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    Echelon Biosciences lipid coated membranes
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    lipid coated membranes  (Echelon Biosciences)


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    Echelon Biosciences lipid coated membranes
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    lipid coated hydrophobic membranes  (Echelon Biosciences)


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    Echelon Biosciences lipid coated hydrophobic membranes
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    membrane lipid strip binding assay lipid  (Echelon Biosciences)


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    Echelon Biosciences membrane lipid strip binding assay lipid
    Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the <t>PS-binding</t> domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, <t>lipid</t> binding profiles of PS-specific Fc fusions using <t>lipid-coated</t> nitrocellulose <t>membranes.</t> Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.
    Membrane Lipid Strip Binding Assay Lipid, 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
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    1) Product Images from "Targeting Phosphatidylserine with Calcium-dependent Protein-Drug Conjugates for the Treatment of Cancer"

    Article Title: Targeting Phosphatidylserine with Calcium-dependent Protein-Drug Conjugates for the Treatment of Cancer

    Journal: Molecular cancer therapeutics

    doi: 10.1158/1535-7163.MCT-17-0092

    Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the PS-binding domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, lipid binding profiles of PS-specific Fc fusions using lipid-coated nitrocellulose membranes. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.
    Figure Legend Snippet: Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the PS-binding domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, lipid binding profiles of PS-specific Fc fusions using lipid-coated nitrocellulose membranes. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.

    Techniques Used: Binding Assay, SDS Page, Flow Cytometry, Labeling, Recombinant, Radioactivity, Injection, Fluorescence

    Cell binding and internalization of PS-specific Fc fusions containing Syt1 C2A. A, schematic representation of bivalent and tetravalent PS-specific Fc fusions with filled circles representing the Syt1 C2A domain (left panel). Right panel shows reducing SDS-PAGE analyses of the Syt1-Fc fusions, with molecular weights (MW) shown in kDa on the right. B, Fc fusions (25 nM) were incubated with nitrocellulose membranes coated with the indicated amounts of PS. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, lipid binding profiles of Syt1-Fc fusions using lipid-coated nitrocellulose membranes as shown in Figure 1B. Bound proteins were detected using goat anti-human IgG (H+L) antibody conjugated with HRP. D, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 50 nM control IgG or PS-specific Fc fusions. Bound Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses (MFI, mean fluorescence intensity). E, 2H11 cells were incubated with Alexa 647-labeled PS-specific Fc fusions on ice at optimized concentrations (220 nM for Fc-Syt1 and 40 nM for Syt1-Fc-Syt1) to achieve similar levels of surface binding. Cells were then incubated at 37°C for the indicated time points. Surface bound Fc fusions were stripped using 5 mM EDTA and internalized proteins quantitated by flow cytometry analyses. F and G, 2H11 (F) or MDA-MB-231 (G) cells were incubated with 50 nM control IgG or PS-specific Fc fusions at 37°C for four hours. Cells were fixed, stained with Cy3/Alexa 555-labeled anti-human IgG (H+L) and LAMP-1-specific antibody followed by Alexa 488-labeled secondary antibody for detecting LAMP-1. Fluorescence images were acquired and Cy3/Alexa 555, Alexa 488 and DAPI are pseudo-colored red, green and blue, respectively, in the overlays. Scale bars: 10 μm (F) and 5 μm (G). For D and E, statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (*, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D and E represent SEM.
    Figure Legend Snippet: Cell binding and internalization of PS-specific Fc fusions containing Syt1 C2A. A, schematic representation of bivalent and tetravalent PS-specific Fc fusions with filled circles representing the Syt1 C2A domain (left panel). Right panel shows reducing SDS-PAGE analyses of the Syt1-Fc fusions, with molecular weights (MW) shown in kDa on the right. B, Fc fusions (25 nM) were incubated with nitrocellulose membranes coated with the indicated amounts of PS. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, lipid binding profiles of Syt1-Fc fusions using lipid-coated nitrocellulose membranes as shown in Figure 1B. Bound proteins were detected using goat anti-human IgG (H+L) antibody conjugated with HRP. D, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 50 nM control IgG or PS-specific Fc fusions. Bound Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses (MFI, mean fluorescence intensity). E, 2H11 cells were incubated with Alexa 647-labeled PS-specific Fc fusions on ice at optimized concentrations (220 nM for Fc-Syt1 and 40 nM for Syt1-Fc-Syt1) to achieve similar levels of surface binding. Cells were then incubated at 37°C for the indicated time points. Surface bound Fc fusions were stripped using 5 mM EDTA and internalized proteins quantitated by flow cytometry analyses. F and G, 2H11 (F) or MDA-MB-231 (G) cells were incubated with 50 nM control IgG or PS-specific Fc fusions at 37°C for four hours. Cells were fixed, stained with Cy3/Alexa 555-labeled anti-human IgG (H+L) and LAMP-1-specific antibody followed by Alexa 488-labeled secondary antibody for detecting LAMP-1. Fluorescence images were acquired and Cy3/Alexa 555, Alexa 488 and DAPI are pseudo-colored red, green and blue, respectively, in the overlays. Scale bars: 10 μm (F) and 5 μm (G). For D and E, statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (*, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D and E represent SEM.

