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cona lectin  (Vector Laboratories)


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    Vector Laboratories cona lectin
    a , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in vivo. WT mice under a regular 12 h light–dark cycle and NR feeding were subcutaneously injected with either vehicle (Veh) or CP-91149 at ZT0 for tissue collections at ZT3, ZT6, ZT9, ZT12 and ZT24. b , Average food consumption of WT mice ( n = 4 biological replicates) 24 h after CP-91149 injection. c , Temporal profiles of glycogen in the liver of Veh-injected and CP-91149-injected mice ( n = 20 (5 timepoints × 4 biological replicates)). d , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated mouse liver were determined by <t>lectin</t> blot analysis with concanavalin A <t>(ConA,</t> n = 20 (5 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (right). e , C3 levels in mouse serum as assessed by ELISA ( n = 20 (5 timepoints × 4 biological replicates)). f , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in AML12 mouse hepatocytes. Treatment with Veh or CP-91149 (67 µM) was performed for 3, 6, 12 and 24 h. g , h , Kinetic profiles of UDP-glucose + UDP-galactose levels ( g ), cytidine 5′-monophospho-N-acetyl neuraminic acid (CMP-Neu5Ac) ( h , left) and uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) ( h , right) in AML12 cells upon CP-91149 treatment ( n = 16 (4 timepoints × 4 biological replicates)). i , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated AML12 cells were determined by lectin blot analysis with ConA ( n = 16 (4 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (bottom). j , ALB, FN1 and C3 levels in cell medium determined by ELISA ( n = 22–24 (4 timepoints × 6 biological replicates, with ALB 14 h Veh and 24 h CP-91149 n = 5)). k , Experimental design (created with BioRender.com ). AML12 cells were treated with Veh or CP-91149 for 14 h in the absence or presence of supplemental UDP-glucose (UDPG; 2 mM). l , m , ALB and C3 levels in cell medium ( l ) and lysates ( m ) as determined by ELISA ( n = 6 biological replicates, except for ALB under CP-91149 treatment ( n = 5)). Data are displayed as means; error bars, s.e.m. Boxplots show the median (centre line), interquartile range (box) and minimum to maximum values (whiskers). A detailed description of the statistical analysis is available in Source Data Fig. . See also Extended Data Fig. .
    Cona Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 302 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cona+lectin/Biotinylated+Concanavalin+A+(Con+A)/pmc12945689-402-34-36
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    94/100 stars

    Images

    1) Product Images from "Feeding-regulated glycogen metabolism drives rhythmic liver protein secretion"

    Article Title: Feeding-regulated glycogen metabolism drives rhythmic liver protein secretion

    Journal: Nature Metabolism

    doi: 10.1038/s42255-026-01453-8

    a , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in vivo. WT mice under a regular 12 h light–dark cycle and NR feeding were subcutaneously injected with either vehicle (Veh) or CP-91149 at ZT0 for tissue collections at ZT3, ZT6, ZT9, ZT12 and ZT24. b , Average food consumption of WT mice ( n = 4 biological replicates) 24 h after CP-91149 injection. c , Temporal profiles of glycogen in the liver of Veh-injected and CP-91149-injected mice ( n = 20 (5 timepoints × 4 biological replicates)). d , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated mouse liver were determined by lectin blot analysis with concanavalin A (ConA, n = 20 (5 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (right). e , C3 levels in mouse serum as assessed by ELISA ( n = 20 (5 timepoints × 4 biological replicates)). f , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in AML12 mouse hepatocytes. Treatment with Veh or CP-91149 (67 µM) was performed for 3, 6, 12 and 24 h. g , h , Kinetic profiles of UDP-glucose + UDP-galactose levels ( g ), cytidine 5′-monophospho-N-acetyl neuraminic acid (CMP-Neu5Ac) ( h , left) and uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) ( h , right) in AML12 cells upon CP-91149 treatment ( n = 16 (4 timepoints × 4 biological replicates)). i , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated AML12 cells were determined by lectin blot analysis with ConA ( n = 16 (4 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (bottom). j , ALB, FN1 and C3 levels in cell medium determined by ELISA ( n = 22–24 (4 timepoints × 6 biological replicates, with ALB 14 h Veh and 24 h CP-91149 n = 5)). k , Experimental design (created with BioRender.com ). AML12 cells were treated with Veh or CP-91149 for 14 h in the absence or presence of supplemental UDP-glucose (UDPG; 2 mM). l , m , ALB and C3 levels in cell medium ( l ) and lysates ( m ) as determined by ELISA ( n = 6 biological replicates, except for ALB under CP-91149 treatment ( n = 5)). Data are displayed as means; error bars, s.e.m. Boxplots show the median (centre line), interquartile range (box) and minimum to maximum values (whiskers). A detailed description of the statistical analysis is available in Source Data Fig. . See also Extended Data Fig. .
    Figure Legend Snippet: a , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in vivo. WT mice under a regular 12 h light–dark cycle and NR feeding were subcutaneously injected with either vehicle (Veh) or CP-91149 at ZT0 for tissue collections at ZT3, ZT6, ZT9, ZT12 and ZT24. b , Average food consumption of WT mice ( n = 4 biological replicates) 24 h after CP-91149 injection. c , Temporal profiles of glycogen in the liver of Veh-injected and CP-91149-injected mice ( n = 20 (5 timepoints × 4 biological replicates)). d , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated mouse liver were determined by lectin blot analysis with concanavalin A (ConA, n = 20 (5 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (right). e , C3 levels in mouse serum as assessed by ELISA ( n = 20 (5 timepoints × 4 biological replicates)). f , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in AML12 mouse hepatocytes. Treatment with Veh or CP-91149 (67 µM) was performed for 3, 6, 12 and 24 h. g , h , Kinetic profiles of UDP-glucose + UDP-galactose levels ( g ), cytidine 5′-monophospho-N-acetyl neuraminic acid (CMP-Neu5Ac) ( h , left) and uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) ( h , right) in AML12 cells upon CP-91149 treatment ( n = 16 (4 timepoints × 4 biological replicates)). i , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated AML12 cells were determined by lectin blot analysis with ConA ( n = 16 (4 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (bottom). j , ALB, FN1 and C3 levels in cell medium determined by ELISA ( n = 22–24 (4 timepoints × 6 biological replicates, with ALB 14 h Veh and 24 h CP-91149 n = 5)). k , Experimental design (created with BioRender.com ). AML12 cells were treated with Veh or CP-91149 for 14 h in the absence or presence of supplemental UDP-glucose (UDPG; 2 mM). l , m , ALB and C3 levels in cell medium ( l ) and lysates ( m ) as determined by ELISA ( n = 6 biological replicates, except for ALB under CP-91149 treatment ( n = 5)). Data are displayed as means; error bars, s.e.m. Boxplots show the median (centre line), interquartile range (box) and minimum to maximum values (whiskers). A detailed description of the statistical analysis is available in Source Data Fig. . See also Extended Data Fig. .

    Techniques Used: Inhibition, In Vivo, Injection, Glycoproteomics, Staining, Control, Enzyme-linked Immunosorbent Assay

    Related Articles

    other:

    Article Title: Evaluation of Caenorhabditis elegans glycoproteins as protective immunogens against Haemonchus contortus challenge in sheep.
    Article Snippet: High levels of protection can be attained against Haemonchus contortus challenge infection in sheep using native antigens isolated from the gut of the adult parasite.. However, vaccination with recombinant forms of these antigens, or components thereof, has disappointingly failed to generate similar levels of protection, suggesting that appropriate nematode glycosylation may be a prerequisite for protection.. The free-living nematode, Caenorhabditis elegans is closely related to H. contortus and has been shown to share similar glycan moieties.

    Nucleic Acid Electrophoresis:

    Article Title: N -acetylneuraminate pyruvate lyase controls sialylation of muscle glycoproteins essential for muscle regeneration and function
    Article Snippet: To test specificity of SNL blotting, protein lysates were treated with exogenous sialidase from Arthrobacter ureafaciens (Sigma-Aldrich, 10269611001) according to the manufacturer’s protocol. .. After separation by SDS–polyacrylamide gel electrophoresis on an 8% gel, the proteins were transferred to a nitrocellulose membrane and hybridized with polyclonal rabbit anti-NPL antibodies (1:2000, Abcam, catalog no. ab223521), mouse anti–α-DG antibody clone IIH6C4 (1:2000, Millipore Sigma), monoclonal mouse anti–β-actin antibody (1:1000, Santa Cruz Biotechnology, catalog no. SC-47778), polyclonal rabbit anti-LRPPRC antibody (1:2000, Thermo Fisher Scientific, catalog no. 21175-1-AP), biotinylated S. nigra lectin (1:5000, Vector Laboratories, catalog no. B-1305-2), PNA lectin (1:1000, Vector Laboratories, catalog no. B-1075-5), or ConA lectin (1:5000, Vector Laboratories, catalog no. B-1005-5) followed by horseradish peroxidase (HRP)–conjugated anti-mouse immunoglobulin G (IgG) and anti-rabbit IgG secondary antibodies (Cell Signaling Technology, 1:8000 and 1:10,000, respectively) or streptavidin-HRP (1:10,000, GE Healthcare). .. The membrane was developed with Pierce ECL Western blotting substrate (Thermo Fisher Scientific), and the signal was detected using the G:Box Chemi XQR system (Syngene).

    Article Title: N -acetylneuraminate pyruvate lyase controls sialylation of muscle glycoproteins essential for muscle regeneration and function.
    Article Snippet: To test specificity of SNL blotting, protein lysates were treated with exogenous sialidase from Arthrobacter ureafaciens (Sigma-Aldrich, 10269611001) according to the manufacturer’s protocol. .. After separation by SDS–polyacrylamide gel electrophoresis on an 8% gel, the proteins were transferred to a nitrocellulose membrane and hybridized with polyclonal rabbit anti-NPL antibodies (1:2000, Abcam, catalog no. ab223521), mouse anti–α-DG antibody clone IIH6C4 (1:2000, Millipore Sigma), monoclonal mouse anti– β-actin antibody (1:1000, Santa Cruz Biotechnology, catalog no. SC47778), polyclonal rabbit anti-LRPPRC antibody (1:2000, Thermo Fisher Scientific, catalog no. 21175-1-AP), biotinylated S. nigra lectin (1:5000, Vector Laboratories, catalog no. B-1305-2), PNA lectin (1:1000, Vector Laboratories, catalog no. B-1075-5), or ConA lectin (1:5000, Vector Laboratories, catalog no. B-1005-5) followed by horseradish peroxidase (HRP)–conjugated anti-mouse immunoglobulin G (IgG) and anti-rabbit IgG secondary antibodies (Cell Signaling Technology, 1:8000 and 1:10,000, respectively) or streptavidin-HRP (1:10,000, GE Healthcare). .. The membrane was developed with Pierce ECL Western blotting substrate (Thermo Fisher Scientific), and the signal was detected using the G:Box Chemi XQR system (Syngene).

    Membrane:

    Article Title: N -acetylneuraminate pyruvate lyase controls sialylation of muscle glycoproteins essential for muscle regeneration and function
    Article Snippet: To test specificity of SNL blotting, protein lysates were treated with exogenous sialidase from Arthrobacter ureafaciens (Sigma-Aldrich, 10269611001) according to the manufacturer’s protocol. .. After separation by SDS–polyacrylamide gel electrophoresis on an 8% gel, the proteins were transferred to a nitrocellulose membrane and hybridized with polyclonal rabbit anti-NPL antibodies (1:2000, Abcam, catalog no. ab223521), mouse anti–α-DG antibody clone IIH6C4 (1:2000, Millipore Sigma), monoclonal mouse anti–β-actin antibody (1:1000, Santa Cruz Biotechnology, catalog no. SC-47778), polyclonal rabbit anti-LRPPRC antibody (1:2000, Thermo Fisher Scientific, catalog no. 21175-1-AP), biotinylated S. nigra lectin (1:5000, Vector Laboratories, catalog no. B-1305-2), PNA lectin (1:1000, Vector Laboratories, catalog no. B-1075-5), or ConA lectin (1:5000, Vector Laboratories, catalog no. B-1005-5) followed by horseradish peroxidase (HRP)–conjugated anti-mouse immunoglobulin G (IgG) and anti-rabbit IgG secondary antibodies (Cell Signaling Technology, 1:8000 and 1:10,000, respectively) or streptavidin-HRP (1:10,000, GE Healthcare). .. The membrane was developed with Pierce ECL Western blotting substrate (Thermo Fisher Scientific), and the signal was detected using the G:Box Chemi XQR system (Syngene).

    Article Title: N -acetylneuraminate pyruvate lyase controls sialylation of muscle glycoproteins essential for muscle regeneration and function.
    Article Snippet: To test specificity of SNL blotting, protein lysates were treated with exogenous sialidase from Arthrobacter ureafaciens (Sigma-Aldrich, 10269611001) according to the manufacturer’s protocol. .. After separation by SDS–polyacrylamide gel electrophoresis on an 8% gel, the proteins were transferred to a nitrocellulose membrane and hybridized with polyclonal rabbit anti-NPL antibodies (1:2000, Abcam, catalog no. ab223521), mouse anti–α-DG antibody clone IIH6C4 (1:2000, Millipore Sigma), monoclonal mouse anti– β-actin antibody (1:1000, Santa Cruz Biotechnology, catalog no. SC47778), polyclonal rabbit anti-LRPPRC antibody (1:2000, Thermo Fisher Scientific, catalog no. 21175-1-AP), biotinylated S. nigra lectin (1:5000, Vector Laboratories, catalog no. B-1305-2), PNA lectin (1:1000, Vector Laboratories, catalog no. B-1075-5), or ConA lectin (1:5000, Vector Laboratories, catalog no. B-1005-5) followed by horseradish peroxidase (HRP)–conjugated anti-mouse immunoglobulin G (IgG) and anti-rabbit IgG secondary antibodies (Cell Signaling Technology, 1:8000 and 1:10,000, respectively) or streptavidin-HRP (1:10,000, GE Healthcare). .. The membrane was developed with Pierce ECL Western blotting substrate (Thermo Fisher Scientific), and the signal was detected using the G:Box Chemi XQR system (Syngene).



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    Vector Laboratories biotinylated plant lectin cona
    EVs glycoprotein enrichment and proteomic analysis. (A) Workflow for proteome identification of EV total proteins and glycoproteins. (B) Principal component analysis of 95C and 95D EVs total proteins (T‐p) and glycoproteins (G‐p). (C) Venn diagram of EVs total proteins and glycoproteins. (D) Pearson correlation coefficient matrix plot of multiple groups. The correlation coefficient was represented by a color scheme from white (negative correlation) to blue (positive correlation). (E) The volcano plot represents the quantitative analysis of N‐glycoproteins in 95D EVs versus 95C EVs. Orange represents proteins that were at least 2‐fold upregulated ( p < 0.05); blue represents proteins that were at least 2‐fold downregulated ( p < 0.05). (F) Distribution plot of the number of N‐glycosylation sites of 95C and 95D EVs. (G‐I) Comparison of the ranking, relative quantity, and unique peptides of three typical glycoproteins before and after <t>ConA</t> enrichment. GO analysis (J) and KEGG pathway enrichment (K) of differentially expressed glycoproteins in EVs. BP, biological process; CC, cellular component; MF, molecular function.
    Biotinylated Plant Lectin Cona, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cona+lectin/Biotinylated+Concanavalin+A+(Con+A)/pm40498437-183-0-4
    Average 94 stars, based on 1 article reviews
    biotinylated plant lectin cona - by Bioz Stars, 2026-09
    94/100 stars
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    biotinylated lectins concanavalin cona  (Vector Laboratories)
    94
    Vector Laboratories biotinylated lectins concanavalin cona
    Lectin detection profiles. A total of 12 plasmon shift values, measured after 15 min of immobilization, were recorded for each lectin, with the average and standard deviation values represented by each band in the graph. Each lectin is used to create the LPS profiles for each bacterial species injected at 100 μg/mL, as well as a PBS buffer blank reference. The <t>lectins</t> chosen are <t>Concanavalin</t> <t>(ConA),</t> Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA). These lectins will be referred by their abbreviation for the next figures to avoid unnecessary length in the legend.
    Biotinylated Lectins Concanavalin Cona, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cona+lectin/Biotinylated+Concanavalin+A+(Con+A)/pmc12019741-37-0-33
    Average 94 stars, based on 1 article reviews
    biotinylated lectins concanavalin cona - by Bioz Stars, 2026-09
    94/100 stars
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    beads coupled to the lectin concanavalin a (cona, canavalia ensiformis , cat. no. 234568)  (Millipore)
    90
    Millipore beads coupled to the lectin concanavalin a (cona, canavalia ensiformis , cat. no. 234568)
    Lectin detection profiles. A total of 12 plasmon shift values, measured after 15 min of immobilization, were recorded for each lectin, with the average and standard deviation values represented by each band in the graph. Each lectin is used to create the LPS profiles for each bacterial species injected at 100 μg/mL, as well as a PBS buffer blank reference. The <t>lectins</t> chosen are <t>Concanavalin</t> <t>(ConA),</t> Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA). These lectins will be referred by their abbreviation for the next figures to avoid unnecessary length in the legend.
    Beads Coupled To The Lectin Concanavalin A (Cona, Canavalia Ensiformis , Cat. No. 234568), supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/cona+lectin/concanavalin++con/pmc11817834-104-11-21
    Average 90 stars, based on 1 article reviews
    beads coupled to the lectin concanavalin a (cona, canavalia ensiformis , cat. no. 234568) - by Bioz Stars, 2026-09
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    Image Search Results


    a , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in vivo. WT mice under a regular 12 h light–dark cycle and NR feeding were subcutaneously injected with either vehicle (Veh) or CP-91149 at ZT0 for tissue collections at ZT3, ZT6, ZT9, ZT12 and ZT24. b , Average food consumption of WT mice ( n = 4 biological replicates) 24 h after CP-91149 injection. c , Temporal profiles of glycogen in the liver of Veh-injected and CP-91149-injected mice ( n = 20 (5 timepoints × 4 biological replicates)). d , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated mouse liver were determined by lectin blot analysis with concanavalin A (ConA, n = 20 (5 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (right). e , C3 levels in mouse serum as assessed by ELISA ( n = 20 (5 timepoints × 4 biological replicates)). f , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in AML12 mouse hepatocytes. Treatment with Veh or CP-91149 (67 µM) was performed for 3, 6, 12 and 24 h. g , h , Kinetic profiles of UDP-glucose + UDP-galactose levels ( g ), cytidine 5′-monophospho-N-acetyl neuraminic acid (CMP-Neu5Ac) ( h , left) and uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) ( h , right) in AML12 cells upon CP-91149 treatment ( n = 16 (4 timepoints × 4 biological replicates)). i , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated AML12 cells were determined by lectin blot analysis with ConA ( n = 16 (4 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (bottom). j , ALB, FN1 and C3 levels in cell medium determined by ELISA ( n = 22–24 (4 timepoints × 6 biological replicates, with ALB 14 h Veh and 24 h CP-91149 n = 5)). k , Experimental design (created with BioRender.com ). AML12 cells were treated with Veh or CP-91149 for 14 h in the absence or presence of supplemental UDP-glucose (UDPG; 2 mM). l , m , ALB and C3 levels in cell medium ( l ) and lysates ( m ) as determined by ELISA ( n = 6 biological replicates, except for ALB under CP-91149 treatment ( n = 5)). Data are displayed as means; error bars, s.e.m. Boxplots show the median (centre line), interquartile range (box) and minimum to maximum values (whiskers). A detailed description of the statistical analysis is available in Source Data Fig. . See also Extended Data Fig. .

    Journal: Nature Metabolism

    Article Title: Feeding-regulated glycogen metabolism drives rhythmic liver protein secretion

    doi: 10.1038/s42255-026-01453-8

    Figure Lengend Snippet: a , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in vivo. WT mice under a regular 12 h light–dark cycle and NR feeding were subcutaneously injected with either vehicle (Veh) or CP-91149 at ZT0 for tissue collections at ZT3, ZT6, ZT9, ZT12 and ZT24. b , Average food consumption of WT mice ( n = 4 biological replicates) 24 h after CP-91149 injection. c , Temporal profiles of glycogen in the liver of Veh-injected and CP-91149-injected mice ( n = 20 (5 timepoints × 4 biological replicates)). d , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated mouse liver were determined by lectin blot analysis with concanavalin A (ConA, n = 20 (5 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (right). e , C3 levels in mouse serum as assessed by ELISA ( n = 20 (5 timepoints × 4 biological replicates)). f , Experimental design (created with BioRender.com ). Inhibition of PYGL-mediated glycogenolysis by CP-91149 in AML12 mouse hepatocytes. Treatment with Veh or CP-91149 (67 µM) was performed for 3, 6, 12 and 24 h. g , h , Kinetic profiles of UDP-glucose + UDP-galactose levels ( g ), cytidine 5′-monophospho-N-acetyl neuraminic acid (CMP-Neu5Ac) ( h , left) and uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) ( h , right) in AML12 cells upon CP-91149 treatment ( n = 16 (4 timepoints × 4 biological replicates)). i , Glycosylation levels of proteins in CP-91149-treated and vehicle-treated AML12 cells were determined by lectin blot analysis with ConA ( n = 16 (4 timepoints × 4 biological replicates)). Amido black staining of the membranes was used as a loading control and serves as a reference for normalization of the quantified values (bottom). j , ALB, FN1 and C3 levels in cell medium determined by ELISA ( n = 22–24 (4 timepoints × 6 biological replicates, with ALB 14 h Veh and 24 h CP-91149 n = 5)). k , Experimental design (created with BioRender.com ). AML12 cells were treated with Veh or CP-91149 for 14 h in the absence or presence of supplemental UDP-glucose (UDPG; 2 mM). l , m , ALB and C3 levels in cell medium ( l ) and lysates ( m ) as determined by ELISA ( n = 6 biological replicates, except for ALB under CP-91149 treatment ( n = 5)). Data are displayed as means; error bars, s.e.m. Boxplots show the median (centre line), interquartile range (box) and minimum to maximum values (whiskers). A detailed description of the statistical analysis is available in Source Data Fig. . See also Extended Data Fig. .

    Article Snippet: Primary antibodies were used at the following dilutions: 1:1,000 for ATF4 (Cell Signaling Technologies, 11815), ARFGAP1 (Cell Signaling Technologies, 14608), Phospho-RPS6 (Cell Signaling Technologies, 2211), Total-RPS6 (Cell Signaling Technologies, 2217), GABARAPL1 (Genetex, GTX132664) and ConA Lectin (Vector Laboratories, B-1005) and 1:2,000 for STX4 (ProteinTech, 14988-1-AP).

    Techniques: Inhibition, In Vivo, Injection, Glycoproteomics, Staining, Control, Enzyme-linked Immunosorbent Assay

    EVs glycoprotein enrichment and proteomic analysis. (A) Workflow for proteome identification of EV total proteins and glycoproteins. (B) Principal component analysis of 95C and 95D EVs total proteins (T‐p) and glycoproteins (G‐p). (C) Venn diagram of EVs total proteins and glycoproteins. (D) Pearson correlation coefficient matrix plot of multiple groups. The correlation coefficient was represented by a color scheme from white (negative correlation) to blue (positive correlation). (E) The volcano plot represents the quantitative analysis of N‐glycoproteins in 95D EVs versus 95C EVs. Orange represents proteins that were at least 2‐fold upregulated ( p < 0.05); blue represents proteins that were at least 2‐fold downregulated ( p < 0.05). (F) Distribution plot of the number of N‐glycosylation sites of 95C and 95D EVs. (G‐I) Comparison of the ranking, relative quantity, and unique peptides of three typical glycoproteins before and after ConA enrichment. GO analysis (J) and KEGG pathway enrichment (K) of differentially expressed glycoproteins in EVs. BP, biological process; CC, cellular component; MF, molecular function.

    Journal: Journal of Extracellular Vesicles

    Article Title: Proteomic Analysis of Extracellular Vesicles Identifies CDCP1 as Critical Metastasis‐Related Glycoprotein in Lung Cancer

    doi: 10.1002/jev2.70128

    Figure Lengend Snippet: EVs glycoprotein enrichment and proteomic analysis. (A) Workflow for proteome identification of EV total proteins and glycoproteins. (B) Principal component analysis of 95C and 95D EVs total proteins (T‐p) and glycoproteins (G‐p). (C) Venn diagram of EVs total proteins and glycoproteins. (D) Pearson correlation coefficient matrix plot of multiple groups. The correlation coefficient was represented by a color scheme from white (negative correlation) to blue (positive correlation). (E) The volcano plot represents the quantitative analysis of N‐glycoproteins in 95D EVs versus 95C EVs. Orange represents proteins that were at least 2‐fold upregulated ( p < 0.05); blue represents proteins that were at least 2‐fold downregulated ( p < 0.05). (F) Distribution plot of the number of N‐glycosylation sites of 95C and 95D EVs. (G‐I) Comparison of the ranking, relative quantity, and unique peptides of three typical glycoproteins before and after ConA enrichment. GO analysis (J) and KEGG pathway enrichment (K) of differentially expressed glycoproteins in EVs. BP, biological process; CC, cellular component; MF, molecular function.

    Article Snippet: Briefly, for 1 mg EVs protein, 1 mL of agarose bound lectin ConA (Vector Laboratories, AL‐1003) was packed into a 2 mL disposable screw end‐cap spin column with filter (Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques: Glycoproteomics, Comparison

    Lectin detection profiles. A total of 12 plasmon shift values, measured after 15 min of immobilization, were recorded for each lectin, with the average and standard deviation values represented by each band in the graph. Each lectin is used to create the LPS profiles for each bacterial species injected at 100 μg/mL, as well as a PBS buffer blank reference. The lectins chosen are Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA). These lectins will be referred by their abbreviation for the next figures to avoid unnecessary length in the legend.

    Journal: ACS Omega

    Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

    doi: 10.1021/acsomega.5c00867

    Figure Lengend Snippet: Lectin detection profiles. A total of 12 plasmon shift values, measured after 15 min of immobilization, were recorded for each lectin, with the average and standard deviation values represented by each band in the graph. Each lectin is used to create the LPS profiles for each bacterial species injected at 100 μg/mL, as well as a PBS buffer blank reference. The lectins chosen are Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA). These lectins will be referred by their abbreviation for the next figures to avoid unnecessary length in the legend.

    Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

    Techniques: Standard Deviation, Injection

    Feature importance coefficient. Each bar illustrates the mean importance coefficients for the 7 features associated with 7 lectins, calculated from 10 randomly selected train/test splits of the data set using a Random Forest model with 100 trees.

    Journal: ACS Omega

    Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

    doi: 10.1021/acsomega.5c00867

    Figure Lengend Snippet: Feature importance coefficient. Each bar illustrates the mean importance coefficients for the 7 features associated with 7 lectins, calculated from 10 randomly selected train/test splits of the data set using a Random Forest model with 100 trees.

    Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

    Techniques:

    Feature reduction for RF and SVM machine learning models. The best-performing lectin set from the combination of increasing number of lectins (1 to 7, from left to right) is used in a 10 repeated 3-fold cross-validation to determine the accuracy for each model. Significant differences are assessed with a t -test ( p > 0.05). An asterisk indicates a distribution with a statistically significant difference in performance compared to a distribution without it.

    Journal: ACS Omega

    Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

    doi: 10.1021/acsomega.5c00867

    Figure Lengend Snippet: Feature reduction for RF and SVM machine learning models. The best-performing lectin set from the combination of increasing number of lectins (1 to 7, from left to right) is used in a 10 repeated 3-fold cross-validation to determine the accuracy for each model. Significant differences are assessed with a t -test ( p > 0.05). An asterisk indicates a distribution with a statistically significant difference in performance compared to a distribution without it.

    Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

    Techniques:

    Classification Report for Different Profile Lengths with the SVM Model

    Journal: ACS Omega

    Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

    doi: 10.1021/acsomega.5c00867

    Figure Lengend Snippet: Classification Report for Different Profile Lengths with the SVM Model

    Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

    Techniques:

    Classification Report for Different Profile Lengths with the RF Model

    Journal: ACS Omega

    Article Title: Lipopolysaccharide Detection with Glycan-Specific Lectins—a Nonspecific Binding Approach Applied to Surface Plasmon Resonance

    doi: 10.1021/acsomega.5c00867

    Figure Lengend Snippet: Classification Report for Different Profile Lengths with the RF Model

    Article Snippet: Biotinylated lectins Concanavalin (ConA), Glycine max agglutinin (SBA), Triticum vulgaris agglutinin (WGA), Dolichos biflorus agglutinin (DBA), Ulex europaeus agglutinin (UEA I), Ricinus communis agglutinin (RCA), and Arachis hypogea agglutinin (PNA) were purchased from Vector Laboratories (Newark, US).

    Techniques: