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anti chicken igy alexafluor488  (Jackson Immuno)


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    Jackson Immuno anti chicken igy alexafluor488
    Anti Chicken Igy Alexafluor488, supplied by Jackson Immuno, used in various techniques. Bioz Stars score: 96/100, based on 1589 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/alexafluor488/Alexa+Fluor+488+AffiniPure+Donkey+Anti-Chicken+IgY/bio_rxiv__64898__2026__02__19__705149-165-30-35
    Average 96 stars, based on 1589 article reviews
    anti chicken igy alexafluor488 - by Bioz Stars, 2026-10
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    Article Title: The mechanisms by which RhoA activity and associated synaptic effects are controlled by the DISC1 scaffolding-like protein
    Article Snippet: Antibody , Secondary antibody donkey-anti-chicken AlexaFluor488 , Jackson ImmunoResearch , Cat# 703-545-155, RRID:AB_2340375 , .

    Article Title: In vivo single-cell CRISPR uncovers distinct TNF-α programs in clonal expansion and tumorigenesis
    Article Snippet: All secondary antibodies used were raised in a donkey host and were conjugated to Alexafluor488, Cy3, or AlexaFluor647 (Jackson ImmunoResearch Laboratory; 1:500-1:1000).

    Article Title: A lectin produced by a Streptomyces species targets mammalian pancreatic acinar cells in mice and humans
    Article Snippet: Donkey anti-rabbit IgG (H + L), AlexaFluor488 , Jackson Immunoresearch , , 711-546-152 , , AB_2340619 , , 1:1000 , , 1:1000 , , Secondary , .

    Article Title: In vivo single-cell CRISPR uncovers distinct TNF programmes in tumour evolution.
    Article Snippet: Secondary antibodies for immunofluoresence: All secondary antibodies used were raised in a donkey host and were conjugated to Alexafluor488(Codes: 703-545-155, 712-545-150, 712-545-153), Cy3(Codes:703-165-155, 711-165-152), or AlexaFluor647(Codes:703-605-155,711-605-152,712-605-153) (Jackson ImmunoResearch Laboratory; 1:500- 1:1000).

    Article Title: In vivo single-cell CRISPR uncovers distinct TNF programmes in tumour evolution
    Article Snippet: Secondary antibodies for immunofluoresence: All secondary antibodies used were raised in a donkey host and were conjugated to Alexafluor488(Codes: 703-545-155, 712-545-150, 712-545-153), Cy3(Codes:703-165-155, 711-165-152), or AlexaFluor647(Codes:703-605-155,711-605-152,712-605-153) (Jackson ImmunoResearch Laboratory; 1:500- 1:1000).

    Incubation:

    Article Title: In vivo single-cell CRISPR uncovers distinct TNF programmes in tumour evolution.
    Article Snippet: Primary antibodies (TNF [D2D4] XP[R] Rabbit anti-mouse monoclonal antibody, CST 11948; 1:300) and purified rat anti-mouse CD104 (also known as β4-integrin) (BD Pharmingen 553745, 1:300) were incubated overnight at 4 °C. .. After washing twice with 1× PBS, slides were incubated with secondary antibodies (Alexafluor488, Cy3, or AlexaFluor647, Jackson ImmunoResearch Laboratory; 1:500–1:1,000) and 0.5 μg ml−1 4′,6-diamidino-2-phenylindole (DAPI) at room temperature for 1 h. Sections were then washed again with 1× PBS, dried, covered with home-made mounting medium and sealed with nail polish before image acquisition. .. Pictures were acquired with a 20× objective on a ZEISS Axio Observer microscope controlled by the ZEN microscopy software (version 3.1).

    Article Title: In vivo single-cell CRISPR uncovers distinct TNF programmes in tumour evolution
    Article Snippet: Primary antibodies (TNF [D2D4] XP[R] Rabbit anti-mouse monoclonal antibody, CST 11948; 1:300) and purified rat anti-mouse CD104 (also known as β4-integrin) (BD Pharmingen 553745, 1:300) were incubated overnight at 4 °C. .. After washing twice with 1× PBS, slides were incubated with secondary antibodies (Alexafluor488, Cy3, or AlexaFluor647, Jackson ImmunoResearch Laboratory; 1:500–1:1,000) and 0.5 μg ml −1 4′,6-diamidino-2-phenylindole (DAPI) at room temperature for 1 h. Sections were then washed again with 1× PBS, dried, covered with home-made mounting medium and sealed with nail polish before image acquisition. .. Pictures were acquired with a 20× objective on a ZEISS Axio Observer microscope controlled by the ZEN microscopy software (version 3.1).

