sphingostrips  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences sphingostrips
    Syntaxin 6 + YKGL or + YQRL protein-lipid interactions and localization to the chlamydial inclusion . In (A) , 3XFLAG-syntaxin 6 wild-type (WT), 3XFLAG-syntaxin 6 + YKGL (YKGL), and 3XFLAG-syntaxin 6 +YQRL (YQRL) were immunoprecipitated from HeLa cells and incubated with <t>Sphingostrips</t> or PIPstrips. Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input. Graph depicts the fold changes in densitometry levels of WT compared to YKGL or YQRL, respectively. The graph combines three independent Sphingostrip and PIPstrip assays. Averages and standard error of the mean are shown. In (B) , HeLa cells were transfected with WT, YKGL, or YQRL constructs, infected and fixed in ethanol as described in Figure 3 . The samples were processed for indirect immunofluorescence to detect the 3XFLAG (red), the inclusion membrane (green), or organisms (blue). Images are representative of two independent experiments. White arrows indicate colocalization with the inclusion; bars, 10 μm.
    Sphingostrips, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sphingostrips/product/Echelon Biosciences
    Average 94 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    sphingostrips - by Bioz Stars, 2022-08
    94/100 stars

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    1) Product Images from "The eukaryotic signal sequence, YGRL, targets the chlamydial inclusion"

    Article Title: The eukaryotic signal sequence, YGRL, targets the chlamydial inclusion

    Journal: Frontiers in Cellular and Infection Microbiology

    doi: 10.3389/fcimb.2014.00129

    Syntaxin 6 + YKGL or + YQRL protein-lipid interactions and localization to the chlamydial inclusion . In (A) , 3XFLAG-syntaxin 6 wild-type (WT), 3XFLAG-syntaxin 6 + YKGL (YKGL), and 3XFLAG-syntaxin 6 +YQRL (YQRL) were immunoprecipitated from HeLa cells and incubated with Sphingostrips or PIPstrips. Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input. Graph depicts the fold changes in densitometry levels of WT compared to YKGL or YQRL, respectively. The graph combines three independent Sphingostrip and PIPstrip assays. Averages and standard error of the mean are shown. In (B) , HeLa cells were transfected with WT, YKGL, or YQRL constructs, infected and fixed in ethanol as described in Figure 3 . The samples were processed for indirect immunofluorescence to detect the 3XFLAG (red), the inclusion membrane (green), or organisms (blue). Images are representative of two independent experiments. White arrows indicate colocalization with the inclusion; bars, 10 μm.
    Figure Legend Snippet: Syntaxin 6 + YKGL or + YQRL protein-lipid interactions and localization to the chlamydial inclusion . In (A) , 3XFLAG-syntaxin 6 wild-type (WT), 3XFLAG-syntaxin 6 + YKGL (YKGL), and 3XFLAG-syntaxin 6 +YQRL (YQRL) were immunoprecipitated from HeLa cells and incubated with Sphingostrips or PIPstrips. Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input. Graph depicts the fold changes in densitometry levels of WT compared to YKGL or YQRL, respectively. The graph combines three independent Sphingostrip and PIPstrip assays. Averages and standard error of the mean are shown. In (B) , HeLa cells were transfected with WT, YKGL, or YQRL constructs, infected and fixed in ethanol as described in Figure 3 . The samples were processed for indirect immunofluorescence to detect the 3XFLAG (red), the inclusion membrane (green), or organisms (blue). Images are representative of two independent experiments. White arrows indicate colocalization with the inclusion; bars, 10 μm.

    Techniques Used: Immunoprecipitation, Incubation, Binding Assay, Transfection, Construct, Infection, Immunofluorescence

