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  • 95
    Millipore folch lipids
    Folch Lipids, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore folch solution
    Folch Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore folch liposomes
    Membrane deformation by human pacsin isoforms. A. Domain organization and structure of pacsin-1. The structure shows a F-BAR domain dimer with the protomers shown in green and orange, respectively. B. SAXS-based comparison of full-length pacsin-1 in solution and in crystals. Distant distribution functions, Rg and Dmax values were determined based on the full-length crystal structure [28] and the solution scattering data [27] . R g /D max (crystal) = 212/60 Å; R g /D max (SAXS) = 215/58 Å. Discrepancies between the respective distance distribution functions can be explained by the flexible linkers that connect the F-BAR and SH3 domains and were not modeled in the crystal structures. C. Negative-stain electron micrographs. The membrane deformation potential of human pacsin isoforms and their isolated F-BAR domains was monitored by EM. <t>Folch</t> <t>fraction</t> I liposomes were incubated with purified proteins (5–10 µM), and processed as described in Materials and Methods. Arrows indicate specific membrane morphologies (solid arrows, pearling structures; dashed arrows, narrow tubules; open triangles, wide tubules). Inset shows liposome-only control; scale bar, 100 nm.
    Folch Liposomes, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/folch liposomes/product/Millipore
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    94
    Millipore folch fraction i
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Folch Fraction I, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Jordi Labs jordi folch pi
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Jordi Folch Pi, supplied by Jordi Labs, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore deformation assay brain derived folch lipids
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Deformation Assay Brain Derived Folch Lipids, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    FUJIFILM folch solution
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Folch Solution, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Avanti Polar folch brain derived lipids
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Folch Brain Derived Lipids, supplied by Avanti Polar, used in various techniques. Bioz Stars score: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher folch extraction
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Folch Extraction, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore folch lipid fraction i
    Nucleotide-dependent liposome binding of hGBP1. <t>Cosedimentation</t> assays of hGBP1 with <t>folch</t> liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).
    Folch Lipid Fraction I, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Membrane deformation by human pacsin isoforms. A. Domain organization and structure of pacsin-1. The structure shows a F-BAR domain dimer with the protomers shown in green and orange, respectively. B. SAXS-based comparison of full-length pacsin-1 in solution and in crystals. Distant distribution functions, Rg and Dmax values were determined based on the full-length crystal structure [28] and the solution scattering data [27] . R g /D max (crystal) = 212/60 Å; R g /D max (SAXS) = 215/58 Å. Discrepancies between the respective distance distribution functions can be explained by the flexible linkers that connect the F-BAR and SH3 domains and were not modeled in the crystal structures. C. Negative-stain electron micrographs. The membrane deformation potential of human pacsin isoforms and their isolated F-BAR domains was monitored by EM. Folch fraction I liposomes were incubated with purified proteins (5–10 µM), and processed as described in Materials and Methods. Arrows indicate specific membrane morphologies (solid arrows, pearling structures; dashed arrows, narrow tubules; open triangles, wide tubules). Inset shows liposome-only control; scale bar, 100 nm.

    Journal: PLoS ONE

    Article Title: Versatile Membrane Deformation Potential of Activated Pacsin

    doi: 10.1371/journal.pone.0051628

    Figure Lengend Snippet: Membrane deformation by human pacsin isoforms. A. Domain organization and structure of pacsin-1. The structure shows a F-BAR domain dimer with the protomers shown in green and orange, respectively. B. SAXS-based comparison of full-length pacsin-1 in solution and in crystals. Distant distribution functions, Rg and Dmax values were determined based on the full-length crystal structure [28] and the solution scattering data [27] . R g /D max (crystal) = 212/60 Å; R g /D max (SAXS) = 215/58 Å. Discrepancies between the respective distance distribution functions can be explained by the flexible linkers that connect the F-BAR and SH3 domains and were not modeled in the crystal structures. C. Negative-stain electron micrographs. The membrane deformation potential of human pacsin isoforms and their isolated F-BAR domains was monitored by EM. Folch fraction I liposomes were incubated with purified proteins (5–10 µM), and processed as described in Materials and Methods. Arrows indicate specific membrane morphologies (solid arrows, pearling structures; dashed arrows, narrow tubules; open triangles, wide tubules). Inset shows liposome-only control; scale bar, 100 nm.

    Article Snippet: Negative Staining Electron Microscopy (EM) Liposomes (1 mg/ml) made from Folch fraction I (bovine) brain lipids (Sigma) or synthetic lipids (27.5/27.5/45 = POPC/POPE/POPS, Avanti Polar Lipids, Inc.) were incubated in the presence or absence of proteins (5–10 μM, unless indicated otherwise) in low salt buffer for 5 min at room temperature.

    Techniques: Staining, Isolation, Incubation, Purification

    Nucleotide-dependent liposome binding of hGBP1. Cosedimentation assays of hGBP1 with folch liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).