    Labeling:

    Article Title: Astrocytes in the rostral ventromedial medulla mediate the analgesic effect of electroacupuncture in a rodent model of chemotherapy-induced peripheral neuropathic pain.
    Article Snippet: Chemotherapy-induced peripheral neuropathic pain aggravates cancer survivors’ life burden.. Electroacupuncture (EA) has exhibited promising analgesic effects on neuropathic pain in previous studies.. We investigated whether EA was effective in a paclitaxel-induced neuropathic pain mouse model. We further explored the functional role of astrocytes in the rostral ventromedial medulla (RVM), a well-established pain modulation center, in the process of neuropathic pain as well as the analgesic effect of EA.



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    (a) Time series of micrographs of primary human macrophages treated with control siRNA or drebrin siRNA, incubated with biotin to label surface proteins and <t>with</t> <t>AlexaFluor488-streptavidin</t> to visualize and quantify endocytosis of biotinylated proteins. Black outlines indicate cells with a high expression of drebrin, while red outlines mark cells with low expression. Note reduced streptavidin signal intensity (i.e. endocytosed surface proteins) in cells showing low drebrin expression and vice versa. (b) Quantification of streptavidin signal intensity, during endocytosis, in cells treated with control siRNA or drebrin siRNA. Signals are normalized to the mean intensity signal of the respective control. N= 49 cells from 4 independent donors, ****P<0.001, according to 2way ANOVA test. Bar: 10 µm. (c) Endocytosis of biotinylated surface proteins from cells treated with control siRNA or drebrin siRNA with representative Western blots showing β1, β2, β3 integrins, and α-tubulin as loading control. Time since start of the experiment is indicated in min. (d-f) Evaluation of signal intensities of blots from (c) Signals are normalized to mean intensity of drebrin signal of respective control. N= 2 independent donors, *P<0.05, according to multiple unpaired T-tests. (g) Analysis of total cellular expression levels of target proteins in primary human macrophages treated with drebrin siRNA for 72 hrs: N= at least 2 samples from independent donors; ns, according to One-way ANOVA test. (h) Western blot of anti-GFP immunoprecipitations from lysates of macrophages expressing drebrin-GFP or GFP empty vector as control, lysed with mild or stringent lysis buffers, and developed with anti-β1, β2, or β3 integrin antibodies. Note prominent coprecipitation of β2 integrin in both conditions and faint coprecipitation of β3 integrin only in mild condition. (i) Western blot analysis of cross-immunoprecipitations of endogenous dynamin or drebrin from macrophage lysates, with whole cell lysate (WCL) as control. Note absence of drebrin in anti-dynamin IP and vice versa. (j) Western blot analysis of whole cell lysates from HUVEC or primary human macrophages (left), and immunopreciptations from human macrophage lysates using control IgG or anti-drebrin antibody, probed for clathrin heavy chain, drebrin, and caveolin-1. Note detection of caveolin-1 in lysates from HUVEC, but not from macrophages. Also note co-precipitation of clathrin heavy chain with drebrin. Molecular weight in kDa is indicated on the right for (c,h-j).
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    (a) Time series of micrographs of primary human macrophages treated with control siRNA or drebrin siRNA, incubated with biotin to label surface proteins and <t>with</t> <t>AlexaFluor488-streptavidin</t> to visualize and quantify endocytosis of biotinylated proteins. Black outlines indicate cells with a high expression of drebrin, while red outlines mark cells with low expression. Note reduced streptavidin signal intensity (i.e. endocytosed surface proteins) in cells showing low drebrin expression and vice versa. (b) Quantification of streptavidin signal intensity, during endocytosis, in cells treated with control siRNA or drebrin siRNA. Signals are normalized to the mean intensity signal of the respective control. N= 49 cells from 4 independent donors, ****P<0.001, according to 2way ANOVA test. Bar: 10 µm. (c) Endocytosis of biotinylated surface proteins from cells treated with control siRNA or drebrin siRNA with representative Western blots showing β1, β2, β3 integrins, and α-tubulin as loading control. Time since start of the experiment is indicated in min. (d-f) Evaluation of signal intensities of blots from (c) Signals are normalized to mean intensity of drebrin signal of respective control. N= 2 independent donors, *P<0.05, according to multiple unpaired T-tests. (g) Analysis of total cellular expression levels of target proteins in primary human macrophages treated with drebrin siRNA for 72 hrs: N= at least 2 samples from independent donors; ns, according to One-way ANOVA test. (h) Western blot of anti-GFP immunoprecipitations from lysates of macrophages expressing drebrin-GFP or GFP empty vector as control, lysed with mild or stringent lysis buffers, and developed with anti-β1, β2, or β3 integrin antibodies. Note prominent coprecipitation of β2 integrin in both conditions and faint coprecipitation of β3 integrin only in mild condition. (i) Western blot analysis of cross-immunoprecipitations of endogenous dynamin or drebrin from macrophage lysates, with whole cell lysate (WCL) as control. Note absence of drebrin in anti-dynamin IP and vice versa. (j) Western blot analysis of whole cell lysates from HUVEC or primary human macrophages (left), and immunopreciptations from human macrophage lysates using control IgG or anti-drebrin antibody, probed for clathrin heavy chain, drebrin, and caveolin-1. Note detection of caveolin-1 in lysates from HUVEC, but not from macrophages. Also note co-precipitation of clathrin heavy chain with drebrin. Molecular weight in kDa is indicated on the right for (c,h-j).
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    Genotypes of the larger population of 114 phenotyped TBs for ( A ) <t>SEL1L</t> c.1810A>G p.Ile604Val and ( B ) VIPAS39:g.22685398_22685470del . The y axis is percent difference in fibrinogen binding compared with control horses. The 35% cutoff line characterizing affected horses is indicated by a dashed line. **** P < 0.0001 by 1-way ANOVA.
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    Image Search Results


