avanti mini extruder Avanti Polar Search Results


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  • 95
    Millipore lipid solution
    Lipid Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 72 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    lipid solution - by Bioz Stars, 2020-02
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    77
    Avanti Polar avanti mini extruder avanti polar lipids
    Avanti Mini Extruder Avanti Polar Lipids, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 77/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Avanti Polar mini extruder liposome extrusion apparatus
    Mini Extruder Liposome Extrusion Apparatus, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 77/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Avanti Polar avanti mini extruder
    Avanti Mini Extruder, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 99/100, based on 452 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Avanti Polar mini extrusion device
    Mini Extrusion Device, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 79 stars, based on 4 article reviews
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    78
    Avanti Polar extrusion membranes
    Extrusion Membranes, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 78/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 78 stars, based on 2 article reviews
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    extrusion membranes - by Bioz Stars, 2020-02
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    88
    Avanti Polar mini extruder apparatus
    Mini Extruder Apparatus, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 88/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Avanti Polar mini extruder kit
    Mini Extruder Kit, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 91/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 37 article reviews
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    91
    Avanti Polar mini extruder device
    Mini Extruder Device, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 91/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 27 article reviews
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    79
    Avanti Polar syringe mini extruder
    Syringe Mini Extruder, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 79 stars, based on 5 article reviews
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    78
    Avanti Polar size extrusion steps
    Size Extrusion Steps, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 78/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 78 stars, based on 10 article reviews
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    79
    Avanti Polar phospholipid vesicle generation
    Phospholipid Vesicle Generation, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 79 stars, based on 5 article reviews
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    76
    Avanti Polar syringe type mini extruder
    Syringe Type Mini Extruder, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 76 stars, based on 1 article reviews
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    93
    Avanti Polar extruder
    Extruder, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 93/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Avanti Polar handheld extruder set
    Handheld Extruder Set, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 79/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 79 stars, based on 7 article reviews
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    96
    Avanti Polar membrane
    Membrane, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 96/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Avanti Polar avanti polar lipid
    Avanti Polar Lipid, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 99/100, based on 350 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    75
    Avanti Polar mini extrusion syringe device
    Mini Extrusion Syringe Device, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Avanti Polar polycarbonate membrane
    Polycarbonate Membrane, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 99/100, based on 441 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Avanti Polar 100 nm pore size filter
    100 Nm Pore Size Filter, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 88/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Avanti Polar polycarbonate filters
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
    Polycarbonate Filters, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 96/100, based on 327 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    75
    Avanti Polar mini extruder system
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
    Mini Extruder System, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 75/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 75 stars, based on 2 article reviews
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    83
