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dilauroyl sn glycero 3 phosphate  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences dilauroyl sn glycero 3 phosphate
    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, <t>1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine;</t> PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.
    Dilauroyl Sn Glycero 3 Phosphate, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Phosphatidic acid generated by PLD2 promotes the plasma membrane recruitment of IQGAP1 and neointima formation"

    Article Title: Phosphatidic acid generated by PLD2 promotes the plasma membrane recruitment of IQGAP1 and neointima formation

    Journal: The FASEB Journal

    doi: 10.1096/fj.201800390RR

    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine; PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.
    Figure Legend Snippet: IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine; PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.

    Techniques Used: Stripping Membranes, Binding Assay, Construct, Purification, Western Blot



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    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, <t>1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine;</t> PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.
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    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, <t>1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine;</t> PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.
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    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, <t>1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine;</t> PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.
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    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, <t>1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine;</t> PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.
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    IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine; PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.

    Journal: The FASEB Journal

    Article Title: Phosphatidic acid generated by PLD2 promotes the plasma membrane recruitment of IQGAP1 and neointima formation

    doi: 10.1096/fj.201800390RR

    Figure Lengend Snippet: IQGAP1 binds to PA directly and specifically. A) Lipid strip binding assay. Top, domain structure of IQGAP1and GST fusion constructs used for the experiment. CHD, calponin homology domain; IQ-Repeat, IQGAP-specific repeat motif; WW, domain with 2 conserved Trp (W) residues; IQ, IQ motif. Bottom, the purified C terminus of IQGAP1 (IQGAP1-C) specifically bound to PA, and to a lesser extent to PI(4,5)P2, PE, and PS. Protein bound to lipid strip was detected using a GST antibody. LPA, D-(+)-sn-1-O-oleoyl-glyceryl-3-phosphate; LPC, 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphocholine; PI(3)P, phosphatidylinositol 3-phosphate diC16; PI(4)P, phosphatidylinositol 4-phosphate diC16; PI(5)P, phosphatidylinositol 5-phosphate diC16; S1P, sphingosine 1-phosphate; PI(3,4)P2, phosphatidylinositol 3,4-bisphosphate diC16; PI(3,5)P2, phosphatidylinositol 3,5-bisphosphate diC16; PI(3,4,5)P3, phosphatidylinositol 3,4,5-trisphosphate. B) IQGAP1-C specifically bound to PA in a liposome pulldown assay. IQGAP1-C bound to liposomes containing indicated phospholipids was detected by Western blot using a GST antibody. C) Quantification of the binding of IQGAP1-C to liposomes in B (n = 3). D) Identification of the PA binding site, A3, on IQGAP1. Left, the candidate PA binding sites on IQGAP1-C and corresponding alanine mutants. Right, Western blot analysis of PA-binding ability of IQGAP1-C WT and mutants in a liposome pulldown assay of serially diluted liposomes. E) Quantification of the binding of IQGAP1-C proteins to PA liposomes in D (n = 3). ***P < 0.001.

    Article Snippet: For exogenous PA stimulation, 1,2-dilauroyl- sn -glycero-3-phosphate from Echelon (Salt Lake City, UT, USA) was dried by nitrogen gas and resuspended in culture medium to make 10 mM stock, and then sonicated briefly with low to medium power.

    Techniques: Stripping Membranes, Binding Assay, Construct, Purification, Western Blot