    (a) Time series of micrographs of primary human macrophages treated with control siRNA or drebrin siRNA, incubated with biotin to label surface proteins and with AlexaFluor488-streptavidin to visualize and quantify endocytosis of biotinylated proteins. Black outlines indicate cells with a high expression of drebrin, while red outlines mark cells with low expression. Note reduced streptavidin signal intensity (i.e. endocytosed surface proteins) in cells showing low drebrin expression and vice versa. (b) Quantification of streptavidin signal intensity, during endocytosis, in cells treated with control siRNA or drebrin siRNA. Signals are normalized to the mean intensity signal of the respective control. N= 49 cells from 4 independent donors, ****P<0.001, according to 2way ANOVA test. Bar: 10 µm. (c) Endocytosis of biotinylated surface proteins from cells treated with control siRNA or drebrin siRNA with representative Western blots showing β1, β2, β3 integrins, and α-tubulin as loading control. Time since start of the experiment is indicated in min. (d-f) Evaluation of signal intensities of blots from (c) Signals are normalized to mean intensity of drebrin signal of respective control. N= 2 independent donors, *P<0.05, according to multiple unpaired T-tests. (g) Analysis of total cellular expression levels of target proteins in primary human macrophages treated with drebrin siRNA for 72 hrs: N= at least 2 samples from independent donors; ns, according to One-way ANOVA test. (h) Western blot of anti-GFP immunoprecipitations from lysates of macrophages expressing drebrin-GFP or GFP empty vector as control, lysed with mild or stringent lysis buffers, and developed with anti-β1, β2, or β3 integrin antibodies. Note prominent coprecipitation of β2 integrin in both conditions and faint coprecipitation of β3 integrin only in mild condition. (i) Western blot analysis of cross-immunoprecipitations of endogenous dynamin or drebrin from macrophage lysates, with whole cell lysate (WCL) as control. Note absence of drebrin in anti-dynamin IP and vice versa. (j) Western blot analysis of whole cell lysates from HUVEC or primary human macrophages (left), and immunopreciptations from human macrophage lysates using control IgG or anti-drebrin antibody, probed for clathrin heavy chain, drebrin, and caveolin-1. Note detection of caveolin-1 in lysates from HUVEC, but not from macrophages. Also note co-precipitation of clathrin heavy chain with drebrin. Molecular weight in kDa is indicated on the right for (c,h-j).