    Avanti Polar hand held mini extrusion device
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
    Hand Held Mini Extrusion Device, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 83/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 83 stars, based on 12 article reviews
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    hand held mini extrusion device - by Bioz Stars, 2020-02
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    78
    GE Healthcare nuclepore extrusion filter membranes
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
    Nuclepore Extrusion Filter Membranes, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 78 stars, based on 4 article reviews
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    75
    Avanti Polar mini handheld extruder kit
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
    Mini Handheld Extruder Kit, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 75/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 75 stars, based on 1 article reviews
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    80
    Avanti Polar handheld mini extruder
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
    Handheld Mini Extruder, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    handheld mini extruder - by Bioz Stars, 2020-02
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    Avanti Polar 100 nm membrane
    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
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    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.
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    Electrophysiological and cryo-EM analysis. A , ΔCR_PrP with a membrane anchor induces spontaneous inward currents in HEK293 cells. Representative whole-cell patch clamp recordings are shown. HEK293 cells were clamped from a holding potential of 0 mV to a test potential of <t>−100</t> mV for 10 s every 30 s. After a control phase, the indicated proteins were added directly to the bath solution. In the presence of FL_PrP-MA ( left ) and ΔCR_PrP without a membrane anchor ( middle ), no or only weak pore forming activity was observed, whereas ΔCR_PrP-MA induced large sodium ( top right ) and calcium ( bottom right ) inward currents. B , cryo-EM images of POPG vesicles ( arrows ) mixed with ΔCR_PrP-MA ( left ) and POPG vesicles alone ( right ). The scale bar is 100 nm.
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    Electrophysiological and cryo-EM analysis. A , ΔCR_PrP with a membrane anchor induces spontaneous inward currents in HEK293 cells. Representative whole-cell patch clamp recordings are shown. HEK293 cells were clamped from a holding potential of 0 mV to a test potential of <t>−100</t> mV for 10 s every 30 s. After a control phase, the indicated proteins were added directly to the bath solution. In the presence of FL_PrP-MA ( left ) and ΔCR_PrP without a membrane anchor ( middle ), no or only weak pore forming activity was observed, whereas ΔCR_PrP-MA induced large sodium ( top right ) and calcium ( bottom right ) inward currents. B , cryo-EM images of POPG vesicles ( arrows ) mixed with ΔCR_PrP-MA ( left ) and POPG vesicles alone ( right ). The scale bar is 100 nm.
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    Electrophysiological and cryo-EM analysis. A , ΔCR_PrP with a membrane anchor induces spontaneous inward currents in HEK293 cells. Representative whole-cell patch clamp recordings are shown. HEK293 cells were clamped from a holding potential of 0 mV to a test potential of <t>−100</t> mV for 10 s every 30 s. After a control phase, the indicated proteins were added directly to the bath solution. In the presence of FL_PrP-MA ( left ) and ΔCR_PrP without a membrane anchor ( middle ), no or only weak pore forming activity was observed, whereas ΔCR_PrP-MA induced large sodium ( top right ) and calcium ( bottom right ) inward currents. B , cryo-EM images of POPG vesicles ( arrows ) mixed with ΔCR_PrP-MA ( left ) and POPG vesicles alone ( right ). The scale bar is 100 nm.
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    Electrophysiological and cryo-EM analysis. A , ΔCR_PrP with a membrane anchor induces spontaneous inward currents in HEK293 cells. Representative whole-cell patch clamp recordings are shown. HEK293 cells were clamped from a holding potential of 0 mV to a test potential of <t>−100</t> mV for 10 s every 30 s. After a control phase, the indicated proteins were added directly to the bath solution. In the presence of FL_PrP-MA ( left ) and ΔCR_PrP without a membrane anchor ( middle ), no or only weak pore forming activity was observed, whereas ΔCR_PrP-MA induced large sodium ( top right ) and calcium ( bottom right ) inward currents. B , cryo-EM images of POPG vesicles ( arrows ) mixed with ΔCR_PrP-MA ( left ) and POPG vesicles alone ( right ). The scale bar is 100 nm.
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    Image Search Results