    Syntaxin 6 and syntaxin 6ΔYGRL protein-lipid interactions . 3XFLAG empty vector (V), 3XFLAG-syntaxin 6 (Stx6) and 3XFLAG-syntaxin 6ΔYGRL (Stx6Δ) were immunopreciptated from HeLa cells and incubated with Sphingostrips (A) or PIPstrips (C) . Protein-lipid interactions with sulfatide (1), phosphatidylinositol 3-phosphate (PI3P) (2), phosphatidylinositol 4-phosphate (PI4P) (3), phosphatidylinositol 5-phosphate (PI5P) (4), and phosphatidylserine (PS) (5) were detected by blotting with anti-3XFLAG. The blank (Bl) is illuminated for orientation purposes. Protein input for sphingostrips and PIP strips was analyzed by blotting with anti-FLAG M2 antibody ( B,D , respectively). Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input (E) . Graph depicts the fold changes in densitometry levels of Stx6 compared to Stx6ΔYGRL. Positive reactions on Sphingostrips and PIPstrips were normalized to input and the graph combines data from three independent Sphingostrip and four independent PIPstrip assays. Averages and standard error of the mean are shown.
    Figure Legend Snippet: Syntaxin 6 and syntaxin 6ΔYGRL protein-lipid interactions . 3XFLAG empty vector (V), 3XFLAG-syntaxin 6 (Stx6) and 3XFLAG-syntaxin 6ΔYGRL (Stx6Δ) were immunopreciptated from HeLa cells and incubated with Sphingostrips (A) or PIPstrips (C) . Protein-lipid interactions with sulfatide (1), phosphatidylinositol 3-phosphate (PI3P) (2), phosphatidylinositol 4-phosphate (PI4P) (3), phosphatidylinositol 5-phosphate (PI5P) (4), and phosphatidylserine (PS) (5) were detected by blotting with anti-3XFLAG. The blank (Bl) is illuminated for orientation purposes. Protein input for sphingostrips and PIP strips was analyzed by blotting with anti-FLAG M2 antibody ( B,D , respectively). Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input (E) . Graph depicts the fold changes in densitometry levels of Stx6 compared to Stx6ΔYGRL. Positive reactions on Sphingostrips and PIPstrips were normalized to input and the graph combines data from three independent Sphingostrip and four independent PIPstrip assays. Averages and standard error of the mean are shown.

    Techniques Used: Plasmid Preparation, Incubation, Binding Assay

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    Echelon Biosciences sphingo strips
    V. parahaemolyticus MAM7 and E. coli MAM HS show different binding preferences for host lipid receptors. (A) The lipid binding profile of E. coli GST-MAM HS was determined by lipid overlay assays. 10 µM recombinant pure protein were incubated with <t>Sphingo-Strips</t> or PIP-Strips, and bound proteins detected by probing membranes with α-GST and α-mouse HRP antibodies, and developing with ECL detection reagent. (B) Comparison of chemical structures of ceramide, phosphatidic acid, and sulfatide head groups. Interactions between V. parahaemolyticus MAM7 (C) or E. coli MAM HS (D) and lipids were quantified using plate assays. Lipids were immobilized in wells and bound protein was quantified by probing wells with a-GST and a-mouse HRP antibodies, and developing with ECL detection reagent. Results shown are means ± SEM from three independent experiments.
    Sphingo Strips, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/sphingo strips/product/Echelon Biosciences
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    sphingo strips - by Bioz Stars, 2022-08
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    V. parahaemolyticus MAM7 and E. coli MAM HS show different binding preferences for host lipid receptors. (A) The lipid binding profile of E. coli GST-MAM HS was determined by lipid overlay assays. 10 µM recombinant pure protein were incubated with Sphingo-Strips or PIP-Strips, and bound proteins detected by probing membranes with α-GST and α-mouse HRP antibodies, and developing with ECL detection reagent. (B) Comparison of chemical structures of ceramide, phosphatidic acid, and sulfatide head groups. Interactions between V. parahaemolyticus MAM7 (C) or E. coli MAM HS (D) and lipids were quantified using plate assays. Lipids were immobilized in wells and bound protein was quantified by probing wells with a-GST and a-mouse HRP antibodies, and developing with ECL detection reagent. Results shown are means ± SEM from three independent experiments.

    Journal: bioRxiv

    Article Title: A commensal adhesin enhances E. coli retention by mucin, while mucin desulfation by mucin-foraging bacteria enhances its transmigration through the mucus barrier

    doi: 10.1101/126672

    Figure Lengend Snippet: V. parahaemolyticus MAM7 and E. coli MAM HS show different binding preferences for host lipid receptors. (A) The lipid binding profile of E. coli GST-MAM HS was determined by lipid overlay assays. 10 µM recombinant pure protein were incubated with Sphingo-Strips or PIP-Strips, and bound proteins detected by probing membranes with α-GST and α-mouse HRP antibodies, and developing with ECL detection reagent. (B) Comparison of chemical structures of ceramide, phosphatidic acid, and sulfatide head groups. Interactions between V. parahaemolyticus MAM7 (C) or E. coli MAM HS (D) and lipids were quantified using plate assays. Lipids were immobilized in wells and bound protein was quantified by probing wells with a-GST and a-mouse HRP antibodies, and developing with ECL detection reagent. Results shown are means ± SEM from three independent experiments.

    Article Snippet: Lipid overlay assays PIP-Strips and Sphingo-Strips (Echelon biosciences) were used to test the lipid binding properties of GST-MAMHS .

    Techniques: Binding Assay, Recombinant, Incubation

    Syntaxin 6 + YKGL or + YQRL protein-lipid interactions and localization to the chlamydial inclusion . In (A) , 3XFLAG-syntaxin 6 wild-type (WT), 3XFLAG-syntaxin 6 + YKGL (YKGL), and 3XFLAG-syntaxin 6 +YQRL (YQRL) were immunoprecipitated from HeLa cells and incubated with Sphingostrips or PIPstrips. Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input. Graph depicts the fold changes in densitometry levels of WT compared to YKGL or YQRL, respectively. The graph combines three independent Sphingostrip and PIPstrip assays. Averages and standard error of the mean are shown. In (B) , HeLa cells were transfected with WT, YKGL, or YQRL constructs, infected and fixed in ethanol as described in Figure 3 . The samples were processed for indirect immunofluorescence to detect the 3XFLAG (red), the inclusion membrane (green), or organisms (blue). Images are representative of two independent experiments. White arrows indicate colocalization with the inclusion; bars, 10 μm.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: The eukaryotic signal sequence, YGRL, targets the chlamydial inclusion

    doi: 10.3389/fcimb.2014.00129

    Figure Lengend Snippet: Syntaxin 6 + YKGL or + YQRL protein-lipid interactions and localization to the chlamydial inclusion . In (A) , 3XFLAG-syntaxin 6 wild-type (WT), 3XFLAG-syntaxin 6 + YKGL (YKGL), and 3XFLAG-syntaxin 6 +YQRL (YQRL) were immunoprecipitated from HeLa cells and incubated with Sphingostrips or PIPstrips. Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input. Graph depicts the fold changes in densitometry levels of WT compared to YKGL or YQRL, respectively. The graph combines three independent Sphingostrip and PIPstrip assays. Averages and standard error of the mean are shown. In (B) , HeLa cells were transfected with WT, YKGL, or YQRL constructs, infected and fixed in ethanol as described in Figure 3 . The samples were processed for indirect immunofluorescence to detect the 3XFLAG (red), the inclusion membrane (green), or organisms (blue). Images are representative of two independent experiments. White arrows indicate colocalization with the inclusion; bars, 10 μm.

    Article Snippet: Protein-lipid interactions assays Immunopreciptated 3XFLAG-syntaxin 6 and 3XFLAG-syntaxin 6 ΔYGRL were incubated with Sphingostrips (S-6000) or PIPstrips (P-6001) (Echelon Biosciences Inc., Salt Lake City, UT).

    Techniques: Immunoprecipitation, Incubation, Binding Assay, Transfection, Construct, Infection, Immunofluorescence

    Syntaxin 6 and syntaxin 6ΔYGRL protein-lipid interactions . 3XFLAG empty vector (V), 3XFLAG-syntaxin 6 (Stx6) and 3XFLAG-syntaxin 6ΔYGRL (Stx6Δ) were immunopreciptated from HeLa cells and incubated with Sphingostrips (A) or PIPstrips (C) . Protein-lipid interactions with sulfatide (1), phosphatidylinositol 3-phosphate (PI3P) (2), phosphatidylinositol 4-phosphate (PI4P) (3), phosphatidylinositol 5-phosphate (PI5P) (4), and phosphatidylserine (PS) (5) were detected by blotting with anti-3XFLAG. The blank (Bl) is illuminated for orientation purposes. Protein input for sphingostrips and PIP strips was analyzed by blotting with anti-FLAG M2 antibody ( B,D , respectively). Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input (E) . Graph depicts the fold changes in densitometry levels of Stx6 compared to Stx6ΔYGRL. Positive reactions on Sphingostrips and PIPstrips were normalized to input and the graph combines data from three independent Sphingostrip and four independent PIPstrip assays. Averages and standard error of the mean are shown.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: The eukaryotic signal sequence, YGRL, targets the chlamydial inclusion