    Journal: Journal of Lipid Research

    Article Title: Purification of the CaaX-modified, dynamin-related large GTPase hGBP1 by coexpression with farnesyltransferase [S]

    doi: 10.1194/jlr.D005397

    Figure Lengend Snippet: Nucleotide-dependent liposome binding of hGBP1. Cosedimentation assays of hGBP1 with folch liposomes were analyzed by SDS-PAGE and Coomassie staining. S, supernatant and P, pellet. A: Farnesylated hGBP1 was incubated with or without liposomes in buffer containing 130 mM KCl. Where indicated, guanine nucleotides were added at 200 µM and, additionally, 300 µM AlCl 3 and 10 mM NaF in the case of GDP * AlFx. Association with liposomes was observed only for farnesylated hGBP1 and in the presence of GDP * AlFx but not with GMP, GDP, GTP, or the nonhydrolyzable GTP analog GTPγS. B: Unmodified hGBP1 bound only in low salt conditions and in the presence of GDP * AlFx (left panel). The association of farnesylated hGBP1 with liposomes and in the presence of GDP * AlFx was observed under all salt conditions tested (right panel).

    Article Snippet: Lipid vesicle preparation and cosedimentation assay Folch fraction I brain lipid extract (Sigma-Aldrich) was dissolved in chloroform and stored at −80°C.

    Techniques: Binding Assay, SDS Page, Staining, Incubation

    Rac1 Ic activation on liposomes by different Dbl family proteins and association with Pak1. ( A ) Differential binding of Vav2, Dbl, TrioN, Tiam1 and P-Rex1 to various liposomes. Lipo +PIP2 is composed of PE, PC, PS, SM and PIP2. In Lipo +PIP3 , PIP2 is replaced by PIP3. ( B ) Efficient Rac1 activation by Dbl and Vav2 on Lipo +PIP2 . ( C ) Displacement from the GDI1 complex, activation by GEFs and association of Rac1 Ic with liposomes and Pak1. ( D ) Tiam1 but not Rac1 Ic binding to Folch III. Rac1GDP, Pak1, Tiam1, GppNHp and different liposomes were preincubated, afterwards the liposome sedimentation assay was conducted. Rac1, PAKα and Tiam1 from the liposome pellet were detected by GST antibody. ( E ) Rac1 Ic repulsion by PC but not PS. Liposomes (PS and PE or PC and PE) at increasing amounts of PS and PC were sedimented after incubation with Rac1 Ic . (F) Thin layer chromatography of Folch I and Folch III liposomes. Relative lipid content of Folch I and Folch III liposomes was analyzed by thin layer chromatography. PE, PS and PC as well as Folch III containing PS and PS were used as controls. CBB, coomassie brilliant blue; Ec , E. coli ; Ic, insect cells; P, liposome pellet; S, supernatant.

    Journal: PLoS ONE

    Article Title: Liposome Reconstitution and Modulation of Recombinant Prenylated Human Rac1 by GEFs, GDI1 and Pak1

    doi: 10.1371/journal.pone.0102425

    Figure Lengend Snippet: Rac1 Ic activation on liposomes by different Dbl family proteins and association with Pak1. ( A ) Differential binding of Vav2, Dbl, TrioN, Tiam1 and P-Rex1 to various liposomes. Lipo +PIP2 is composed of PE, PC, PS, SM and PIP2. In Lipo +PIP3 , PIP2 is replaced by PIP3. ( B ) Efficient Rac1 activation by Dbl and Vav2 on Lipo +PIP2 . ( C ) Displacement from the GDI1 complex, activation by GEFs and association of Rac1 Ic with liposomes and Pak1. ( D ) Tiam1 but not Rac1 Ic binding to Folch III. Rac1GDP, Pak1, Tiam1, GppNHp and different liposomes were preincubated, afterwards the liposome sedimentation assay was conducted. Rac1, PAKα and Tiam1 from the liposome pellet were detected by GST antibody. ( E ) Rac1 Ic repulsion by PC but not PS. Liposomes (PS and PE or PC and PE) at increasing amounts of PS and PC were sedimented after incubation with Rac1 Ic . (F) Thin layer chromatography of Folch I and Folch III liposomes. Relative lipid content of Folch I and Folch III liposomes was analyzed by thin layer chromatography. PE, PS and PC as well as Folch III containing PS and PS were used as controls. CBB, coomassie brilliant blue; Ec , E. coli ; Ic, insect cells; P, liposome pellet; S, supernatant.

    Article Snippet: Phosphatidylserine (PS), Phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM), phosphatidylinositol 4,5-bisphosphate (PIP2), and Folch I and Folch III brain lipid extracts were purchased from Sigma-Aldrich (Munich, Germany).

    Techniques: Activation Assay, Binding Assay, Sedimentation, Incubation, Thin Layer Chromatography