    Identifying the minimal machinery required for SNX9-regulated actin assembly.  (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2  + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2  alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.

    Journal: The Journal of Cell Biology

    Article Title: Control of actin polymerization via the coincidence of phosphoinositides and high membrane curvature

    doi: 10.1083/jcb.201704061

    Figure Lengend Snippet: Identifying the minimal machinery required for SNX9-regulated actin assembly. (A) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2 + 1% PI(3)P (with 48% PC and 47% PS) assayed by pyrene actin assay in the minimal reconstituted system (20 nM Arp2/3 complex, 500 nM Cdc42⋅GTP-γS, 100 nM N-WASP/WIP complex, 100 nM SNX9, and 1 µM actin, 65:35 pyrene actin) compared with 4% PI(4,5)P 2 alone, actin alone, and activation by GST-VCA fragment from N-WASP as a positive control. Data show the mean of eight traces. AU, arbitrary units. (B) Maximal rates from two technical repeats each of four independent experiments showing the mean and SEM. The maximal rates were normalized against 100% activation by GST-VCA. Significance was tested using an ANOVA test with a Tukey's multiple comparison post-hoc test; actin versus PI(4,5)P 2 : P = 0.900; actin versus PI(4,5)P 2 /PI(3)P: ***, P = 0.001; actin versus −Cdc42: P = 0.9000. ns, not significant. (C) Direct observation of liposomes (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing 50 nM Arp2/3 complex, 50 nM Cdc42⋅GTP-γS, 100 nM N-WASP–WIP complex, 100 nM SNX9, 8 µM unlabeled actin, and 0.3 µM Alexa Fluor 647–labeled actin. Actin asters form at the surface of highly curved liposomes only when all components are present. (D) Activation of Cdc42 is needed. Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm (4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, 30% PS; purple) in the presence of the minimal purified system containing Cdc42⋅GDP. (C and D) Bars, 3 µm. (E) Electron micrograph of actin asters after incubation of PI(4,5)P 2 /PI(3)P liposomes with the minimal purified system shows disordered and branched actin filaments. Bar, 100 nm. (F–I) All components of the purified system are required for efficient actin polymerization. No actin polymerization is seen with the minimal purified system minus each individual component: Cdc42⋅GTP-γS (F), SNX9 (G), N-WASP–WIP (H), or Arp2/3 complex (I). Bars, 6 µm.

    Article Snippet: In parallel, large unilamellar vesicles and small unilamellar vesicles were prepared from the same sample by freeze/thawing as above eight times, followed by extrusion 15 times, initially through an 800-nm polycarbonate filter and then a 50-nm polycarbonate filter (Mini-Extruder; Avanti Polar Lipids).

    Techniques: Activation Assay, Pyrene Actin Assay, Positive Control, Purification, Labeling, Incubation

    PI(4,5)P 2  and PI(3)P signal actin polymerization via SNX9.  (A) Cascade of phosphoinositide lipid conversion steps during endocytosis: dephosphorylation of PI(4,5)P 2  to PI(4)P by synaptojanin, phosphorylation by PI 3-kinase to produce PI(3,4)P 2 , and dephosphorylation by INPP4A to form the PI(3)P signal characteristic of the early endosome. (B) Schematic diagram of our cell-free assay for phosphoinositide environment in actin polymerization. Competitive assay that examines phosphoinositide preferences (PI(4,5)P 2  + PI(3)P or PI(4,5)P 2  + PI(3,4)P 2 ) in the range of curvatures at a budding CCP. (C) Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm. Rhodamine fluorescence was used for 4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, and 30% PS liposomes (all percentages by molecular fraction, purple) and NBD for 4% PI(4,5)P 2 , 1% PI(3,4)P 2 , 65% PC, and 30% PS (cyan) using spinning-disk confocal microscopy. (D) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2 , 1% PI(3)P, 48% PC, and 47% PS assayed by pyrene actin assay with HSS compared with 4% PI(4,5)P 2  alone or 4% PI(4,5)P 2  + 1% PI(3,4)P 2 . Data show mean of four traces from two independent experiments. AU, arbitrary units. (E) As in C, except 10% PI(3,4)P 2  (cyan). (F) 10% PI(3,4)P 2  liposomes (cyan), extracts + SNX9. In all experiments, we exclusively observed the formation of comet tail at the surface of PI(4,5)P 2 /PI(3)P liposomes. (G) 10% PI(3,4)P 2  liposomes (cyan) preincubated with INPP4A. Actin polymerization occurred from the cyan liposomes. Bars, 3 µm.

    Journal: The Journal of Cell Biology

    Article Title: Control of actin polymerization via the coincidence of phosphoinositides and high membrane curvature