    Journal: bioRxiv

    Article Title: Drebrin forms a cortical hub that connects actin, microtubules, and clathrin for endocytic transport of β2 integrin

    doi: 10.64898/2026.03.12.711275

    Figure Lengend Snippet: (a) Time series of micrographs of primary human macrophages treated with control siRNA or drebrin siRNA, incubated with biotin to label surface proteins and with AlexaFluor488-streptavidin to visualize and quantify endocytosis of biotinylated proteins. Black outlines indicate cells with a high expression of drebrin, while red outlines mark cells with low expression. Note reduced streptavidin signal intensity (i.e. endocytosed surface proteins) in cells showing low drebrin expression and vice versa. (b) Quantification of streptavidin signal intensity, during endocytosis, in cells treated with control siRNA or drebrin siRNA. Signals are normalized to the mean intensity signal of the respective control. N= 49 cells from 4 independent donors, ****P<0.001, according to 2way ANOVA test. Bar: 10 µm. (c) Endocytosis of biotinylated surface proteins from cells treated with control siRNA or drebrin siRNA with representative Western blots showing β1, β2, β3 integrins, and α-tubulin as loading control. Time since start of the experiment is indicated in min. (d-f) Evaluation of signal intensities of blots from (c) Signals are normalized to mean intensity of drebrin signal of respective control. N= 2 independent donors, *P<0.05, according to multiple unpaired T-tests. (g) Analysis of total cellular expression levels of target proteins in primary human macrophages treated with drebrin siRNA for 72 hrs: N= at least 2 samples from independent donors; ns, according to One-way ANOVA test. (h) Western blot of anti-GFP immunoprecipitations from lysates of macrophages expressing drebrin-GFP or GFP empty vector as control, lysed with mild or stringent lysis buffers, and developed with anti-β1, β2, or β3 integrin antibodies. Note prominent coprecipitation of β2 integrin in both conditions and faint coprecipitation of β3 integrin only in mild condition. (i) Western blot analysis of cross-immunoprecipitations of endogenous dynamin or drebrin from macrophage lysates, with whole cell lysate (WCL) as control. Note absence of drebrin in anti-dynamin IP and vice versa. (j) Western blot analysis of whole cell lysates from HUVEC or primary human macrophages (left), and immunopreciptations from human macrophage lysates using control IgG or anti-drebrin antibody, probed for clathrin heavy chain, drebrin, and caveolin-1. Note detection of caveolin-1 in lysates from HUVEC, but not from macrophages. Also note co-precipitation of clathrin heavy chain with drebrin. Molecular weight in kDa is indicated on the right for (c,h-j).

    Article Snippet: Following fixation, samples were washed three times with DPBS, regularly permeabilized for 5 min with 0.5 % Triton X-100, blocked for 1 hr with 2% BSA and 5% NGS, incubated for 90 min with blocking solution containing 1:400 AlexaFluor488-streptavidin (ThermoFisher Scientific, Cat# S32354), 1:400 AlexaFluor568-phalloidin (ThermoFisher Scientific, Cat# A12380), 1:1000 DAPI (ThermoFisher Scientific, Cat# 62248) and 1:200 anti-drebrin polyclonal Ab (ThermoFisher Scientific, Cat# PA5-84067), washed with 0.05% Triton X-100 (3x5 min) and then incubated for 60 min with blocking solution containing AlexaFluor647-anti-rabbit Ab (ThermoFisher Scientific, Cat# A-21246) before 3x5 min washes with 0.05% Triton X and mounting with Fluoromount-G medium (ThermoFisher Scientific, Cat# 00-4958-02).

    Techniques: Control, Incubation, Expressing, Western Blot, Plasmid Preparation, Lysis, Molecular Weight

    Genotypes of the larger population of 114 phenotyped TBs for ( A ) SEL1L c.1810A>G p.Ile604Val and ( B ) VIPAS39:g.22685398_22685470del . The y axis is percent difference in fibrinogen binding compared with control horses. The 35% cutoff line characterizing affected horses is indicated by a dashed line. **** P < 0.0001 by 1-way ANOVA.

