aal fitc  (Vector Laboratories)


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    Vector Laboratories aal fitc
    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate <t>(FITC)-conjugated</t> LTL (left) or <t>AAL</t> (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Aal Fitc, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aal fitc/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
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    Images

    1) Product Images from "Paeniclostridium sordellii hemorrhagic toxin targets TMPRSS2 to induce colonic epithelial lesions"

    Article Title: Paeniclostridium sordellii hemorrhagic toxin targets TMPRSS2 to induce colonic epithelial lesions

    Journal: Nature Communications

    doi: 10.1038/s41467-022-31994-x

    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate (FITC)-conjugated LTL (left) or AAL (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Figure Legend Snippet: a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate (FITC)-conjugated LTL (left) or AAL (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.

    Techniques Used: Flow Cytometry, Binding Assay, Expressing, Western Blot, Fluorescence, Labeling, Staining, Incubation

    aal fitc  (Vector Laboratories)


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    Vector Laboratories aal fitc
    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate <t>(FITC)-conjugated</t> LTL (left) or <t>AAL</t> (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Aal Fitc, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Paeniclostridium sordellii hemorrhagic toxin targets TMPRSS2 to induce colonic epithelial lesions"

    Article Title: Paeniclostridium sordellii hemorrhagic toxin targets TMPRSS2 to induce colonic epithelial lesions

    Journal: Nature Communications

    doi: 10.1038/s41467-022-31994-x

    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate (FITC)-conjugated LTL (left) or AAL (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Figure Legend Snippet: a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate (FITC)-conjugated LTL (left) or AAL (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.

    Techniques Used: Flow Cytometry, Binding Assay, Expressing, Western Blot, Fluorescence, Labeling, Staining, Incubation

    fluorescein aleuria aurantia lectin  (Vector Laboratories)


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    Vector Laboratories fluorescein aleuria aurantia lectin
    Fluorescein Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    fluorescein aleuria aurantia lectin  (Vector Laboratories)


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    Vector Laboratories fluorescein aleuria aurantia lectin
    Fluorescein Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    fitc labelled sna  (Vector Laboratories)


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    Vector Laboratories fitc labelled sna
    Fitc Labelled Sna, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    fluorescein isothiocyanate fitc labelled lectin sambucus nigra  (Vector Laboratories)


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    Vector Laboratories fluorescein isothiocyanate fitc labelled lectin sambucus nigra
    Fluorescein Isothiocyanate Fitc Labelled Lectin Sambucus Nigra, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    fluorescein labelled aleuria aurantia lectin aal  (Vector Laboratories)


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    Vector Laboratories fluorescein labelled aleuria aurantia lectin aal
    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. <t>Lectin</t> binding studies and quantification in fibroblasts. <t>Aleuria</t> aurantia lectin <t>(AAL)</t> was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Fluorescein Labelled Aleuria Aurantia Lectin Aal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein labelled aleuria aurantia lectin aal/product/Vector Laboratories
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    1) Product Images from "A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder"

    Article Title: A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder

    Journal: EMBO Molecular Medicine

    doi: 10.15252/emmm.202114332

    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. Lectin binding studies and quantification in fibroblasts. Aleuria aurantia lectin (AAL) was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Figure Legend Snippet: Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. Lectin binding studies and quantification in fibroblasts. Aleuria aurantia lectin (AAL) was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.

    Techniques Used: Western Blot, Expressing, SDS Page, Derivative Assay, Quantitative RT-PCR, In Vitro, Transformation Assay, Binding Assay, Staining, Infection, Introduce, Clone Assay, Plasmid Preparation, Transfection

    Aleuria aurantia lectin (AAL) was used to address the fucosylation level in sera of controls and the patient (left) which revealed significant loss of fucose residues in case of the patient. Data were obtained from serum; n = 6; experiment was independently repeated three times, for statistics an unpaired t ‐test was performed. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after therapy start Data information: ** P < 0.01. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Figure Legend Snippet: Aleuria aurantia lectin (AAL) was used to address the fucosylation level in sera of controls and the patient (left) which revealed significant loss of fucose residues in case of the patient. Data were obtained from serum; n = 6; experiment was independently repeated three times, for statistics an unpaired t ‐test was performed. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after therapy start Data information: ** P < 0.01. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.

    Techniques Used: Flow Cytometry, Staining

    A Merge of lectin (green) and DAPI (blue) staining of a control. B Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother. C Merge of lectin (green) and DAPI (blue) staining of the patient. D Lectin staining of a blood smear of a control (green). E Lectin staining of a blood smear of the heterozygous mother (green). F Lectin staining of a blood smear of the patient (green). G Digital enlargement of an image area of the control shown in Fig to show presence of AAL positive platelets (green). H Pappenheim staining of control to show presence of platelets. I Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). J Pappenheim staining of control to show presence of platelets. K Digital enlargement of an image area of the control shown in Fig to show lack of AAL positive platelets (green). L Pappenheim staining of control to show presence of platelets. A1 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother immediately before the first dose of fucose. B1 Merge of lectin (green) and DAPI (blue) staining of the patient immediately before the first dose of fucose. C1 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D1 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E1 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. A2 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 2 weeks of fucose therapy. B2 Merge of lectin (green) and DAPI (blue) staining of the patient after 2 weeks of fucose therapy. C2 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D2 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E2 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 2 weeks after the start of fucose therapy. A3 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 4 weeks of fucose therapy. B3 Merge of lectin (green) and DAPI (blue) staining of the patient after 4 weeks of fucose therapy. C3 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D3 Digital enlargement of an image area of the patient shown in Fig to show presence of AAL positive platelets (green). E3 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 4 weeks after the start of fucose therapy. A4 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 8 weeks of fucose therapy. B4 Merge of lectin (green) and DA.PI (blue) staining of the patient after 8 weeks of fucose therapy. C4 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D4 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E4 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after the start of fucose therapy. Data information: Green: Aleuria aurantia lectin; Blue: DAPI. PBMCs are highlighted by a white arrow in panel E. Platelets are highlighted by white or black arrows. Pappenheim images were taken with a 40x magnification. No lectin staining of platelets was visible in the blood smear of the individual (K). Pappenheim staining of the patient's blood showed presence of platelets (L). Scale bars = 50 µm with exception of C1, D1, C2, D2, C3, D3, C4, D4, here 10 µm scale bars are shown. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy.
    Figure Legend Snippet: A Merge of lectin (green) and DAPI (blue) staining of a control. B Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother. C Merge of lectin (green) and DAPI (blue) staining of the patient. D Lectin staining of a blood smear of a control (green). E Lectin staining of a blood smear of the heterozygous mother (green). F Lectin staining of a blood smear of the patient (green). G Digital enlargement of an image area of the control shown in Fig to show presence of AAL positive platelets (green). H Pappenheim staining of control to show presence of platelets. I Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). J Pappenheim staining of control to show presence of platelets. K Digital enlargement of an image area of the control shown in Fig to show lack of AAL positive platelets (green). L Pappenheim staining of control to show presence of platelets. A1 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother immediately before the first dose of fucose. B1 Merge of lectin (green) and DAPI (blue) staining of the patient immediately before the first dose of fucose. C1 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D1 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E1 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. A2 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 2 weeks of fucose therapy. B2 Merge of lectin (green) and DAPI (blue) staining of the patient after 2 weeks of fucose therapy. C2 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D2 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E2 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 2 weeks after the start of fucose therapy. A3 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 4 weeks of fucose therapy. B3 Merge of lectin (green) and DAPI (blue) staining of the patient after 4 weeks of fucose therapy. C3 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D3 Digital enlargement of an image area of the patient shown in Fig to show presence of AAL positive platelets (green). E3 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 4 weeks after the start of fucose therapy. A4 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 8 weeks of fucose therapy. B4 Merge of lectin (green) and DA.PI (blue) staining of the patient after 8 weeks of fucose therapy. C4 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D4 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E4 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after the start of fucose therapy. Data information: Green: Aleuria aurantia lectin; Blue: DAPI. PBMCs are highlighted by a white arrow in panel E. Platelets are highlighted by white or black arrows. Pappenheim images were taken with a 40x magnification. No lectin staining of platelets was visible in the blood smear of the individual (K). Pappenheim staining of the patient's blood showed presence of platelets (L). Scale bars = 50 µm with exception of C1, D1, C2, D2, C3, D3, C4, D4, here 10 µm scale bars are shown. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy.

    Techniques Used: Staining, Flow Cytometry

    A–D Blood samples were taken 2 months prior to therapy initiation. (A, C) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (B, D) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. E, F Lectin staining of serum proteins taken 2, 4 and 8 weeks after start of fucose therapy. (E) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (F) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. G Lectin blots revealed a severe reduction of protein fucosylation in patient serum and PBMCs. Data information: A severe reduction of fucosylated proteins is present in serum and PBMCs of the affected individual compared to her mother 2 month before start of fucose treatment. M: mother; P: affected individual. Source data are available online for this figure.
    Figure Legend Snippet: A–D Blood samples were taken 2 months prior to therapy initiation. (A, C) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (B, D) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. E, F Lectin staining of serum proteins taken 2, 4 and 8 weeks after start of fucose therapy. (E) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (F) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. G Lectin blots revealed a severe reduction of protein fucosylation in patient serum and PBMCs. Data information: A severe reduction of fucosylated proteins is present in serum and PBMCs of the affected individual compared to her mother 2 month before start of fucose treatment. M: mother; P: affected individual. Source data are available online for this figure.

    Techniques Used: Staining

    fluorescein labeled aleuria aurantia lectin aal  (Vector Laboratories)


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    Vector Laboratories fluorescein labeled aleuria aurantia lectin aal
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    Vector Laboratories fluorescein labeled aleuria aurantia lectin
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    Vector Laboratories fluorescein labeled aleuria aurantia lectin
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    Vector Laboratories fluorescein labelled aleuria aurantia lectin
    Fluorescein Labelled Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories aal fitc
    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate <t>(FITC)-conjugated</t> LTL (left) or <t>AAL</t> (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Aal Fitc, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories fluorescein aleuria aurantia lectin
    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate <t>(FITC)-conjugated</t> LTL (left) or <t>AAL</t> (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Fluorescein Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories fitc labelled sna
    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate <t>(FITC)-conjugated</t> LTL (left) or <t>AAL</t> (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Fitc Labelled Sna, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories fluorescein isothiocyanate fitc labelled lectin sambucus nigra
    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate <t>(FITC)-conjugated</t> LTL (left) or <t>AAL</t> (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.
    Fluorescein Isothiocyanate Fitc Labelled Lectin Sambucus Nigra, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories fluorescein labelled aleuria aurantia lectin aal
    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. <t>Lectin</t> binding studies and quantification in fibroblasts. <t>Aleuria</t> aurantia lectin <t>(AAL)</t> was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Fluorescein Labelled Aleuria Aurantia Lectin Aal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories fluorescein labeled aleuria aurantia lectin aal
    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. <t>Lectin</t> binding studies and quantification in fibroblasts. <t>Aleuria</t> aurantia lectin <t>(AAL)</t> was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Fluorescein Labeled Aleuria Aurantia Lectin Aal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Vector Laboratories fluorescein labeled aleuria aurantia lectin
    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. <t>Lectin</t> binding studies and quantification in fibroblasts. <t>Aleuria</t> aurantia lectin <t>(AAL)</t> was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Fluorescein Labeled Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein labeled aleuria aurantia lectin/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fluorescein labeled aleuria aurantia lectin - by Bioz Stars, 2024-05
    93/100 stars
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    93
    Vector Laboratories fluorescein labelled aleuria aurantia lectin
    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. <t>Lectin</t> binding studies and quantification in fibroblasts. <t>Aleuria</t> aurantia lectin <t>(AAL)</t> was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.
    Fluorescein Labelled Aleuria Aurantia Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein labelled aleuria aurantia lectin/product/Vector Laboratories
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fluorescein labelled aleuria aurantia lectin - by Bioz Stars, 2024-05
    93/100 stars
      Buy from Supplier

    Image Search Results


    a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate (FITC)-conjugated LTL (left) or AAL (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.

    Journal: Nature Communications

    Article Title: Paeniclostridium sordellii hemorrhagic toxin targets TMPRSS2 to induce colonic epithelial lesions

    doi: 10.1038/s41467-022-31994-x

    Figure Lengend Snippet: a The sensitivities of MCF-7 TMPRSS2 ‒/‒ , GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cell lines to TcsH were measured using the cytopathic cell-rounding assay. Error bars represent mean ± s.d., n = 6. b Schematic view of biosynthesis of fucosylated glycans, genes identified from the screens were highlighted. c Flow cytometry profiles of fluorescein isothiocyanate (FITC)-conjugated LTL (left) or AAL (right) binding to MCF-7 WT and KO cells. d The absence of TMPRSS2 expression in the MCF-7 TMPRSS2 ‒/‒ cells was validated by Western blot analysis. The MCF-7 GMDS ‒/‒ , FUT4 ‒/‒ , and SLC35C1 ‒/‒ cells have similar TMPRSS2 expression levels compared to the WT cells. The experiments have been repeated independently twice with similar results. e Confocal fluorescence images show Rhodamine-labeled TcsH (green) or GFP-TcsH 1832–2618 (green) bindings to the MCF-7 WT, GMDS ‒/‒ , FUT4 ‒/‒ , SLC35C1 ‒/‒ , and TMPRSS2 ‒/‒ cells, respectively. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm. f Co-incubation of the AAL (8 μg/mL) with TcsH (10 pM, 3.5 h) protected MCF-7 cells from intoxication and prevented cell rounding. g Confocal fluorescence images show binding of different GFP-fused TcsH CROPs fragments to the MCF-7 cells. Cell nuclei were stained by Hoechst (blue). The scale bar represents 50 μm.

    Article Snippet: The following antibodies and reagents were purchased from the commercial vendors: mouse monoclonal antibody against non-glucosylated RAC1 (Clone 102, #610650, BD Biosciences, 1:1000), total RAC1 (Clone 23A8, MA1-20580, Invitrogen, 1:1000), and Flag-tag (Clone 5A8E5, A01809, GenScript, 1:200), rabbit monoclonal antibody against TMPRSS2 (Clone EPR3862, ab109131, Abcam, 1:2000 for Western blot) and β-actin (Clone AC-15, #078M4809V, Sigma, 1:5000), rabbit polyclonal antibody against TMPRSS2 (14437-1-AP, Proteintech, 1:1000 for IHC), horseradish peroxidase-labeled goat anti-rabbit IgG (H + L, PI-1000, Vector Labs, 1:10000 for Western blot), horseradish peroxidase-labeled goat anti-mouse IgG (H + L, PI-1000, Vector Labs, 1:10000 for Western blot), Precast PAGE Gel (abs9308, Absin), Hoechst 33258 (E607301, BBI), LTL-FITC (FL-1321, Vector Laboratories), AAL-FITC (FL-1391, Vector Laboratories), Camostat mesylate (HY-13512, MCE), Polyethylenimine Linear (40816ES03, Yeasen), and NHS-Rhodamine fluorescent labeling kit (#46406, ThermoFisher Scientific).

    Techniques: Flow Cytometry, Binding Assay, Expressing, Western Blot, Fluorescence, Labeling, Staining, Incubation

    Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. Lectin binding studies and quantification in fibroblasts. Aleuria aurantia lectin (AAL) was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.

    Journal: EMBO Molecular Medicine

    Article Title: A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder

    doi: 10.15252/emmm.202114332

    Figure Lengend Snippet: Western blot analysis and quantification of GFUS. Expression of GFUS was analysed by western blotting on a 15% SDS–PAGE with cytosolic fractions derived from control and patient fibroblasts. Quantification revealed a significant decrease of GFUS protein. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. mRNA expression studies. qRT–PCR studies showed a significant decrease in mRNA level of GFUS by 40.0% (± 9.3%, ** P = 0.0010) normalized to a control. Also, expression of SLC35C1 and SLC35C2 were significantly decreased in patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 10; experiment was independently repeated three times, for statistics an one‐way ANOVA was performed. Conversion of GDP‐D‐mannose into GDP‐L‐fucose. The conversion GDP‐D‐[ 14 C]mannose to GDP‐L‐[ 14 C]fucose was analysed in an in vitro assay. After 1 h, nearly half of GDP‐D‐mannose was transformed to GDP‐fucose in the control cell line, whereas the patient's fibroblasts were nearly unable to catalyse the reaction. Data were obtained from fibroblasts; n = 1. Lectin binding studies and quantification in fibroblasts. Aleuria aurantia lectin (AAL) was used to address the fucosylation level in fibroblasts. AAL staining was performed before and after treatment of the patient cell line with 100 µM L‐fucose. Before sugar supplementation, a significant loss of AAL signal strength was measured, whereas after treatment a significant re‐fucosylation was detected. Data were obtained from fibroblasts; n = 4; experiment was independently repeated four times, for statistics an unpaired t ‐test was performed. Complementation study with patient‐derived fibroblasts. Viral infection was used to introduce an empty cloning vector and the wild‐type GFUS cDNA in patient cells, respectively. For analysis lysates of a control cell line, a control cell line supplemented with 100 µM fucose, patient cells, patient cells supplemented with 100 µM fucose, patient cells transfected with an empty vector and patient cells transfected with wild‐type GFUS were analysed by AAL staining clearly indicating the disease‐causing influence of the defective GFUS in the patient. Western blot analysis against GFUS further showed expression of wild‐type GFUS protein in the infected patient‐derived fibroblasts. Data were obtained from fibroblasts; n = 4; experiment was independently repeated two times, for statistics an one‐way ANOVA was performed. Data information: * P < 0.05; ** P < 0.01; *** P < 0.001. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.

    Article Snippet: Blood smears were washed 3 × 3 min in PBS and incubated for 30 min with fluorescein‐labelled Aleuria aurantia lectin (AAL) (Vectorlabs, VECFL‐1391).

    Techniques: Western Blot, Expressing, SDS Page, Derivative Assay, Quantitative RT-PCR, In Vitro, Transformation Assay, Binding Assay, Staining, Infection, Introduce, Clone Assay, Plasmid Preparation, Transfection

    Aleuria aurantia lectin (AAL) was used to address the fucosylation level in sera of controls and the patient (left) which revealed significant loss of fucose residues in case of the patient. Data were obtained from serum; n = 6; experiment was independently repeated three times, for statistics an unpaired t ‐test was performed. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after therapy start Data information: ** P < 0.01. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.

    Journal: EMBO Molecular Medicine

    Article Title: A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder

    doi: 10.15252/emmm.202114332

    Figure Lengend Snippet: Aleuria aurantia lectin (AAL) was used to address the fucosylation level in sera of controls and the patient (left) which revealed significant loss of fucose residues in case of the patient. Data were obtained from serum; n = 6; experiment was independently repeated three times, for statistics an unpaired t ‐test was performed. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. FACS analysis of PBMCs. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after therapy start Data information: ** P < 0.01. Bars and error bars represent mean ± SD. Exact P ‐values are reported in the results part.

    Article Snippet: Blood smears were washed 3 × 3 min in PBS and incubated for 30 min with fluorescein‐labelled Aleuria aurantia lectin (AAL) (Vectorlabs, VECFL‐1391).

    Techniques: Flow Cytometry, Staining

    A Merge of lectin (green) and DAPI (blue) staining of a control. B Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother. C Merge of lectin (green) and DAPI (blue) staining of the patient. D Lectin staining of a blood smear of a control (green). E Lectin staining of a blood smear of the heterozygous mother (green). F Lectin staining of a blood smear of the patient (green). G Digital enlargement of an image area of the control shown in Fig to show presence of AAL positive platelets (green). H Pappenheim staining of control to show presence of platelets. I Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). J Pappenheim staining of control to show presence of platelets. K Digital enlargement of an image area of the control shown in Fig to show lack of AAL positive platelets (green). L Pappenheim staining of control to show presence of platelets. A1 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother immediately before the first dose of fucose. B1 Merge of lectin (green) and DAPI (blue) staining of the patient immediately before the first dose of fucose. C1 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D1 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E1 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. A2 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 2 weeks of fucose therapy. B2 Merge of lectin (green) and DAPI (blue) staining of the patient after 2 weeks of fucose therapy. C2 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D2 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E2 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 2 weeks after the start of fucose therapy. A3 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 4 weeks of fucose therapy. B3 Merge of lectin (green) and DAPI (blue) staining of the patient after 4 weeks of fucose therapy. C3 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D3 Digital enlargement of an image area of the patient shown in Fig to show presence of AAL positive platelets (green). E3 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 4 weeks after the start of fucose therapy. A4 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 8 weeks of fucose therapy. B4 Merge of lectin (green) and DA.PI (blue) staining of the patient after 8 weeks of fucose therapy. C4 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D4 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E4 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after the start of fucose therapy. Data information: Green: Aleuria aurantia lectin; Blue: DAPI. PBMCs are highlighted by a white arrow in panel E. Platelets are highlighted by white or black arrows. Pappenheim images were taken with a 40x magnification. No lectin staining of platelets was visible in the blood smear of the individual (K). Pappenheim staining of the patient's blood showed presence of platelets (L). Scale bars = 50 µm with exception of C1, D1, C2, D2, C3, D3, C4, D4, here 10 µm scale bars are shown. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy.

    Journal: EMBO Molecular Medicine

    Article Title: A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder

    doi: 10.15252/emmm.202114332

    Figure Lengend Snippet: A Merge of lectin (green) and DAPI (blue) staining of a control. B Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother. C Merge of lectin (green) and DAPI (blue) staining of the patient. D Lectin staining of a blood smear of a control (green). E Lectin staining of a blood smear of the heterozygous mother (green). F Lectin staining of a blood smear of the patient (green). G Digital enlargement of an image area of the control shown in Fig to show presence of AAL positive platelets (green). H Pappenheim staining of control to show presence of platelets. I Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). J Pappenheim staining of control to show presence of platelets. K Digital enlargement of an image area of the control shown in Fig to show lack of AAL positive platelets (green). L Pappenheim staining of control to show presence of platelets. A1 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother immediately before the first dose of fucose. B1 Merge of lectin (green) and DAPI (blue) staining of the patient immediately before the first dose of fucose. C1 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D1 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E1 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy. A2 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 2 weeks of fucose therapy. B2 Merge of lectin (green) and DAPI (blue) staining of the patient after 2 weeks of fucose therapy. C2 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D2 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E2 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 2 weeks after the start of fucose therapy. A3 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 4 weeks of fucose therapy. B3 Merge of lectin (green) and DAPI (blue) staining of the patient after 4 weeks of fucose therapy. C3 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D3 Digital enlargement of an image area of the patient shown in Fig to show presence of AAL positive platelets (green). E3 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 4 weeks after the start of fucose therapy. A4 Merge of lectin (green) and DAPI (blue) staining of the heterozygous mother after 8 weeks of fucose therapy. B4 Merge of lectin (green) and DA.PI (blue) staining of the patient after 8 weeks of fucose therapy. C4 Digital enlargement of an image area of the heterozygous mother shown in Fig to show presence of AAL positive platelets (green). D4 Digital enlargement of an image area of the patient shown in Fig to show lack of AAL positive platelets (green). E4 FACS analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) 8 weeks after the start of fucose therapy. Data information: Green: Aleuria aurantia lectin; Blue: DAPI. PBMCs are highlighted by a white arrow in panel E. Platelets are highlighted by white or black arrows. Pappenheim images were taken with a 40x magnification. No lectin staining of platelets was visible in the blood smear of the individual (K). Pappenheim staining of the patient's blood showed presence of platelets (L). Scale bars = 50 µm with exception of C1, D1, C2, D2, C3, D3, C4, D4, here 10 µm scale bars are shown. Results of flow cytometry analysis of patient (red) and control (green) PBMCs stained with 1 µg/ml FAA lectin without (dark) or with 200 mM L‐fucose (light) before the start of fucose therapy.

    Article Snippet: Blood smears were washed 3 × 3 min in PBS and incubated for 30 min with fluorescein‐labelled Aleuria aurantia lectin (AAL) (Vectorlabs, VECFL‐1391).

    Techniques: Staining, Flow Cytometry

    A–D Blood samples were taken 2 months prior to therapy initiation. (A, C) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (B, D) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. E, F Lectin staining of serum proteins taken 2, 4 and 8 weeks after start of fucose therapy. (E) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (F) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. G Lectin blots revealed a severe reduction of protein fucosylation in patient serum and PBMCs. Data information: A severe reduction of fucosylated proteins is present in serum and PBMCs of the affected individual compared to her mother 2 month before start of fucose treatment. M: mother; P: affected individual. Source data are available online for this figure.

    Journal: EMBO Molecular Medicine

    Article Title: A spoonful of L‐fucose—an efficient therapy for GFUS‐CDG, a new glycosylation disorder

    doi: 10.15252/emmm.202114332

    Figure Lengend Snippet: A–D Blood samples were taken 2 months prior to therapy initiation. (A, C) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (B, D) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. E, F Lectin staining of serum proteins taken 2, 4 and 8 weeks after start of fucose therapy. (E) Ponceau red staining which was used as loading control. In addition, different volumes were separated for better comparability. (F) Blots probed with the Aleuria aurantia lectin for visualization of core‐fucosylated proteins. G Lectin blots revealed a severe reduction of protein fucosylation in patient serum and PBMCs. Data information: A severe reduction of fucosylated proteins is present in serum and PBMCs of the affected individual compared to her mother 2 month before start of fucose treatment. M: mother; P: affected individual. Source data are available online for this figure.

    Article Snippet: Blood smears were washed 3 × 3 min in PBS and incubated for 30 min with fluorescein‐labelled Aleuria aurantia lectin (AAL) (Vectorlabs, VECFL‐1391).

    Techniques: Staining