    doi: 10.3389/fcimb.2014.00129

    Figure Lengend Snippet: Syntaxin 6 and syntaxin 6ΔYGRL protein-lipid interactions . 3XFLAG empty vector (V), 3XFLAG-syntaxin 6 (Stx6) and 3XFLAG-syntaxin 6ΔYGRL (Stx6Δ) were immunopreciptated from HeLa cells and incubated with Sphingostrips (A) or PIPstrips (C) . Protein-lipid interactions with sulfatide (1), phosphatidylinositol 3-phosphate (PI3P) (2), phosphatidylinositol 4-phosphate (PI4P) (3), phosphatidylinositol 5-phosphate (PI5P) (4), and phosphatidylserine (PS) (5) were detected by blotting with anti-3XFLAG. The blank (Bl) is illuminated for orientation purposes. Protein input for sphingostrips and PIP strips was analyzed by blotting with anti-FLAG M2 antibody ( B,D , respectively). Fold increase in syntaxin 6-lipid binding was determined by normalization of densitometry to input (E) . Graph depicts the fold changes in densitometry levels of Stx6 compared to Stx6ΔYGRL. Positive reactions on Sphingostrips and PIPstrips were normalized to input and the graph combines data from three independent Sphingostrip and four independent PIPstrip assays. Averages and standard error of the mean are shown.

    Article Snippet: Protein-lipid interactions assays Immunopreciptated 3XFLAG-syntaxin 6 and 3XFLAG-syntaxin 6 ΔYGRL were incubated with Sphingostrips (S-6000) or PIPstrips (P-6001) (Echelon Biosciences Inc., Salt Lake City, UT).

    Techniques: Plasmid Preparation, Incubation, Binding Assay

    V. parahemolyticus MAM7 and E. coli MAM HS show different binding preferences for host–lipid receptors. A, lipid-binding profile of E. coli GST-MAM HS and GST control was determined by lipid overlay assays. 10 μ m recombinant pure proteins were incubated with Sphingo-Strips or PIP-Strips (containing 100 pmol of each lipid species), and bound proteins were detected by probing membranes with α-GST and α-mouse HRP antibodies and developed with enhanced chemiluminescence detection reagent. Pictures shown are representative of at least three independent experiments. PC, phosphatidylcholine; PtdIns, phosphatidylinositol. B, comparison of chemical structures of ceramide, phosphatidic acid, and sulfatide headgroups. Interactions between V. parahemolyticus MAM7 ( C ) or E. coli MAM HS ( D ) and lipids were quantified using plate assays. Lipids were immobilized in wells, and bound protein was quantified by probing wells with α-GST and α-mouse HRP antibodies, developed with ECL detection reagent, and measured by relative luminescence emission ( RLU ). Results shown are means ± S.E. ( n = 3).

    Journal: The Journal of Biological Chemistry

    Article Title: 3-Sulfogalactosyl-dependent adhesion of Escherichia coli HS multivalent adhesion molecule is attenuated by sulfatase activity

    doi: 10.1074/jbc.M117.817908

    Figure Lengend Snippet: V. parahemolyticus MAM7 and E. coli MAM HS show different binding preferences for host–lipid receptors. A, lipid-binding profile of E. coli GST-MAM HS and GST control was determined by lipid overlay assays. 10 μ m recombinant pure proteins were incubated with Sphingo-Strips or PIP-Strips (containing 100 pmol of each lipid species), and bound proteins were detected by probing membranes with α-GST and α-mouse HRP antibodies and developed with enhanced chemiluminescence detection reagent. Pictures shown are representative of at least three independent experiments. PC, phosphatidylcholine; PtdIns, phosphatidylinositol. B, comparison of chemical structures of ceramide, phosphatidic acid, and sulfatide headgroups. Interactions between V. parahemolyticus MAM7 ( C ) or E. coli MAM HS ( D ) and lipids were quantified using plate assays. Lipids were immobilized in wells, and bound protein was quantified by probing wells with α-GST and α-mouse HRP antibodies, developed with ECL detection reagent, and measured by relative luminescence emission ( RLU ). Results shown are means ± S.E. ( n = 3).

    Article Snippet: Lipid overlay assays PIP-Strips and Sphingo-Strips (Echelon Biosciences) were used to test the lipid-binding properties of GST and GST-MAMHS .

    Techniques: Binding Assay, Recombinant, Incubation