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e coli polar lipid extract phospholipids  (Croda International Plc)

 
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    Croda International Plc e coli polar lipid extract phospholipids
    (A) Membrane fusion of TatABC proteoliposomes with MPIase liposomes enabled the detection of the SufI translocation. INV, prepared from BL21/pT7-TatABC, were solubilized with OG, and then mixed with purified F 0 F 1 -ATPase. The proteoliposomes were then formed by removing the detergent. PL/DAG liposomes or PL/DAG/MPIase liposomes were fused to the reconstituted proteoliposomes. SufI translocation was performed co-translationally (left) or post-translationally (right) in the presence of these proteoliposomes. SufI(RR) (top left) or SufI(KK) (bottom left) was used as the substrate. One-ninth of the reaction mixture was analyzed as the translation standard (-) for the co-translational reactions. For the post-translational reactions, ATP was added as indicated. Translocation activities are shown at the bottom of the left panels. (B) Purification of F 0 F 1 -ATPase and the Tat components. F 0 F 1 -ATPase from a thermophilic Bacillus PS3 (left), and <t>E.</t> <t>coli</t> TatA-His (lane 1), TatB-His (lane 2), and TatC-His (lane 3) (right) were subjected to SDS-PAGE, followed by Coomassie Brilliant Blue staining. (C, D) Complete reconstitution of the TAT system using the purified components. (C) Purified TatA, TatB, and TatC (in a 1:1:1 ratio) and F 0 F 1 -ATPase were mixed with <t>phospholipids.</t> Then, detergent was removed to form proteoliposomes. The reconstituted proteoliposomes were then fused with PL/DAG liposomes or PL/DAG/MPIase liposomes. Translocation activity was assayed with SufI(RR) (left) or SufI(KK) (right). (D) Proteoliposomes were reconstituted with the indicated components, followed by TorA-GFP translocation. The TatA:TatB:TatC ratio was 10:1:1. CCCP (20 μM), a protonophore, was added to the sample on the left. TorA-GFP(RR) (top) or TorA-GFP(KK) (bottom) was used as the substrate. Translocation activities are shown at the bottom of each gel.
    E Coli Polar Lipid Extract Phospholipids, supplied by Croda International Plc, used in various techniques. Bioz Stars score: 92/100, based on 1025 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/phospholipids/E%2E+coli+Extract+Polar/bio_rxiv__64898__2026__06__05__730299-226-1-14
    Average 92 stars, based on 1025 article reviews
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    Images

    1) Product Images from "Glycolipid MPIase is essential for the TAT (Twin-Arginine Translocation) pathway"

    Article Title: Glycolipid MPIase is essential for the TAT (Twin-Arginine Translocation) pathway

    Journal: bioRxiv

    doi: 10.64898/2026.06.05.730299

    (A) Membrane fusion of TatABC proteoliposomes with MPIase liposomes enabled the detection of the SufI translocation. INV, prepared from BL21/pT7-TatABC, were solubilized with OG, and then mixed with purified F 0 F 1 -ATPase. The proteoliposomes were then formed by removing the detergent. PL/DAG liposomes or PL/DAG/MPIase liposomes were fused to the reconstituted proteoliposomes. SufI translocation was performed co-translationally (left) or post-translationally (right) in the presence of these proteoliposomes. SufI(RR) (top left) or SufI(KK) (bottom left) was used as the substrate. One-ninth of the reaction mixture was analyzed as the translation standard (-) for the co-translational reactions. For the post-translational reactions, ATP was added as indicated. Translocation activities are shown at the bottom of the left panels. (B) Purification of F 0 F 1 -ATPase and the Tat components. F 0 F 1 -ATPase from a thermophilic Bacillus PS3 (left), and E. coli TatA-His (lane 1), TatB-His (lane 2), and TatC-His (lane 3) (right) were subjected to SDS-PAGE, followed by Coomassie Brilliant Blue staining. (C, D) Complete reconstitution of the TAT system using the purified components. (C) Purified TatA, TatB, and TatC (in a 1:1:1 ratio) and F 0 F 1 -ATPase were mixed with phospholipids. Then, detergent was removed to form proteoliposomes. The reconstituted proteoliposomes were then fused with PL/DAG liposomes or PL/DAG/MPIase liposomes. Translocation activity was assayed with SufI(RR) (left) or SufI(KK) (right). (D) Proteoliposomes were reconstituted with the indicated components, followed by TorA-GFP translocation. The TatA:TatB:TatC ratio was 10:1:1. CCCP (20 μM), a protonophore, was added to the sample on the left. TorA-GFP(RR) (top) or TorA-GFP(KK) (bottom) was used as the substrate. Translocation activities are shown at the bottom of each gel.
    Figure Legend Snippet: (A) Membrane fusion of TatABC proteoliposomes with MPIase liposomes enabled the detection of the SufI translocation. INV, prepared from BL21/pT7-TatABC, were solubilized with OG, and then mixed with purified F 0 F 1 -ATPase. The proteoliposomes were then formed by removing the detergent. PL/DAG liposomes or PL/DAG/MPIase liposomes were fused to the reconstituted proteoliposomes. SufI translocation was performed co-translationally (left) or post-translationally (right) in the presence of these proteoliposomes. SufI(RR) (top left) or SufI(KK) (bottom left) was used as the substrate. One-ninth of the reaction mixture was analyzed as the translation standard (-) for the co-translational reactions. For the post-translational reactions, ATP was added as indicated. Translocation activities are shown at the bottom of the left panels. (B) Purification of F 0 F 1 -ATPase and the Tat components. F 0 F 1 -ATPase from a thermophilic Bacillus PS3 (left), and E. coli TatA-His (lane 1), TatB-His (lane 2), and TatC-His (lane 3) (right) were subjected to SDS-PAGE, followed by Coomassie Brilliant Blue staining. (C, D) Complete reconstitution of the TAT system using the purified components. (C) Purified TatA, TatB, and TatC (in a 1:1:1 ratio) and F 0 F 1 -ATPase were mixed with phospholipids. Then, detergent was removed to form proteoliposomes. The reconstituted proteoliposomes were then fused with PL/DAG liposomes or PL/DAG/MPIase liposomes. Translocation activity was assayed with SufI(RR) (left) or SufI(KK) (right). (D) Proteoliposomes were reconstituted with the indicated components, followed by TorA-GFP translocation. The TatA:TatB:TatC ratio was 10:1:1. CCCP (20 μM), a protonophore, was added to the sample on the left. TorA-GFP(RR) (top) or TorA-GFP(KK) (bottom) was used as the substrate. Translocation activities are shown at the bottom of each gel.

    Techniques Used: Membrane, Liposomes, Translocation Assay, Purification, SDS Page, Staining, Activity Assay

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    Article Snippet: .. The process began with the dissolution of a lipid mixture composed of phospholipids [L-α-phosphatidylcholine from soybean (≥99% purity) was provided by Avanti Polar Lipids (Alabaster, AL, USA; product no. 840051P) and cholesterol (≥99% purity, Sigma-Aldrich, St. Louis, MO, USA; product no. C8667)], in a molar ratio of 7:3, in a solution of organic solvents (chloroform and methanol in a 3:1, v/v ratio), a proportion widely recognized in the literature for its suitability in topical and transdermal formulations [ , ]. .. After complete solubilization of the lipids, a dry lipid film was formed by evaporation of the solvents using a rotary evaporator (Rotavapor ® R-100, BUCHI Labortechnik AG, Flawil, Switzerland; manufactured by Büchi Operations India Pvt Ltd, Surat, India) for 2 h at 40 °C.



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    Diagnostica Stago phospholipid mixture
    (A) Membrane fusion of TatABC proteoliposomes with MPIase liposomes enabled the detection of the SufI translocation. INV, prepared from BL21/pT7-TatABC, were solubilized with OG, and then mixed with purified F 0 F 1 -ATPase. The proteoliposomes were then formed by removing the detergent. PL/DAG liposomes or PL/DAG/MPIase liposomes were fused to the reconstituted proteoliposomes. SufI translocation was performed co-translationally (left) or post-translationally (right) in the presence of these proteoliposomes. SufI(RR) (top left) or SufI(KK) (bottom left) was used as the substrate. One-ninth of the reaction mixture was analyzed as the translation standard (-) for the co-translational reactions. For the post-translational reactions, ATP was added as indicated. Translocation activities are shown at the bottom of the left panels. (B) Purification of F 0 F 1 -ATPase and the Tat components. F 0 F 1 -ATPase from a thermophilic Bacillus PS3 (left), and <t>E.</t> <t>coli</t> TatA-His (lane 1), TatB-His (lane 2), and TatC-His (lane 3) (right) were subjected to SDS-PAGE, followed by Coomassie Brilliant Blue staining. (C, D) Complete reconstitution of the TAT system using the purified components. (C) Purified TatA, TatB, and TatC (in a 1:1:1 ratio) and F 0 F 1 -ATPase were mixed with <t>phospholipids.</t> Then, detergent was removed to form proteoliposomes. The reconstituted proteoliposomes were then fused with PL/DAG liposomes or PL/DAG/MPIase liposomes. Translocation activity was assayed with SufI(RR) (left) or SufI(KK) (right). (D) Proteoliposomes were reconstituted with the indicated components, followed by TorA-GFP translocation. The TatA:TatB:TatC ratio was 10:1:1. CCCP (20 μM), a protonophore, was added to the sample on the left. TorA-GFP(RR) (top) or TorA-GFP(KK) (bottom) was used as the substrate. Translocation activities are shown at the bottom of each gel.
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    (A) Membrane fusion of TatABC proteoliposomes with MPIase liposomes enabled the detection of the SufI translocation. INV, prepared from BL21/pT7-TatABC, were solubilized with OG, and then mixed with purified F 0 F 1 -ATPase. The proteoliposomes were then formed by removing the detergent. PL/DAG liposomes or PL/DAG/MPIase liposomes were fused to the reconstituted proteoliposomes. SufI translocation was performed co-translationally (left) or post-translationally (right) in the presence of these proteoliposomes. SufI(RR) (top left) or SufI(KK) (bottom left) was used as the substrate. One-ninth of the reaction mixture was analyzed as the translation standard (-) for the co-translational reactions. For the post-translational reactions, ATP was added as indicated. Translocation activities are shown at the bottom of the left panels. (B) Purification of F 0 F 1 -ATPase and the Tat components. F 0 F 1 -ATPase from a thermophilic Bacillus PS3 (left), and E. coli TatA-His (lane 1), TatB-His (lane 2), and TatC-His (lane 3) (right) were subjected to SDS-PAGE, followed by Coomassie Brilliant Blue staining. (C, D) Complete reconstitution of the TAT system using the purified components. (C) Purified TatA, TatB, and TatC (in a 1:1:1 ratio) and F 0 F 1 -ATPase were mixed with phospholipids. Then, detergent was removed to form proteoliposomes. The reconstituted proteoliposomes were then fused with PL/DAG liposomes or PL/DAG/MPIase liposomes. Translocation activity was assayed with SufI(RR) (left) or SufI(KK) (right). (D) Proteoliposomes were reconstituted with the indicated components, followed by TorA-GFP translocation. The TatA:TatB:TatC ratio was 10:1:1. CCCP (20 μM), a protonophore, was added to the sample on the left. TorA-GFP(RR) (top) or TorA-GFP(KK) (bottom) was used as the substrate. Translocation activities are shown at the bottom of each gel.

    Journal: bioRxiv

    Article Title: Glycolipid MPIase is essential for the TAT (Twin-Arginine Translocation) pathway

    doi: 10.64898/2026.06.05.730299

    Figure Lengend Snippet: (A) Membrane fusion of TatABC proteoliposomes with MPIase liposomes enabled the detection of the SufI translocation. INV, prepared from BL21/pT7-TatABC, were solubilized with OG, and then mixed with purified F 0 F 1 -ATPase. The proteoliposomes were then formed by removing the detergent. PL/DAG liposomes or PL/DAG/MPIase liposomes were fused to the reconstituted proteoliposomes. SufI translocation was performed co-translationally (left) or post-translationally (right) in the presence of these proteoliposomes. SufI(RR) (top left) or SufI(KK) (bottom left) was used as the substrate. One-ninth of the reaction mixture was analyzed as the translation standard (-) for the co-translational reactions. For the post-translational reactions, ATP was added as indicated. Translocation activities are shown at the bottom of the left panels. (B) Purification of F 0 F 1 -ATPase and the Tat components. F 0 F 1 -ATPase from a thermophilic Bacillus PS3 (left), and E. coli TatA-His (lane 1), TatB-His (lane 2), and TatC-His (lane 3) (right) were subjected to SDS-PAGE, followed by Coomassie Brilliant Blue staining. (C, D) Complete reconstitution of the TAT system using the purified components. (C) Purified TatA, TatB, and TatC (in a 1:1:1 ratio) and F 0 F 1 -ATPase were mixed with phospholipids. Then, detergent was removed to form proteoliposomes. The reconstituted proteoliposomes were then fused with PL/DAG liposomes or PL/DAG/MPIase liposomes. Translocation activity was assayed with SufI(RR) (left) or SufI(KK) (right). (D) Proteoliposomes were reconstituted with the indicated components, followed by TorA-GFP translocation. The TatA:TatB:TatC ratio was 10:1:1. CCCP (20 μM), a protonophore, was added to the sample on the left. TorA-GFP(RR) (top) or TorA-GFP(KK) (bottom) was used as the substrate. Translocation activities are shown at the bottom of each gel.

    Article Snippet: The E. coli polar lipid extract (phospholipids), 18:1 NBD-PE, and dioleoylglycerol were obtained from Avanti Polar Lipids, Inc. n -Octyl-β-D-glucopyranoside (OG) and n -dodecyl-β-D-maltopyranoside (DDM) were obtained from Dojindo Laboratories.

    Techniques: Membrane, Liposomes, Translocation Assay, Purification, SDS Page, Staining, Activity Assay