    doi: 10.1083/jcb.201704061

    Figure Lengend Snippet: PI(4,5)P 2 and PI(3)P signal actin polymerization via SNX9. (A) Cascade of phosphoinositide lipid conversion steps during endocytosis: dephosphorylation of PI(4,5)P 2 to PI(4)P by synaptojanin, phosphorylation by PI 3-kinase to produce PI(3,4)P 2 , and dephosphorylation by INPP4A to form the PI(3)P signal characteristic of the early endosome. (B) Schematic diagram of our cell-free assay for phosphoinositide environment in actin polymerization. Competitive assay that examines phosphoinositide preferences (PI(4,5)P 2 + PI(3)P or PI(4,5)P 2 + PI(3,4)P 2 ) in the range of curvatures at a budding CCP. (C) Direct observation of liposome samples with a continuous size distribution from 50 nm to 5 µm. Rhodamine fluorescence was used for 4% PI(4,5)P 2 , 1% PI(3)P, 65% PC, and 30% PS liposomes (all percentages by molecular fraction, purple) and NBD for 4% PI(4,5)P 2 , 1% PI(3,4)P 2 , 65% PC, and 30% PS (cyan) using spinning-disk confocal microscopy. (D) Maximal activation of actin polymerization by liposomes containing 4% PI(4,5)P 2 , 1% PI(3)P, 48% PC, and 47% PS assayed by pyrene actin assay with HSS compared with 4% PI(4,5)P 2 alone or 4% PI(4,5)P 2 + 1% PI(3,4)P 2 . Data show mean of four traces from two independent experiments. AU, arbitrary units. (E) As in C, except 10% PI(3,4)P 2 (cyan). (F) 10% PI(3,4)P 2 liposomes (cyan), extracts + SNX9. In all experiments, we exclusively observed the formation of comet tail at the surface of PI(4,5)P 2 /PI(3)P liposomes. (G) 10% PI(3,4)P 2 liposomes (cyan) preincubated with INPP4A. Actin polymerization occurred from the cyan liposomes. Bars, 3 µm.

    Article Snippet: In parallel, large unilamellar vesicles and small unilamellar vesicles were prepared from the same sample by freeze/thawing as above eight times, followed by extrusion 15 times, initially through an 800-nm polycarbonate filter and then a 50-nm polycarbonate filter (Mini-Extruder; Avanti Polar Lipids).

    Techniques: De-Phosphorylation Assay, Cell-Free Assay, Fluorescence, Confocal Microscopy, Activation Assay, Pyrene Actin Assay

    Electrophysiological and cryo-EM analysis. A , ΔCR_PrP with a membrane anchor induces spontaneous inward currents in HEK293 cells. Representative whole-cell patch clamp recordings are shown. HEK293 cells were clamped from a holding potential of 0 mV to a test potential of −100 mV for 10 s every 30 s. After a control phase, the indicated proteins were added directly to the bath solution. In the presence of FL_PrP-MA ( left ) and ΔCR_PrP without a membrane anchor ( middle ), no or only weak pore forming activity was observed, whereas ΔCR_PrP-MA induced large sodium ( top right ) and calcium ( bottom right ) inward currents. B , cryo-EM images of POPG vesicles ( arrows ) mixed with ΔCR_PrP-MA ( left ) and POPG vesicles alone ( right ). The scale bar is 100 nm.

    Journal: The Journal of Biological Chemistry

    Article Title: A C-terminal Membrane Anchor Affects the Interactions of Prion Proteins with Lipid Membranes *

    doi: 10.1074/jbc.M114.587345

    Figure Lengend Snippet: Electrophysiological and cryo-EM analysis. A , ΔCR_PrP with a membrane anchor induces spontaneous inward currents in HEK293 cells. Representative whole-cell patch clamp recordings are shown. HEK293 cells were clamped from a holding potential of 0 mV to a test potential of −100 mV for 10 s every 30 s. After a control phase, the indicated proteins were added directly to the bath solution. In the presence of FL_PrP-MA ( left ) and ΔCR_PrP without a membrane anchor ( middle ), no or only weak pore forming activity was observed, whereas ΔCR_PrP-MA induced large sodium ( top right ) and calcium ( bottom right ) inward currents. B , cryo-EM images of POPG vesicles ( arrows ) mixed with ΔCR_PrP-MA ( left ) and POPG vesicles alone ( right ). The scale bar is 100 nm.

    Article Snippet: The lipid solution was passed 20 times through a mini-extruder with a 100-nm polycarbonate membrane (Avanti Polar Lipids).

    Techniques: Patch Clamp, Activity Assay