    Techniques Used: Binding Assay, SDS Page, Incubation, Labeling, Flow Cytometry, Fluorescence, Staining

    Therapeutic effects of Fc-Syt1_MMAE are dependent on PS binding. A, reducing SDS-PAGE analyses of the unconjugated or MMAE-conjugated PS-specific Fc fusions and control IgG1 Fc, with molecular weights (MW) shown in kDa on the left. B, lipid-coated nitrocellulose membranes were incubated with 2 μg/ml Fc-Syt1 or Fc-Syt1(DN), and bound proteins detected using goat anti-human IgG antibody conjugated with HRP. C, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 5 μg/ml control Fc, Fc-Syt1 or Fc-Syt1(DN). Bound Fc or Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses. Statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (***, P < 0.001; ****, P < 0.0001). D, female BALB/c SCID mice (n = 6 mice/group) bearing MDA-MB-231 tumors were treated with the indicated agents at a dose of 1 nmole/mouse (4.1 mg/Kg for Fc-Syt1_MMAE or Fc-Syt1(DN)_MMAE, 2.6 mg/Kg for Fc_MMAE) twice per week for four weeks (day 28–56) and tumor sizes were measured for a further 2.5 weeks (day 56–74). Statistically significant differences between Fc-Syt1_MMAE and Fc-Syt1(DN)_MMAE treatment groups at the treatment end point were analyzed using one-way ANOVA followed by Bonferroni post hoc test (***, P < 0.001). E, tumors in each group shown in D were isolated and photographed. Scale bar: 1 cm. Error bars in C and D indicate SEM.
    Figure Legend Snippet: Therapeutic effects of Fc-Syt1_MMAE are dependent on PS binding. A, reducing SDS-PAGE analyses of the unconjugated or MMAE-conjugated PS-specific Fc fusions and control IgG1 Fc, with molecular weights (MW) shown in kDa on the left. B, lipid-coated nitrocellulose membranes were incubated with 2 μg/ml Fc-Syt1 or Fc-Syt1(DN), and bound proteins detected using goat anti-human IgG antibody conjugated with HRP. C, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 5 μg/ml control Fc, Fc-Syt1 or Fc-Syt1(DN). Bound Fc or Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses. Statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (***, P < 0.001; ****, P < 0.0001). D, female BALB/c SCID mice (n = 6 mice/group) bearing MDA-MB-231 tumors were treated with the indicated agents at a dose of 1 nmole/mouse (4.1 mg/Kg for Fc-Syt1_MMAE or Fc-Syt1(DN)_MMAE, 2.6 mg/Kg for Fc_MMAE) twice per week for four weeks (day 28–56) and tumor sizes were measured for a further 2.5 weeks (day 56–74). Statistically significant differences between Fc-Syt1_MMAE and Fc-Syt1(DN)_MMAE treatment groups at the treatment end point were analyzed using one-way ANOVA followed by Bonferroni post hoc test (***, P < 0.001). E, tumors in each group shown in D were isolated and photographed. Scale bar: 1 cm. Error bars in C and D indicate SEM.

    Techniques Used: Binding Assay, SDS Page, Incubation, Labeling, Flow Cytometry, Isolation

    membrane lipid strip binding assay lipid  (Echelon Biosciences)


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    lipid coated hydrophobic membranes  (Echelon Biosciences)


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    lipid coated hydrophobic membranes  (Echelon Biosciences)


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    Echelon Biosciences lipid coated hydrophobic membranes
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    lipid coated hydrophobic membranes  (Echelon Biosciences)


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    Echelon Biosciences lipid coated hydrophobic membranes
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    Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the <t>PS-binding</t> domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, <t>lipid</t> binding profiles of PS-specific Fc fusions using <t>lipid-coated</t> nitrocellulose <t>membranes.</t> Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.
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    Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the <t>PS-binding</t> domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, <t>lipid</t> binding profiles of PS-specific Fc fusions using <t>lipid-coated</t> nitrocellulose <t>membranes.</t> Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.
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    Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the PS-binding domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, lipid binding profiles of PS-specific Fc fusions using lipid-coated nitrocellulose membranes. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.

    Journal: Molecular cancer therapeutics

    Article Title: Targeting Phosphatidylserine with Calcium-dependent Protein-Drug Conjugates for the Treatment of Cancer

    doi: 10.1158/1535-7163.MCT-17-0092

    Figure Lengend Snippet: Generation and characterization of PS-targeting agents. A, schematic representation of PS agents (left panel). Filled circles and rectangles represent the PS-binding domains and IgG1 hinge region, respectively. Right panel shows reducing SDS-PAGE analyses of the PS-specific Fc fusions, with molecular weights (MW) shown in kDa on the left. B, lipid binding profiles of PS-specific Fc fusions using lipid-coated nitrocellulose membranes. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, binding of PS-specific Fc fusions to PS-positive 2H11 and MDA-MB-231 cells using flow cytometry analysis, using Alexa 647-labeled anti-human IgG (H+L) for detection. 2nd and Fc represent negative controls using secondary conjugate or recombinant Fc fragment, respectively. D, pharmacokinetic analyses of PS-specific Fc fusions in BALB/c SCID mice (n = 5 mice/group). Whole body and blood levels of radioactivity were measured at the indicated time points. E, areas under curves in panel D for whole body (upper panel) and blood (lower panel) counts were quantitated. F, nude mice bearing orthotopic human MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific Fc fusions, and NIR fluorescence images acquired at the indicated time points. G, tumor-associated fluorescence intensities at 48 hours in F normalized to the corresponding tumor volumes were quantitated. H, female BALB/c SCID mice bearing MDA-MB-231 tumors (n = 3 mice/group) were injected with IRDye800CW-labeled PS-specific agents. 48 hours post-injection, tumors were dissected out and NIR images were acquired. I, tumor-associated fluorescence intensities in H normalized to the corresponding tumor weights. Statistically significant differences in E, G and I were analyzed using one-way ANOVA followed by Tukey post hoc test (**, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D, E, G and I represent SEM.

    Article Snippet: Membrane lipid strip binding assay Lipid-coated membrane strips (Echelon, catalog # P-6002) were first hydrated with TBST (20 mM Tris, 150 mM NaCl, 0.1% Tween 20, pH 7.5) and then incubated with blocking solution (4% fatty acid free BSA dissolved in TBST) at room temperature for 1 hour.

    Techniques: Binding Assay, SDS Page, Flow Cytometry, Labeling, Recombinant, Radioactivity, Injection, Fluorescence

    Cell binding and internalization of PS-specific Fc fusions containing Syt1 C2A. A, schematic representation of bivalent and tetravalent PS-specific Fc fusions with filled circles representing the Syt1 C2A domain (left panel). Right panel shows reducing SDS-PAGE analyses of the Syt1-Fc fusions, with molecular weights (MW) shown in kDa on the right. B, Fc fusions (25 nM) were incubated with nitrocellulose membranes coated with the indicated amounts of PS. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, lipid binding profiles of Syt1-Fc fusions using lipid-coated nitrocellulose membranes as shown in Figure 1B. Bound proteins were detected using goat anti-human IgG (H+L) antibody conjugated with HRP. D, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 50 nM control IgG or PS-specific Fc fusions. Bound Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses (MFI, mean fluorescence intensity). E, 2H11 cells were incubated with Alexa 647-labeled PS-specific Fc fusions on ice at optimized concentrations (220 nM for Fc-Syt1 and 40 nM for Syt1-Fc-Syt1) to achieve similar levels of surface binding. Cells were then incubated at 37°C for the indicated time points. Surface bound Fc fusions were stripped using 5 mM EDTA and internalized proteins quantitated by flow cytometry analyses. F and G, 2H11 (F) or MDA-MB-231 (G) cells were incubated with 50 nM control IgG or PS-specific Fc fusions at 37°C for four hours. Cells were fixed, stained with Cy3/Alexa 555-labeled anti-human IgG (H+L) and LAMP-1-specific antibody followed by Alexa 488-labeled secondary antibody for detecting LAMP-1. Fluorescence images were acquired and Cy3/Alexa 555, Alexa 488 and DAPI are pseudo-colored red, green and blue, respectively, in the overlays. Scale bars: 10 μm (F) and 5 μm (G). For D and E, statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (*, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D and E represent SEM.

    Journal: Molecular cancer therapeutics

    Article Title: Targeting Phosphatidylserine with Calcium-dependent Protein-Drug Conjugates for the Treatment of Cancer

    doi: 10.1158/1535-7163.MCT-17-0092

    Figure Lengend Snippet: Cell binding and internalization of PS-specific Fc fusions containing Syt1 C2A. A, schematic representation of bivalent and tetravalent PS-specific Fc fusions with filled circles representing the Syt1 C2A domain (left panel). Right panel shows reducing SDS-PAGE analyses of the Syt1-Fc fusions, with molecular weights (MW) shown in kDa on the right. B, Fc fusions (25 nM) were incubated with nitrocellulose membranes coated with the indicated amounts of PS. Bound proteins were detected with goat anti-human IgG (H+L) antibody conjugated with HRP. C, lipid binding profiles of Syt1-Fc fusions using lipid-coated nitrocellulose membranes as shown in Figure 1B. Bound proteins were detected using goat anti-human IgG (H+L) antibody conjugated with HRP. D, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 50 nM control IgG or PS-specific Fc fusions. Bound Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses (MFI, mean fluorescence intensity). E, 2H11 cells were incubated with Alexa 647-labeled PS-specific Fc fusions on ice at optimized concentrations (220 nM for Fc-Syt1 and 40 nM for Syt1-Fc-Syt1) to achieve similar levels of surface binding. Cells were then incubated at 37°C for the indicated time points. Surface bound Fc fusions were stripped using 5 mM EDTA and internalized proteins quantitated by flow cytometry analyses. F and G, 2H11 (F) or MDA-MB-231 (G) cells were incubated with 50 nM control IgG or PS-specific Fc fusions at 37°C for four hours. Cells were fixed, stained with Cy3/Alexa 555-labeled anti-human IgG (H+L) and LAMP-1-specific antibody followed by Alexa 488-labeled secondary antibody for detecting LAMP-1. Fluorescence images were acquired and Cy3/Alexa 555, Alexa 488 and DAPI are pseudo-colored red, green and blue, respectively, in the overlays. Scale bars: 10 μm (F) and 5 μm (G). For D and E, statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (*, P < 0.05; **, P < 0.01; ***, P < 0.001; ****, P < 0.0001). Error bars in D and E represent SEM.

    Article Snippet: Membrane lipid strip binding assay Lipid-coated membrane strips (Echelon, catalog # P-6002) were first hydrated with TBST (20 mM Tris, 150 mM NaCl, 0.1% Tween 20, pH 7.5) and then incubated with blocking solution (4% fatty acid free BSA dissolved in TBST) at room temperature for 1 hour.

    Techniques: Binding Assay, SDS Page, Incubation, Labeling, Flow Cytometry, Fluorescence, Staining

    Therapeutic effects of Fc-Syt1_MMAE are dependent on PS binding. A, reducing SDS-PAGE analyses of the unconjugated or MMAE-conjugated PS-specific Fc fusions and control IgG1 Fc, with molecular weights (MW) shown in kDa on the left. B, lipid-coated nitrocellulose membranes were incubated with 2 μg/ml Fc-Syt1 or Fc-Syt1(DN), and bound proteins detected using goat anti-human IgG antibody conjugated with HRP. C, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 5 μg/ml control Fc, Fc-Syt1 or Fc-Syt1(DN). Bound Fc or Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses. Statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (***, P < 0.001; ****, P < 0.0001). D, female BALB/c SCID mice (n = 6 mice/group) bearing MDA-MB-231 tumors were treated with the indicated agents at a dose of 1 nmole/mouse (4.1 mg/Kg for Fc-Syt1_MMAE or Fc-Syt1(DN)_MMAE, 2.6 mg/Kg for Fc_MMAE) twice per week for four weeks (day 28–56) and tumor sizes were measured for a further 2.5 weeks (day 56–74). Statistically significant differences between Fc-Syt1_MMAE and Fc-Syt1(DN)_MMAE treatment groups at the treatment end point were analyzed using one-way ANOVA followed by Bonferroni post hoc test (***, P < 0.001). E, tumors in each group shown in D were isolated and photographed. Scale bar: 1 cm. Error bars in C and D indicate SEM.

    Journal: Molecular cancer therapeutics

    Article Title: Targeting Phosphatidylserine with Calcium-dependent Protein-Drug Conjugates for the Treatment of Cancer

    doi: 10.1158/1535-7163.MCT-17-0092

    Figure Lengend Snippet: Therapeutic effects of Fc-Syt1_MMAE are dependent on PS binding. A, reducing SDS-PAGE analyses of the unconjugated or MMAE-conjugated PS-specific Fc fusions and control IgG1 Fc, with molecular weights (MW) shown in kDa on the left. B, lipid-coated nitrocellulose membranes were incubated with 2 μg/ml Fc-Syt1 or Fc-Syt1(DN), and bound proteins detected using goat anti-human IgG antibody conjugated with HRP. C, 2H11 cells were treated with 50 nM docetaxel for 72 hours, or treated with vehicle control (DMSO), and incubated with 5 μg/ml control Fc, Fc-Syt1 or Fc-Syt1(DN). Bound Fc or Fc fusion was detected using Alexa 488-labeled anti-human IgG (H+L), followed by flow cytometry analyses. Statistically significant differences were analyzed using two-way ANOVA followed by Tukey post hoc test (***, P < 0.001; ****, P < 0.0001). D, female BALB/c SCID mice (n = 6 mice/group) bearing MDA-MB-231 tumors were treated with the indicated agents at a dose of 1 nmole/mouse (4.1 mg/Kg for Fc-Syt1_MMAE or Fc-Syt1(DN)_MMAE, 2.6 mg/Kg for Fc_MMAE) twice per week for four weeks (day 28–56) and tumor sizes were measured for a further 2.5 weeks (day 56–74). Statistically significant differences between Fc-Syt1_MMAE and Fc-Syt1(DN)_MMAE treatment groups at the treatment end point were analyzed using one-way ANOVA followed by Bonferroni post hoc test (***, P < 0.001). E, tumors in each group shown in D were isolated and photographed. Scale bar: 1 cm. Error bars in C and D indicate SEM.

    Article Snippet: Membrane lipid strip binding assay Lipid-coated membrane strips (Echelon, catalog # P-6002) were first hydrated with TBST (20 mM Tris, 150 mM NaCl, 0.1% Tween 20, pH 7.5) and then incubated with blocking solution (4% fatty acid free BSA dissolved in TBST) at room temperature for 1 hour.

    Techniques: Binding Assay, SDS Page, Incubation, Labeling, Flow Cytometry, Isolation