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: Genotypes of the larger population of 114 phenotyped TBs for ( A ) SEL1L c.1810A>G p.Ile604Val and ( B ) VIPAS39:g.22685398_22685470del . The y axis is percent difference in fibrinogen binding compared with control horses. The 35% cutoff line characterizing affected horses is indicated by a dashed line. **** P < 0.0001 by 1-way ANOVA.

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: Binding Assay, Control

    SEL1L protein expression from flow cytometry in ( A ) resting permeabilized platelets and ( B ) on the surface of thrombin-activated platelets. The median for each horse and the SD are shown. n = 7 Ref/Ref, 6 Ref/Alt, and 2 Alt/Alt. The percent platelets that were positive for SEL1L was decreased in the Alt/Alt horses compared with the Ref/Ref horses in both resting and activated platelets.

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: SEL1L protein expression from flow cytometry in ( A ) resting permeabilized platelets and ( B ) on the surface of thrombin-activated platelets. The median for each horse and the SD are shown. n = 7 Ref/Ref, 6 Ref/Alt, and 2 Alt/Alt. The percent platelets that were positive for SEL1L was decreased in the Alt/Alt horses compared with the Ref/Ref horses in both resting and activated platelets.

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: Expressing, Flow Cytometry

    ( A ) TBTs using horses that were Ref/Ref or Alt/Alt for the SEL1L c.1810A>G p.Ile604Val variant found no significant difference between genotypes by 2-tailed Student’s t test. n = 10 Ref/Ref and 3 Alt/Alt. ( B ) SEL1L (red) localization in relation to P selectin (green) in (top) resting permeabilized platelets and (bottom) thrombin-activated platelet surface of horses that are Ref/Ref for SEL1L c.1810A>G p.Ile604Val. SEL1L did not localize to the surface in resting permeabilized platelets (top) but did localize to the surface in thrombin-activated platelets (bottom). n = 2. Original magnification, ×100. ( C ) Collagen spreading assay comparing median platelet area to genotype. There was a substantial difference between homozygous Ref and Alt genotypes. n = 11 Ref/Ref, 5 Ref/Alt, and 2 Alt/Alt.

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: ( A ) TBTs using horses that were Ref/Ref or Alt/Alt for the SEL1L c.1810A>G p.Ile604Val variant found no significant difference between genotypes by 2-tailed Student’s t test. n = 10 Ref/Ref and 3 Alt/Alt. ( B ) SEL1L (red) localization in relation to P selectin (green) in (top) resting permeabilized platelets and (bottom) thrombin-activated platelet surface of horses that are Ref/Ref for SEL1L c.1810A>G p.Ile604Val. SEL1L did not localize to the surface in resting permeabilized platelets (top) but did localize to the surface in thrombin-activated platelets (bottom). n = 2. Original magnification, ×100. ( C ) Collagen spreading assay comparing median platelet area to genotype. There was a substantial difference between homozygous Ref and Alt genotypes. n = 11 Ref/Ref, 5 Ref/Alt, and 2 Alt/Alt.

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: Variant Assay

    ( A ) Flow cytometry analyses of human megakaryocytic surface markers from differentiated cord blood. CD61 hi CD42b hi megakaryocytes are observed after 2 weeks of differentiation. ( B ) Phase contrast microscopy of mature human megakaryocytes and ( C ) proplatelets. Scale bars: 50 μm. ( D ) Representative Western blot analysis of SEL1L during megakaryopoiesis and in platelets from peripheral blood. ( E ) Densitometric analyses of SEL1L isoforms ( n = 7, results are presented as mean ± SD). ** P < 0.01, *** P < 0.001, and **** P < 0.0001 by 1-way ANOVA with post hoc pairwise comparisons. ( F and G ) Immunofluorescence microscopy of megakaryocytes extending proplatelets. Scale bars: 30 μm. ( H ) Analysis of SEL1L fluorescence intensity in the megakaryocytic cell body and proplatelet tips. **** P < 0.0001 by 2-tailed Student’s t test.

