange) and rhodamine-labelled DOPE/DOPC liposomes (left column, a/c/e) and DPhPC liposomes (right column, b/d/f). Conditions tested included extrusion buffer [NaCl] containing 12.5, 25, 50, 100, 200 and 400 mM NaCl (a/b), extrusion buffer [MgCl 2 ] containing 0, 10, 20, 40 and 80 mM MgCl 2 (c/d) and extrusion buffer [pH] adjusted to pH values of 2, 4, 6, 7, 8 and 10 (e/f).

    Journal: bioRxiv

    Article Title: Optimised assembly of DNA-lipid nanostructures

    doi: 10.1101/2020.06.01.128686

    Figure Lengend Snippet: The effect of NaCl, MgCl 2 and pH on DNA-liposome colocalisation. Colocalisation scores and standard deviations are shown for Alexa647-labelled cholesterol-tagged single stranded DNA (ssDNA, pink), cholesterol-tagged double stranded DNA (dsDNA, blue) and cholesterol-tagged double stranded DNA with a 6 nt overhang (dsDNA-6nt, green) as well as dsDNA with no cholesterol tag (yellow) and ssDNA with no cholesterol tag (orange) and rhodamine-labelled DOPE/DOPC liposomes (left column, a/c/e) and DPhPC liposomes (right column, b/d/f). Conditions tested included extrusion buffer [NaCl] containing 12.5, 25, 50, 100, 200 and 400 mM NaCl (a/b), extrusion buffer [MgCl 2 ] containing 0, 10, 20, 40 and 80 mM MgCl 2 (c/d) and extrusion buffer [pH] adjusted to pH values of 2, 4, 6, 7, 8 and 10 (e/f).

    Article Snippet: Liposomes with cholesterol were prepared by replacing either DPhPC or equal parts of DOPE and DOPC with cholesterol [700000P Avanti Polar Lipids].

    Techniques: