biotinylated plant lectins mal  (Vector Laboratories)


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    Vector Laboratories biotinylated plant lectins mal
    Biotinylated Plant Lectins Mal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    biotinylated galananthus novalis lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated galananthus novalis lectin
    A Binding of α-swH1N2 virus to a sialoside microarray containing glycans with α2-3 or α2-6 linked sialic acids representing avian-type and human-type influenza receptors, respectively. Bars represent the fluorescence intensity of bound α-swH1N2. Glycan structures corresponding to numbers are shown on the x-axis are found in Supplementary Table . Signal values are calculated from the mean intensities of 4 of 6 replicate spots with the highest and lowest signal omitted. B Replication of swine influenza virus in human bronchial epithelial (HBE) air-liquid interface cell cultures. HBE cell cultures were infected in triplicate with 10 3 TCID 50 (tissue culture infectious dose 50) per well of H1N1pdm09, γ-swH1N1, or α-swH1N2. The apical supernatant was collected at the indicated time points and virus titers were determined on MDCK cells using TCID 50 assays. A ratio of swine virus titer relative to H1N1pdm09 titer at 24 and 48 h of all HBE patient cell cultures is shown. Each dot represents an average of three technical replicates per HBE culture, and seven biological replicates from different HBE patient cultures are displayed. Data are presented as mean values +/− SD of the seven biological replicates each with three technical replicates. C Stability of α-swH1N2 influenza virus in small droplets over a range of relative humidity (RH) conditions. Ten 1 uL droplets of pooled virus from panel B were spotted into the wells of a tissue culture dish for 2 h. Decay of the virus at each RH was calculated compared to the titer of ten 1 uL droplets deposited and immediately recovered from a tissue culture dish. Log 10 decay of HBE-propagated H1N1pdm09 (black) and α-swH1N2 (green) is shown and represents mean values (±SD) from eight biological replicates performed in three technical replicates. D H1N1pdm09 (gray, N = 8) and α-swH1N2 (green, N = 4) viruses were incubated in PBS solutions of different pHs for 1 h at 37 °C. Virus titers were determined by TCID 50 assay and the EC 50 values were plotted using regression analysis of the dose-response curve. The reported mean corresponds to at least four independent biological replicates, each performed in three technical replicates. E The NA activities of H1N1pdm09 (gray) and α-swH1N2 (green) were determined using an enzyme-linked <t>lectin</t> assay with fetuin as the substrate. Viruses were normalized for equal infectivity and displayed data are the mean (±SD) of three independent biological replicates performed in technical duplicates.
    Biotinylated Galananthus Novalis Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Potential pandemic risk of circulating swine H1N2 influenza viruses"

    Article Title: Potential pandemic risk of circulating swine H1N2 influenza viruses

    Journal: Nature Communications

    doi: 10.1038/s41467-024-49117-z

    A Binding of α-swH1N2 virus to a sialoside microarray containing glycans with α2-3 or α2-6 linked sialic acids representing avian-type and human-type influenza receptors, respectively. Bars represent the fluorescence intensity of bound α-swH1N2. Glycan structures corresponding to numbers are shown on the x-axis are found in Supplementary Table . Signal values are calculated from the mean intensities of 4 of 6 replicate spots with the highest and lowest signal omitted. B Replication of swine influenza virus in human bronchial epithelial (HBE) air-liquid interface cell cultures. HBE cell cultures were infected in triplicate with 10 3 TCID 50 (tissue culture infectious dose 50) per well of H1N1pdm09, γ-swH1N1, or α-swH1N2. The apical supernatant was collected at the indicated time points and virus titers were determined on MDCK cells using TCID 50 assays. A ratio of swine virus titer relative to H1N1pdm09 titer at 24 and 48 h of all HBE patient cell cultures is shown. Each dot represents an average of three technical replicates per HBE culture, and seven biological replicates from different HBE patient cultures are displayed. Data are presented as mean values +/− SD of the seven biological replicates each with three technical replicates. C Stability of α-swH1N2 influenza virus in small droplets over a range of relative humidity (RH) conditions. Ten 1 uL droplets of pooled virus from panel B were spotted into the wells of a tissue culture dish for 2 h. Decay of the virus at each RH was calculated compared to the titer of ten 1 uL droplets deposited and immediately recovered from a tissue culture dish. Log 10 decay of HBE-propagated H1N1pdm09 (black) and α-swH1N2 (green) is shown and represents mean values (±SD) from eight biological replicates performed in three technical replicates. D H1N1pdm09 (gray, N = 8) and α-swH1N2 (green, N = 4) viruses were incubated in PBS solutions of different pHs for 1 h at 37 °C. Virus titers were determined by TCID 50 assay and the EC 50 values were plotted using regression analysis of the dose-response curve. The reported mean corresponds to at least four independent biological replicates, each performed in three technical replicates. E The NA activities of H1N1pdm09 (gray) and α-swH1N2 (green) were determined using an enzyme-linked lectin assay with fetuin as the substrate. Viruses were normalized for equal infectivity and displayed data are the mean (±SD) of three independent biological replicates performed in technical duplicates.
    Figure Legend Snippet: A Binding of α-swH1N2 virus to a sialoside microarray containing glycans with α2-3 or α2-6 linked sialic acids representing avian-type and human-type influenza receptors, respectively. Bars represent the fluorescence intensity of bound α-swH1N2. Glycan structures corresponding to numbers are shown on the x-axis are found in Supplementary Table . Signal values are calculated from the mean intensities of 4 of 6 replicate spots with the highest and lowest signal omitted. B Replication of swine influenza virus in human bronchial epithelial (HBE) air-liquid interface cell cultures. HBE cell cultures were infected in triplicate with 10 3 TCID 50 (tissue culture infectious dose 50) per well of H1N1pdm09, γ-swH1N1, or α-swH1N2. The apical supernatant was collected at the indicated time points and virus titers were determined on MDCK cells using TCID 50 assays. A ratio of swine virus titer relative to H1N1pdm09 titer at 24 and 48 h of all HBE patient cell cultures is shown. Each dot represents an average of three technical replicates per HBE culture, and seven biological replicates from different HBE patient cultures are displayed. Data are presented as mean values +/− SD of the seven biological replicates each with three technical replicates. C Stability of α-swH1N2 influenza virus in small droplets over a range of relative humidity (RH) conditions. Ten 1 uL droplets of pooled virus from panel B were spotted into the wells of a tissue culture dish for 2 h. Decay of the virus at each RH was calculated compared to the titer of ten 1 uL droplets deposited and immediately recovered from a tissue culture dish. Log 10 decay of HBE-propagated H1N1pdm09 (black) and α-swH1N2 (green) is shown and represents mean values (±SD) from eight biological replicates performed in three technical replicates. D H1N1pdm09 (gray, N = 8) and α-swH1N2 (green, N = 4) viruses were incubated in PBS solutions of different pHs for 1 h at 37 °C. Virus titers were determined by TCID 50 assay and the EC 50 values were plotted using regression analysis of the dose-response curve. The reported mean corresponds to at least four independent biological replicates, each performed in three technical replicates. E The NA activities of H1N1pdm09 (gray) and α-swH1N2 (green) were determined using an enzyme-linked lectin assay with fetuin as the substrate. Viruses were normalized for equal infectivity and displayed data are the mean (±SD) of three independent biological replicates performed in technical duplicates.

    Techniques Used: Binding Assay, Virus, Microarray, Fluorescence, Infection, Incubation

    biotinylated mal ii lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated mal ii lectin
    (A) Analysis of the correlation between key genes for sialic acid synthesis mRNA expression and CD274 (PD-L1) in tumors using the TIMER 2.0 tool. (B) Analysis of the fold change in key genes for sialic acid synthesis mRNA expression in the PD-L1 high group compared to the PD-L1 low group, compiled from TCGA data. (C) <t>Lectin</t> blot analysis of the sialic acid level in RAW264.7 cells after treated by PD-L1 nanobody (Nb16). (D) Quantitative PCR analysis of Cd274 mRNA expression in RAW264.7 cells after treated by sialidase (Sia).
    Biotinylated Mal Ii Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "A nanobody-enzyme fusion protein targeting PD-L1 and sialic acid exerts anti-tumor effects by affecting tumor associated macrophages"

    Article Title: A nanobody-enzyme fusion protein targeting PD-L1 and sialic acid exerts anti-tumor effects by affecting tumor associated macrophages

    Journal: bioRxiv

    doi: 10.1101/2024.06.05.597674

    (A) Analysis of the correlation between key genes for sialic acid synthesis mRNA expression and CD274 (PD-L1) in tumors using the TIMER 2.0 tool. (B) Analysis of the fold change in key genes for sialic acid synthesis mRNA expression in the PD-L1 high group compared to the PD-L1 low group, compiled from TCGA data. (C) Lectin blot analysis of the sialic acid level in RAW264.7 cells after treated by PD-L1 nanobody (Nb16). (D) Quantitative PCR analysis of Cd274 mRNA expression in RAW264.7 cells after treated by sialidase (Sia).
    Figure Legend Snippet: (A) Analysis of the correlation between key genes for sialic acid synthesis mRNA expression and CD274 (PD-L1) in tumors using the TIMER 2.0 tool. (B) Analysis of the fold change in key genes for sialic acid synthesis mRNA expression in the PD-L1 high group compared to the PD-L1 low group, compiled from TCGA data. (C) Lectin blot analysis of the sialic acid level in RAW264.7 cells after treated by PD-L1 nanobody (Nb16). (D) Quantitative PCR analysis of Cd274 mRNA expression in RAW264.7 cells after treated by sialidase (Sia).

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction

    (A) KEGG analysis of the differential genes between Sia-treated group and negative control. (B) GSEA enrichment analysis of C-type lectin pathway. (C) Heatmap of the differential genes in C-type lectin pathway. (D) Representative image of western blot in detecting SYK, JNK and NOS2 expression at protein level. The quantitative results are analyzed by gray value and shown (E). Table1 Pharmacokinetic parameters of Nb16-Sia after intraperitoneal injection of a single dose of Nb16-Sia (5 mg/kg) in mice.
    Figure Legend Snippet: (A) KEGG analysis of the differential genes between Sia-treated group and negative control. (B) GSEA enrichment analysis of C-type lectin pathway. (C) Heatmap of the differential genes in C-type lectin pathway. (D) Representative image of western blot in detecting SYK, JNK and NOS2 expression at protein level. The quantitative results are analyzed by gray value and shown (E). Table1 Pharmacokinetic parameters of Nb16-Sia after intraperitoneal injection of a single dose of Nb16-Sia (5 mg/kg) in mice.

    Techniques Used: Negative Control, Western Blot, Expressing, Injection

    biotinylated lectin solution con a  (Vector Laboratories)


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    Vector Laboratories biotinylated lectin solution con a
    Detection and persistence of <t>lectin,</t> antibody, and DNA targets on keratinocyte cells on the panel of substrates. 5000 keratinocyte cells were seeded on 10 substrates. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of keratinocyte cells on substrates thanks to SEM. The second and third images showed keratinocyte cells visualized by confocal microscopy. For raw wood, no SEM images could be taken due to the fibrous nature of the substrate. Cells were incubated in the presence of <t>Con</t> <t>A</t> lectin (orange) that recognizes mannose carbohydrates, or labelled with antibody specifically directed against keratin 10 (Green). DNA from nuclei was stained with Hoechst 33342 (Blue). Images are representative data from three independent experiments. Scale bar: 10 µm.
    Biotinylated Lectin Solution Con A, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Detection of invisible biological traces in relation to the physicochemical properties of substrates surfaces in forensic casework"

    Article Title: Detection of invisible biological traces in relation to the physicochemical properties of substrates surfaces in forensic casework

    Journal: Scientific Reports

    doi: 10.1038/s41598-024-63911-1

    Detection and persistence of lectin, antibody, and DNA targets on keratinocyte cells on the panel of substrates. 5000 keratinocyte cells were seeded on 10 substrates. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of keratinocyte cells on substrates thanks to SEM. The second and third images showed keratinocyte cells visualized by confocal microscopy. For raw wood, no SEM images could be taken due to the fibrous nature of the substrate. Cells were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates, or labelled with antibody specifically directed against keratin 10 (Green). DNA from nuclei was stained with Hoechst 33342 (Blue). Images are representative data from three independent experiments. Scale bar: 10 µm.
    Figure Legend Snippet: Detection and persistence of lectin, antibody, and DNA targets on keratinocyte cells on the panel of substrates. 5000 keratinocyte cells were seeded on 10 substrates. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of keratinocyte cells on substrates thanks to SEM. The second and third images showed keratinocyte cells visualized by confocal microscopy. For raw wood, no SEM images could be taken due to the fibrous nature of the substrate. Cells were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates, or labelled with antibody specifically directed against keratin 10 (Green). DNA from nuclei was stained with Hoechst 33342 (Blue). Images are representative data from three independent experiments. Scale bar: 10 µm.

    Techniques Used: Adhesive, Confocal Microscopy, Incubation, Staining

    Detection and persistence of lectin, antibody, and DNA targets on fingermarks on the panel of substrates. Fingermarks were deposited on 10 substrates for 10 s. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of fingermarks on substrates thanks to SEM. The second and third images showed fingermarks visualized by confocal microscopy. Fingermarks were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates or labelled with antibody specifically directed against keratin 10 (K10, green). DNA was stained with Hoechst 33342 (blue). Images are representative data from three independent experiments. Scale bar: 10 µm.
    Figure Legend Snippet: Detection and persistence of lectin, antibody, and DNA targets on fingermarks on the panel of substrates. Fingermarks were deposited on 10 substrates for 10 s. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of fingermarks on substrates thanks to SEM. The second and third images showed fingermarks visualized by confocal microscopy. Fingermarks were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates or labelled with antibody specifically directed against keratin 10 (K10, green). DNA was stained with Hoechst 33342 (blue). Images are representative data from three independent experiments. Scale bar: 10 µm.

    Techniques Used: Adhesive, Confocal Microscopy, Incubation, Staining

    biotinylated plant lectins mal  (Vector Laboratories)


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    Vector Laboratories biotinylated plant lectins mal
    Biotinylated Plant Lectins Mal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    biotinylated lectins  (Vector Laboratories)


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    Vector Laboratories biotinylated lectins
    <t> Lectins </t> used in this study, and the glycans to which they bind, according to CFG data. <t> Lectins </t> displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .
    Biotinylated Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins"

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms25115725

     Lectins  used in this study, and the glycans to which they bind, according to CFG data.  Lectins  displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .
    Figure Legend Snippet: Lectins used in this study, and the glycans to which they bind, according to CFG data. Lectins displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .

    Techniques Used: Binding Assay, Flow Cytometry

    Solid-phase detection of lectin binding to MVs. MVs were derived from EA.hy 926 cells and immobilized on glass slides (solid-phase assay), incubated with biotinylated lectins, and then visualized with Str-Alexa Fluor 555, as described in the Materials and Methods section.
    Figure Legend Snippet: Solid-phase detection of lectin binding to MVs. MVs were derived from EA.hy 926 cells and immobilized on glass slides (solid-phase assay), incubated with biotinylated lectins, and then visualized with Str-Alexa Fluor 555, as described in the Materials and Methods section.

    Techniques Used: Binding Assay, Derivative Assay, Incubation

    Flow cytometry detection of lectins DSA and SNA binding to glycosidase-treated MVs. MVs were incubated with either β-galactosidase or neuraminidase, washed and incubated with biotinylated lectins, as described in the Materials and Methods section. In the dot plots, forward scatter (FS) was plotted against the logarithm of fluorescence (FL1) and the number given in the rectangles (for the purple dots) indicate the percentage of lectin bound to MVs.
    Figure Legend Snippet: Flow cytometry detection of lectins DSA and SNA binding to glycosidase-treated MVs. MVs were incubated with either β-galactosidase or neuraminidase, washed and incubated with biotinylated lectins, as described in the Materials and Methods section. In the dot plots, forward scatter (FS) was plotted against the logarithm of fluorescence (FL1) and the number given in the rectangles (for the purple dots) indicate the percentage of lectin bound to MVs.

    Techniques Used: Flow Cytometry, Binding Assay, Incubation, Fluorescence

    Flow cytometry binding of lectins to EA.hy 926 cells. Cells were incubated with biotinylated lectins followed by Str-FITC, as described in the Materials and Methods Section. Results shown include data from four experiments and error bars represent standard deviations. A mean fluorescence <50 was considered as negative.
    Figure Legend Snippet: Flow cytometry binding of lectins to EA.hy 926 cells. Cells were incubated with biotinylated lectins followed by Str-FITC, as described in the Materials and Methods Section. Results shown include data from four experiments and error bars represent standard deviations. A mean fluorescence <50 was considered as negative.

    Techniques Used: Flow Cytometry, Binding Assay, Incubation, Fluorescence

    Binding of lectins to MVs derived from EA.hy 926 cells treated with inhibitors to N -glycosylation, DMJ ( A ) or O -glycosylation, GalNAcαBn ( B ). MVs were isolated from native cells and cells treated overnight with GalNAcαBn or DMJ. Flow cytometry results shown include data from two experiments and error bars represent standard deviations; *** p < 0.001, ** p < 0.01, * p < 0.1.
    Figure Legend Snippet: Binding of lectins to MVs derived from EA.hy 926 cells treated with inhibitors to N -glycosylation, DMJ ( A ) or O -glycosylation, GalNAcαBn ( B ). MVs were isolated from native cells and cells treated overnight with GalNAcαBn or DMJ. Flow cytometry results shown include data from two experiments and error bars represent standard deviations; *** p < 0.001, ** p < 0.01, * p < 0.1.

    Techniques Used: Binding Assay, Derivative Assay, Isolation, Flow Cytometry

    Binding of lectins to MVs released from the EA.hy 926 cells treated with enzymes. MVs were isolated from cells treated with collagenase, hyaluronidase, and trypsin. Flow cytometry results include data from three experiments; error bars represent standard deviations; * p < 0.1.
    Figure Legend Snippet: Binding of lectins to MVs released from the EA.hy 926 cells treated with enzymes. MVs were isolated from cells treated with collagenase, hyaluronidase, and trypsin. Flow cytometry results include data from three experiments; error bars represent standard deviations; * p < 0.1.

    Techniques Used: Binding Assay, Isolation, Flow Cytometry

    biotinylated maackia amurensis lectin 1  (Vector Laboratories)


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    Vector Laboratories biotinylated maackia amurensis lectin 1
    Biotinylated Maackia Amurensis Lectin 1, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    biotinylated wisteria floribunda lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated wisteria floribunda lectin
    Biotinylated Wisteria Floribunda Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    biotinylated lectins  (Vector Laboratories)


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    Vector Laboratories biotinylated lectins
    A) Binding preference of multiple <t>lectins</t> and sites of glycosidase sensitivity: VVA binds to Tn-antigen; PNA binds T-antigen and is cleaved by O-glycosidase; ConA binds the core structure of N-glycans and is cleaved by PNGase F. B) VVA binding to endogenous Tn-antigen is absent in protein blots of wild type mouse cortex but generated in Synl and Gfap Cosme-eKO lines with distinct patterns, consistent with differential inhibition of O-GalNAc extension in these conditional knock-outs. C) Total levels of O-GalNAc glycans detected by PNA blotting after neuraminidase treatment showed no significant reduction in either cKO line, though the migration patterns of some protein bands differed compared to WT. D) ConA binding to N-glycans in cortex was unaffected in all mouse lines. Each lane contains cortical lysates from an individual mouse of the corresponding genotype. Experiment was replicated twice with similar results. E) Quantification of lectin binding from (B-D) normalized to total protein (TP) staining within the same lane of each blot. Data presented as the mean binding intensity +/- SEM, with data points for each individual mouse included. 15 µg protein lysate added per well.
    Biotinylated Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "O-GalNAc glycans enrich in white matter tracts and regulate nodes of Ranvier"

    Article Title: O-GalNAc glycans enrich in white matter tracts and regulate nodes of Ranvier

    Journal: bioRxiv

    doi: 10.1101/2024.05.09.593410

    A) Binding preference of multiple lectins and sites of glycosidase sensitivity: VVA binds to Tn-antigen; PNA binds T-antigen and is cleaved by O-glycosidase; ConA binds the core structure of N-glycans and is cleaved by PNGase F. B) VVA binding to endogenous Tn-antigen is absent in protein blots of wild type mouse cortex but generated in Synl and Gfap Cosme-eKO lines with distinct patterns, consistent with differential inhibition of O-GalNAc extension in these conditional knock-outs. C) Total levels of O-GalNAc glycans detected by PNA blotting after neuraminidase treatment showed no significant reduction in either cKO line, though the migration patterns of some protein bands differed compared to WT. D) ConA binding to N-glycans in cortex was unaffected in all mouse lines. Each lane contains cortical lysates from an individual mouse of the corresponding genotype. Experiment was replicated twice with similar results. E) Quantification of lectin binding from (B-D) normalized to total protein (TP) staining within the same lane of each blot. Data presented as the mean binding intensity +/- SEM, with data points for each individual mouse included. 15 µg protein lysate added per well.
    Figure Legend Snippet: A) Binding preference of multiple lectins and sites of glycosidase sensitivity: VVA binds to Tn-antigen; PNA binds T-antigen and is cleaved by O-glycosidase; ConA binds the core structure of N-glycans and is cleaved by PNGase F. B) VVA binding to endogenous Tn-antigen is absent in protein blots of wild type mouse cortex but generated in Synl and Gfap Cosme-eKO lines with distinct patterns, consistent with differential inhibition of O-GalNAc extension in these conditional knock-outs. C) Total levels of O-GalNAc glycans detected by PNA blotting after neuraminidase treatment showed no significant reduction in either cKO line, though the migration patterns of some protein bands differed compared to WT. D) ConA binding to N-glycans in cortex was unaffected in all mouse lines. Each lane contains cortical lysates from an individual mouse of the corresponding genotype. Experiment was replicated twice with similar results. E) Quantification of lectin binding from (B-D) normalized to total protein (TP) staining within the same lane of each blot. Data presented as the mean binding intensity +/- SEM, with data points for each individual mouse included. 15 µg protein lysate added per well.

    Techniques Used: Binding Assay, Generated, Inhibition, Migration, Staining

    biotinylated vva lectin  (Vector Laboratories)


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    Vector Laboratories biotinylated vva lectin
    Biotinylated Vva Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories biotinylated plant lectins mal
    Biotinylated Plant Lectins Mal, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories biotinylated galananthus novalis lectin
    A Binding of α-swH1N2 virus to a sialoside microarray containing glycans with α2-3 or α2-6 linked sialic acids representing avian-type and human-type influenza receptors, respectively. Bars represent the fluorescence intensity of bound α-swH1N2. Glycan structures corresponding to numbers are shown on the x-axis are found in Supplementary Table . Signal values are calculated from the mean intensities of 4 of 6 replicate spots with the highest and lowest signal omitted. B Replication of swine influenza virus in human bronchial epithelial (HBE) air-liquid interface cell cultures. HBE cell cultures were infected in triplicate with 10 3 TCID 50 (tissue culture infectious dose 50) per well of H1N1pdm09, γ-swH1N1, or α-swH1N2. The apical supernatant was collected at the indicated time points and virus titers were determined on MDCK cells using TCID 50 assays. A ratio of swine virus titer relative to H1N1pdm09 titer at 24 and 48 h of all HBE patient cell cultures is shown. Each dot represents an average of three technical replicates per HBE culture, and seven biological replicates from different HBE patient cultures are displayed. Data are presented as mean values +/− SD of the seven biological replicates each with three technical replicates. C Stability of α-swH1N2 influenza virus in small droplets over a range of relative humidity (RH) conditions. Ten 1 uL droplets of pooled virus from panel B were spotted into the wells of a tissue culture dish for 2 h. Decay of the virus at each RH was calculated compared to the titer of ten 1 uL droplets deposited and immediately recovered from a tissue culture dish. Log 10 decay of HBE-propagated H1N1pdm09 (black) and α-swH1N2 (green) is shown and represents mean values (±SD) from eight biological replicates performed in three technical replicates. D H1N1pdm09 (gray, N = 8) and α-swH1N2 (green, N = 4) viruses were incubated in PBS solutions of different pHs for 1 h at 37 °C. Virus titers were determined by TCID 50 assay and the EC 50 values were plotted using regression analysis of the dose-response curve. The reported mean corresponds to at least four independent biological replicates, each performed in three technical replicates. E The NA activities of H1N1pdm09 (gray) and α-swH1N2 (green) were determined using an enzyme-linked <t>lectin</t> assay with fetuin as the substrate. Viruses were normalized for equal infectivity and displayed data are the mean (±SD) of three independent biological replicates performed in technical duplicates.
    Biotinylated Galananthus Novalis Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories biotinylated mal ii lectin
    (A) Analysis of the correlation between key genes for sialic acid synthesis mRNA expression and CD274 (PD-L1) in tumors using the TIMER 2.0 tool. (B) Analysis of the fold change in key genes for sialic acid synthesis mRNA expression in the PD-L1 high group compared to the PD-L1 low group, compiled from TCGA data. (C) <t>Lectin</t> blot analysis of the sialic acid level in RAW264.7 cells after treated by PD-L1 nanobody (Nb16). (D) Quantitative PCR analysis of Cd274 mRNA expression in RAW264.7 cells after treated by sialidase (Sia).
    Biotinylated Mal Ii Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Vector Laboratories biotinylated lectin solution con a
    Detection and persistence of <t>lectin,</t> antibody, and DNA targets on keratinocyte cells on the panel of substrates. 5000 keratinocyte cells were seeded on 10 substrates. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of keratinocyte cells on substrates thanks to SEM. The second and third images showed keratinocyte cells visualized by confocal microscopy. For raw wood, no SEM images could be taken due to the fibrous nature of the substrate. Cells were incubated in the presence of <t>Con</t> <t>A</t> lectin (orange) that recognizes mannose carbohydrates, or labelled with antibody specifically directed against keratin 10 (Green). DNA from nuclei was stained with Hoechst 33342 (Blue). Images are representative data from three independent experiments. Scale bar: 10 µm.
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    Vector Laboratories biotinylated lectins
    <t> Lectins </t> used in this study, and the glycans to which they bind, according to CFG data. <t> Lectins </t> displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .
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    <t> Lectins </t> used in this study, and the glycans to which they bind, according to CFG data. <t> Lectins </t> displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .
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    <t> Lectins </t> used in this study, and the glycans to which they bind, according to CFG data. <t> Lectins </t> displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .
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    Vector Laboratories biotinylated vva lectin
    <t> Lectins </t> used in this study, and the glycans to which they bind, according to CFG data. <t> Lectins </t> displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .
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    Image Search Results


    A Binding of α-swH1N2 virus to a sialoside microarray containing glycans with α2-3 or α2-6 linked sialic acids representing avian-type and human-type influenza receptors, respectively. Bars represent the fluorescence intensity of bound α-swH1N2. Glycan structures corresponding to numbers are shown on the x-axis are found in Supplementary Table . Signal values are calculated from the mean intensities of 4 of 6 replicate spots with the highest and lowest signal omitted. B Replication of swine influenza virus in human bronchial epithelial (HBE) air-liquid interface cell cultures. HBE cell cultures were infected in triplicate with 10 3 TCID 50 (tissue culture infectious dose 50) per well of H1N1pdm09, γ-swH1N1, or α-swH1N2. The apical supernatant was collected at the indicated time points and virus titers were determined on MDCK cells using TCID 50 assays. A ratio of swine virus titer relative to H1N1pdm09 titer at 24 and 48 h of all HBE patient cell cultures is shown. Each dot represents an average of three technical replicates per HBE culture, and seven biological replicates from different HBE patient cultures are displayed. Data are presented as mean values +/− SD of the seven biological replicates each with three technical replicates. C Stability of α-swH1N2 influenza virus in small droplets over a range of relative humidity (RH) conditions. Ten 1 uL droplets of pooled virus from panel B were spotted into the wells of a tissue culture dish for 2 h. Decay of the virus at each RH was calculated compared to the titer of ten 1 uL droplets deposited and immediately recovered from a tissue culture dish. Log 10 decay of HBE-propagated H1N1pdm09 (black) and α-swH1N2 (green) is shown and represents mean values (±SD) from eight biological replicates performed in three technical replicates. D H1N1pdm09 (gray, N = 8) and α-swH1N2 (green, N = 4) viruses were incubated in PBS solutions of different pHs for 1 h at 37 °C. Virus titers were determined by TCID 50 assay and the EC 50 values were plotted using regression analysis of the dose-response curve. The reported mean corresponds to at least four independent biological replicates, each performed in three technical replicates. E The NA activities of H1N1pdm09 (gray) and α-swH1N2 (green) were determined using an enzyme-linked lectin assay with fetuin as the substrate. Viruses were normalized for equal infectivity and displayed data are the mean (±SD) of three independent biological replicates performed in technical duplicates.

    Journal: Nature Communications

    Article Title: Potential pandemic risk of circulating swine H1N2 influenza viruses

    doi: 10.1038/s41467-024-49117-z

    Figure Lengend Snippet: A Binding of α-swH1N2 virus to a sialoside microarray containing glycans with α2-3 or α2-6 linked sialic acids representing avian-type and human-type influenza receptors, respectively. Bars represent the fluorescence intensity of bound α-swH1N2. Glycan structures corresponding to numbers are shown on the x-axis are found in Supplementary Table . Signal values are calculated from the mean intensities of 4 of 6 replicate spots with the highest and lowest signal omitted. B Replication of swine influenza virus in human bronchial epithelial (HBE) air-liquid interface cell cultures. HBE cell cultures were infected in triplicate with 10 3 TCID 50 (tissue culture infectious dose 50) per well of H1N1pdm09, γ-swH1N1, or α-swH1N2. The apical supernatant was collected at the indicated time points and virus titers were determined on MDCK cells using TCID 50 assays. A ratio of swine virus titer relative to H1N1pdm09 titer at 24 and 48 h of all HBE patient cell cultures is shown. Each dot represents an average of three technical replicates per HBE culture, and seven biological replicates from different HBE patient cultures are displayed. Data are presented as mean values +/− SD of the seven biological replicates each with three technical replicates. C Stability of α-swH1N2 influenza virus in small droplets over a range of relative humidity (RH) conditions. Ten 1 uL droplets of pooled virus from panel B were spotted into the wells of a tissue culture dish for 2 h. Decay of the virus at each RH was calculated compared to the titer of ten 1 uL droplets deposited and immediately recovered from a tissue culture dish. Log 10 decay of HBE-propagated H1N1pdm09 (black) and α-swH1N2 (green) is shown and represents mean values (±SD) from eight biological replicates performed in three technical replicates. D H1N1pdm09 (gray, N = 8) and α-swH1N2 (green, N = 4) viruses were incubated in PBS solutions of different pHs for 1 h at 37 °C. Virus titers were determined by TCID 50 assay and the EC 50 values were plotted using regression analysis of the dose-response curve. The reported mean corresponds to at least four independent biological replicates, each performed in three technical replicates. E The NA activities of H1N1pdm09 (gray) and α-swH1N2 (green) were determined using an enzyme-linked lectin assay with fetuin as the substrate. Viruses were normalized for equal infectivity and displayed data are the mean (±SD) of three independent biological replicates performed in technical duplicates.

    Article Snippet: Slides were then washed with phosphate buffered saline (PBS) and water, followed by incubation with biotinylated Galananthus Novalis Lectin (GNL; Vector Labs) at 1ug/mL in 1X PBS for 1 h . Sides were washed with PBS and overlayed with 1 µg/ml Streptavidin-AlexaFluor488 (LifeTech) for 1 h and washed with PBS and water.

    Techniques: Binding Assay, Virus, Microarray, Fluorescence, Infection, Incubation

    (A) Analysis of the correlation between key genes for sialic acid synthesis mRNA expression and CD274 (PD-L1) in tumors using the TIMER 2.0 tool. (B) Analysis of the fold change in key genes for sialic acid synthesis mRNA expression in the PD-L1 high group compared to the PD-L1 low group, compiled from TCGA data. (C) Lectin blot analysis of the sialic acid level in RAW264.7 cells after treated by PD-L1 nanobody (Nb16). (D) Quantitative PCR analysis of Cd274 mRNA expression in RAW264.7 cells after treated by sialidase (Sia).

    Journal: bioRxiv

    Article Title: A nanobody-enzyme fusion protein targeting PD-L1 and sialic acid exerts anti-tumor effects by affecting tumor associated macrophages

    doi: 10.1101/2024.06.05.597674

    Figure Lengend Snippet: (A) Analysis of the correlation between key genes for sialic acid synthesis mRNA expression and CD274 (PD-L1) in tumors using the TIMER 2.0 tool. (B) Analysis of the fold change in key genes for sialic acid synthesis mRNA expression in the PD-L1 high group compared to the PD-L1 low group, compiled from TCGA data. (C) Lectin blot analysis of the sialic acid level in RAW264.7 cells after treated by PD-L1 nanobody (Nb16). (D) Quantitative PCR analysis of Cd274 mRNA expression in RAW264.7 cells after treated by sialidase (Sia).

    Article Snippet: Different from the Western blot, biotinylated MAL-II lectin (10 μg/mL, B-1265-1; Vectorlab) was used for the primary antibody and Streptavidin-HRP (dilution 1:2000, A0303; Beyotime) for the secondary antibody.

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    (A) KEGG analysis of the differential genes between Sia-treated group and negative control. (B) GSEA enrichment analysis of C-type lectin pathway. (C) Heatmap of the differential genes in C-type lectin pathway. (D) Representative image of western blot in detecting SYK, JNK and NOS2 expression at protein level. The quantitative results are analyzed by gray value and shown (E). Table1 Pharmacokinetic parameters of Nb16-Sia after intraperitoneal injection of a single dose of Nb16-Sia (5 mg/kg) in mice.

    Journal: bioRxiv

    Article Title: A nanobody-enzyme fusion protein targeting PD-L1 and sialic acid exerts anti-tumor effects by affecting tumor associated macrophages

    doi: 10.1101/2024.06.05.597674

    Figure Lengend Snippet: (A) KEGG analysis of the differential genes between Sia-treated group and negative control. (B) GSEA enrichment analysis of C-type lectin pathway. (C) Heatmap of the differential genes in C-type lectin pathway. (D) Representative image of western blot in detecting SYK, JNK and NOS2 expression at protein level. The quantitative results are analyzed by gray value and shown (E). Table1 Pharmacokinetic parameters of Nb16-Sia after intraperitoneal injection of a single dose of Nb16-Sia (5 mg/kg) in mice.

    Article Snippet: Different from the Western blot, biotinylated MAL-II lectin (10 μg/mL, B-1265-1; Vectorlab) was used for the primary antibody and Streptavidin-HRP (dilution 1:2000, A0303; Beyotime) for the secondary antibody.

    Techniques: Negative Control, Western Blot, Expressing, Injection

    Detection and persistence of lectin, antibody, and DNA targets on keratinocyte cells on the panel of substrates. 5000 keratinocyte cells were seeded on 10 substrates. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of keratinocyte cells on substrates thanks to SEM. The second and third images showed keratinocyte cells visualized by confocal microscopy. For raw wood, no SEM images could be taken due to the fibrous nature of the substrate. Cells were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates, or labelled with antibody specifically directed against keratin 10 (Green). DNA from nuclei was stained with Hoechst 33342 (Blue). Images are representative data from three independent experiments. Scale bar: 10 µm.

    Journal: Scientific Reports

    Article Title: Detection of invisible biological traces in relation to the physicochemical properties of substrates surfaces in forensic casework

    doi: 10.1038/s41598-024-63911-1

    Figure Lengend Snippet: Detection and persistence of lectin, antibody, and DNA targets on keratinocyte cells on the panel of substrates. 5000 keratinocyte cells were seeded on 10 substrates. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of keratinocyte cells on substrates thanks to SEM. The second and third images showed keratinocyte cells visualized by confocal microscopy. For raw wood, no SEM images could be taken due to the fibrous nature of the substrate. Cells were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates, or labelled with antibody specifically directed against keratin 10 (Green). DNA from nuclei was stained with Hoechst 33342 (Blue). Images are representative data from three independent experiments. Scale bar: 10 µm.

    Article Snippet: At each time point (T0, 1, and 2 months), non-specific sites of keratinocyte cells and fingermarks were blocked 30 min with PBS-BSA 0.5% at room temperature and incubated for 2 h with primary antibody Keratin 10 (SAB4501656, (Sigma-Aldrich, USA), 1:50 in PBS-BSA 0.5%), or incubated for 20 min in a humidity chamber using a biotinylated lectin solution Con A (B-1005 (Vector laboratories, USA), at final concentration 10 µg/ml).

    Techniques: Adhesive, Confocal Microscopy, Incubation, Staining

    Detection and persistence of lectin, antibody, and DNA targets on fingermarks on the panel of substrates. Fingermarks were deposited on 10 substrates for 10 s. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of fingermarks on substrates thanks to SEM. The second and third images showed fingermarks visualized by confocal microscopy. Fingermarks were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates or labelled with antibody specifically directed against keratin 10 (K10, green). DNA was stained with Hoechst 33342 (blue). Images are representative data from three independent experiments. Scale bar: 10 µm.

    Journal: Scientific Reports

    Article Title: Detection of invisible biological traces in relation to the physicochemical properties of substrates surfaces in forensic casework

    doi: 10.1038/s41598-024-63911-1

    Figure Lengend Snippet: Detection and persistence of lectin, antibody, and DNA targets on fingermarks on the panel of substrates. Fingermarks were deposited on 10 substrates for 10 s. These 10 substrates were divided into 3 groups according to the principal component analysis of their physicochemical characteristics: group 1 (PVC flooring, raw wood), group 2 (glass, C1, C2), group 3 (polystyrene, sticky adhesive tape, non-sticky adhesive tape, metal, varnished wood). Substrates were placed indoors or outdoors for 2 months. The first line was the visualization of fingermarks on substrates thanks to SEM. The second and third images showed fingermarks visualized by confocal microscopy. Fingermarks were incubated in the presence of Con A lectin (orange) that recognizes mannose carbohydrates or labelled with antibody specifically directed against keratin 10 (K10, green). DNA was stained with Hoechst 33342 (blue). Images are representative data from three independent experiments. Scale bar: 10 µm.

    Article Snippet: At each time point (T0, 1, and 2 months), non-specific sites of keratinocyte cells and fingermarks were blocked 30 min with PBS-BSA 0.5% at room temperature and incubated for 2 h with primary antibody Keratin 10 (SAB4501656, (Sigma-Aldrich, USA), 1:50 in PBS-BSA 0.5%), or incubated for 20 min in a humidity chamber using a biotinylated lectin solution Con A (B-1005 (Vector laboratories, USA), at final concentration 10 µg/ml).

    Techniques: Adhesive, Confocal Microscopy, Incubation, Staining

     Lectins  used in this study, and the glycans to which they bind, according to CFG data.  Lectins  displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .

    Journal: International Journal of Molecular Sciences

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    doi: 10.3390/ijms25115725

    Figure Lengend Snippet: Lectins used in this study, and the glycans to which they bind, according to CFG data. Lectins displayed binding to MVs are marked in grey. The three lectins marked with * displayed binding non-specifically to the glass slides, and those lectins along with the lectin marked # were only analyzed using flow cytometry. The structure of glycans was presented in the symbol nomenclature for glycans (SNFGs) format ( https://www.ncbi.nlm.nih.gov/glycans/snfg.html accessed on 26 February 2024) using Carbohydrate Structure Databases, 16 March 2024 found at http://csdb.glycoscience.ru/database/core/wizard.html .

    Article Snippet: The biotinylated lectins listed in were obtained from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Binding Assay, Flow Cytometry

    Solid-phase detection of lectin binding to MVs. MVs were derived from EA.hy 926 cells and immobilized on glass slides (solid-phase assay), incubated with biotinylated lectins, and then visualized with Str-Alexa Fluor 555, as described in the Materials and Methods section.

    Journal: International Journal of Molecular Sciences

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    doi: 10.3390/ijms25115725

    Figure Lengend Snippet: Solid-phase detection of lectin binding to MVs. MVs were derived from EA.hy 926 cells and immobilized on glass slides (solid-phase assay), incubated with biotinylated lectins, and then visualized with Str-Alexa Fluor 555, as described in the Materials and Methods section.

    Article Snippet: The biotinylated lectins listed in were obtained from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Binding Assay, Derivative Assay, Incubation

    Flow cytometry detection of lectins DSA and SNA binding to glycosidase-treated MVs. MVs were incubated with either β-galactosidase or neuraminidase, washed and incubated with biotinylated lectins, as described in the Materials and Methods section. In the dot plots, forward scatter (FS) was plotted against the logarithm of fluorescence (FL1) and the number given in the rectangles (for the purple dots) indicate the percentage of lectin bound to MVs.

    Journal: International Journal of Molecular Sciences

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    doi: 10.3390/ijms25115725

    Figure Lengend Snippet: Flow cytometry detection of lectins DSA and SNA binding to glycosidase-treated MVs. MVs were incubated with either β-galactosidase or neuraminidase, washed and incubated with biotinylated lectins, as described in the Materials and Methods section. In the dot plots, forward scatter (FS) was plotted against the logarithm of fluorescence (FL1) and the number given in the rectangles (for the purple dots) indicate the percentage of lectin bound to MVs.

    Article Snippet: The biotinylated lectins listed in were obtained from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Flow Cytometry, Binding Assay, Incubation, Fluorescence

    Flow cytometry binding of lectins to EA.hy 926 cells. Cells were incubated with biotinylated lectins followed by Str-FITC, as described in the Materials and Methods Section. Results shown include data from four experiments and error bars represent standard deviations. A mean fluorescence <50 was considered as negative.

    Journal: International Journal of Molecular Sciences

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    doi: 10.3390/ijms25115725

    Figure Lengend Snippet: Flow cytometry binding of lectins to EA.hy 926 cells. Cells were incubated with biotinylated lectins followed by Str-FITC, as described in the Materials and Methods Section. Results shown include data from four experiments and error bars represent standard deviations. A mean fluorescence <50 was considered as negative.

    Article Snippet: The biotinylated lectins listed in were obtained from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Flow Cytometry, Binding Assay, Incubation, Fluorescence

    Binding of lectins to MVs derived from EA.hy 926 cells treated with inhibitors to N -glycosylation, DMJ ( A ) or O -glycosylation, GalNAcαBn ( B ). MVs were isolated from native cells and cells treated overnight with GalNAcαBn or DMJ. Flow cytometry results shown include data from two experiments and error bars represent standard deviations; *** p < 0.001, ** p < 0.01, * p < 0.1.

    Journal: International Journal of Molecular Sciences

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    doi: 10.3390/ijms25115725

    Figure Lengend Snippet: Binding of lectins to MVs derived from EA.hy 926 cells treated with inhibitors to N -glycosylation, DMJ ( A ) or O -glycosylation, GalNAcαBn ( B ). MVs were isolated from native cells and cells treated overnight with GalNAcαBn or DMJ. Flow cytometry results shown include data from two experiments and error bars represent standard deviations; *** p < 0.001, ** p < 0.01, * p < 0.1.

    Article Snippet: The biotinylated lectins listed in were obtained from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Binding Assay, Derivative Assay, Isolation, Flow Cytometry

    Binding of lectins to MVs released from the EA.hy 926 cells treated with enzymes. MVs were isolated from cells treated with collagenase, hyaluronidase, and trypsin. Flow cytometry results include data from three experiments; error bars represent standard deviations; * p < 0.1.

    Journal: International Journal of Molecular Sciences

    Article Title: Surface Glycans of Microvesicles Derived from Endothelial Cells, as Probed Using Plant Lectins

    doi: 10.3390/ijms25115725

    Figure Lengend Snippet: Binding of lectins to MVs released from the EA.hy 926 cells treated with enzymes. MVs were isolated from cells treated with collagenase, hyaluronidase, and trypsin. Flow cytometry results include data from three experiments; error bars represent standard deviations; * p < 0.1.

    Article Snippet: The biotinylated lectins listed in were obtained from Vector Laboratories (Burlingame, CA, USA).

    Techniques: Binding Assay, Isolation, Flow Cytometry