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: ( A ) Flow cytometry analyses of human megakaryocytic surface markers from differentiated cord blood. CD61 hi CD42b hi megakaryocytes are observed after 2 weeks of differentiation. ( B ) Phase contrast microscopy of mature human megakaryocytes and ( C ) proplatelets. Scale bars: 50 μm. ( D ) Representative Western blot analysis of SEL1L during megakaryopoiesis and in platelets from peripheral blood. ( E ) Densitometric analyses of SEL1L isoforms ( n = 7, results are presented as mean ± SD). ** P < 0.01, *** P < 0.001, and **** P < 0.0001 by 1-way ANOVA with post hoc pairwise comparisons. ( F and G ) Immunofluorescence microscopy of megakaryocytes extending proplatelets. Scale bars: 30 μm. ( H ) Analysis of SEL1L fluorescence intensity in the megakaryocytic cell body and proplatelet tips. **** P < 0.0001 by 2-tailed Student’s t test.

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: Flow Cytometry, Microscopy, Western Blot, Immunofluorescence, Fluorescence

    ( A ) Representative images of murine platelets (green) adhering to a collagen-coated chamber after perfusion of whole blood from both a control Mx1-cre – Sel1l fl/fl and a knockdown Mx1-cre + Sel1l fl/fl mouse. Scale bars: 10 μm. ( B ) Quantification of the change in MFI between the beginning and end of the whole blood perfusion across collagen was normalized to the control for each pair. n = 6 cre + /cre – sibling pairs. * P < 0.05 by Wilcoxon’s matched-pairs signed-rank test; a significant decrease in MFI change was found between control and knockdown groups.

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: ( A ) Representative images of murine platelets (green) adhering to a collagen-coated chamber after perfusion of whole blood from both a control Mx1-cre – Sel1l fl/fl and a knockdown Mx1-cre + Sel1l fl/fl mouse. Scale bars: 10 μm. ( B ) Quantification of the change in MFI between the beginning and end of the whole blood perfusion across collagen was normalized to the control for each pair. n = 6 cre + /cre – sibling pairs. * P < 0.05 by Wilcoxon’s matched-pairs signed-rank test; a significant decrease in MFI change was found between control and knockdown groups.

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: Control, Knockdown

    TEG was performed on control Mx1-cre − Sel1l fl/fl ( n = 7) and knockdown Mx1-cre + Sel1l fl/fl ( n = 6) mice. The results showed ( A ) no significant difference in reaction time, ( B ) a significant decrease in maximum amplitude, ( C ) a significant increase in the time for the clot to reach a strength of 20 mm (K time), ( D ) a significant decrease in the rate of clot formation (α-angle), and ( E ) a significant decrease in maximal rate of thrombus generation. ( F ) Representative tracings and velocity curves show the difference between the control in black and the KO in gray. * P < 0.05 and *** P < 0.001 by 2-tailed Student’s t test.

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: TEG was performed on control Mx1-cre − Sel1l fl/fl ( n = 7) and knockdown Mx1-cre + Sel1l fl/fl ( n = 6) mice. The results showed ( A ) no significant difference in reaction time, ( B ) a significant decrease in maximum amplitude, ( C ) a significant increase in the time for the clot to reach a strength of 20 mm (K time), ( D ) a significant decrease in the rate of clot formation (α-angle), and ( E ) a significant decrease in maximal rate of thrombus generation. ( F ) Representative tracings and velocity curves show the difference between the control in black and the KO in gray. * P < 0.05 and *** P < 0.001 by 2-tailed Student’s t test.

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: Control, Knockdown

    Journal: The Journal of Clinical Investigation

    Article Title: ER-associated degradation pathway protein SEL1L plays an evolutionarily conserved role in platelet adhesion

    doi: 10.1172/JCI191433

    Figure Lengend Snippet: Human phenotypes associated with SEL1L variants

    Article Snippet: Washed equine platelets ( SEL1L A>G : n = 7 WT, 5 heterozygous, and 2 homozygous alternate) were fixed in 1% paraformaldehyde, permeabilized in 0.1% NP-40, and labeled with a monoclonal SEL1L antibody conjugated to AlexaFluor488 (Santa Cruz Biotechnology; sc-377350) and a monoclonal P selectin antibody conjugated to APC (Invitrogen; 17-0626-82).

    Techniques: