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lectin concanavalin a cona  (Vector Laboratories)


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    Structured Review

    Vector Laboratories lectin concanavalin a cona
    Effect of the fungal lectins tested in this study on the viability of Listeria innocua and Listeria monocytogenes within the biofilm, their sensitivity to proteinase K digestion and their known binding motifs.
    Lectin Concanavalin A Cona, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 522 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lectin concanavalin a cona/product/Vector Laboratories
    Average 94 stars, based on 522 article reviews
    lectin concanavalin a cona - by Bioz Stars, 2026-05
    94/100 stars

    Images

    1) Product Images from "Exposure to specific fungal lectins during adhesion impairs biofilm formation of Listeria on polystyrene"

    Article Title: Exposure to specific fungal lectins during adhesion impairs biofilm formation of Listeria on polystyrene

    Journal: Microbial Biotechnology

    doi: 10.1111/1751-7915.70040

    Effect of the fungal lectins tested in this study on the viability of Listeria innocua and Listeria monocytogenes within the biofilm, their sensitivity to proteinase K digestion and their known binding motifs.
    Figure Legend Snippet: Effect of the fungal lectins tested in this study on the viability of Listeria innocua and Listeria monocytogenes within the biofilm, their sensitivity to proteinase K digestion and their known binding motifs.

    Techniques Used: Binding Assay, Activity Assay

    Effect of the lectin CGL2 on biofilm development of Listeria innocua and Listeria monocytogenes at the time of adhesion (1 h) and its effect on the 24‐h‐old mature biofilm to study its ability to disperse the biofilm. CGL2 was the only lectin tested that affected the mature biofilm. The bacteria of the remaining biofilm were labelled with the DNA probe Syto9, and images were taken at 10× magnification.
    Figure Legend Snippet: Effect of the lectin CGL2 on biofilm development of Listeria innocua and Listeria monocytogenes at the time of adhesion (1 h) and its effect on the 24‐h‐old mature biofilm to study its ability to disperse the biofilm. CGL2 was the only lectin tested that affected the mature biofilm. The bacteria of the remaining biofilm were labelled with the DNA probe Syto9, and images were taken at 10× magnification.

    Techniques Used: Bacteria



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    A) The general workflow for enrichment and glycoproteomic analysis of co-occupied peptides from complex samples is depicted. An N-glycopeptide-level enrichment was performed on HeLa lysate with the lectin, <t>ConA.</t> Similarly, an O-glycopeptide-level enrichment was performed on human serum with the lectin, Jacalin, and mucin-domain glycoprotein-level enrichment was performed on HeLa lysate <t>with</t> <t>StcE</t> E447D . All glycopeptides were treated with PNGaseF (for quantitation) and analyzed by LC-MS/MS. XICs were generated for each glycopeptide and AUC quantitation was performed. B) LC-MS/MS analysis was used to identify 14 N- and O-glycopeptides across all enrichments.
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    A) The general workflow for enrichment and glycoproteomic analysis of co-occupied peptides from complex samples is depicted. An N-glycopeptide-level enrichment was performed on HeLa lysate with the lectin, <t>ConA.</t> Similarly, an O-glycopeptide-level enrichment was performed on human serum with the lectin, Jacalin, and mucin-domain glycoprotein-level enrichment was performed on HeLa lysate <t>with</t> <t>StcE</t> E447D . All glycopeptides were treated with PNGaseF (for quantitation) and analyzed by LC-MS/MS. XICs were generated for each glycopeptide and AUC quantitation was performed. B) LC-MS/MS analysis was used to identify 14 N- and O-glycopeptides across all enrichments.
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    Image Search Results


    Effect of the fungal lectins tested in this study on the viability of Listeria innocua and Listeria monocytogenes within the biofilm, their sensitivity to proteinase K digestion and their known binding motifs.

    Journal: Microbial Biotechnology

    Article Title: Exposure to specific fungal lectins during adhesion impairs biofilm formation of Listeria on polystyrene

    doi: 10.1111/1751-7915.70040

    Figure Lengend Snippet: Effect of the fungal lectins tested in this study on the viability of Listeria innocua and Listeria monocytogenes within the biofilm, their sensitivity to proteinase K digestion and their known binding motifs.

    Article Snippet: Lectin Concanavalin A (ConA) (L‐1000) was purchased from Vector Labs.

    Techniques: Binding Assay, Activity Assay

    Effect of the lectin CGL2 on biofilm development of Listeria innocua and Listeria monocytogenes at the time of adhesion (1 h) and its effect on the 24‐h‐old mature biofilm to study its ability to disperse the biofilm. CGL2 was the only lectin tested that affected the mature biofilm. The bacteria of the remaining biofilm were labelled with the DNA probe Syto9, and images were taken at 10× magnification.

    Journal: Microbial Biotechnology

    Article Title: Exposure to specific fungal lectins during adhesion impairs biofilm formation of Listeria on polystyrene

    doi: 10.1111/1751-7915.70040

    Figure Lengend Snippet: Effect of the lectin CGL2 on biofilm development of Listeria innocua and Listeria monocytogenes at the time of adhesion (1 h) and its effect on the 24‐h‐old mature biofilm to study its ability to disperse the biofilm. CGL2 was the only lectin tested that affected the mature biofilm. The bacteria of the remaining biofilm were labelled with the DNA probe Syto9, and images were taken at 10× magnification.

    Article Snippet: Lectin Concanavalin A (ConA) (L‐1000) was purchased from Vector Labs.

    Techniques: Bacteria

    A) The general workflow for enrichment and glycoproteomic analysis of co-occupied peptides from complex samples is depicted. An N-glycopeptide-level enrichment was performed on HeLa lysate with the lectin, ConA. Similarly, an O-glycopeptide-level enrichment was performed on human serum with the lectin, Jacalin, and mucin-domain glycoprotein-level enrichment was performed on HeLa lysate with StcE E447D . All glycopeptides were treated with PNGaseF (for quantitation) and analyzed by LC-MS/MS. XICs were generated for each glycopeptide and AUC quantitation was performed. B) LC-MS/MS analysis was used to identify 14 N- and O-glycopeptides across all enrichments.

    Journal: bioRxiv

    Article Title: Quantification and site-specific analysis of co-occupied N- and O-glycopeptides

    doi: 10.1101/2024.07.06.602348

    Figure Lengend Snippet: A) The general workflow for enrichment and glycoproteomic analysis of co-occupied peptides from complex samples is depicted. An N-glycopeptide-level enrichment was performed on HeLa lysate with the lectin, ConA. Similarly, an O-glycopeptide-level enrichment was performed on human serum with the lectin, Jacalin, and mucin-domain glycoprotein-level enrichment was performed on HeLa lysate with StcE E447D . All glycopeptides were treated with PNGaseF (for quantitation) and analyzed by LC-MS/MS. XICs were generated for each glycopeptide and AUC quantitation was performed. B) LC-MS/MS analysis was used to identify 14 N- and O-glycopeptides across all enrichments.

    Article Snippet: Conjugation of 1 mg of StcE E447D or ConA (Vector Laboratories, L-1000) to 1 mL of NHS-activated Sepharose 4 Fast Flow (Cytiva, 17090601) was performed by rotation at 4 ºC for 4 hours.

    Techniques: Quantitation Assay, Liquid Chromatography with Mass Spectroscopy, Generated