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cona agarose beads  (Vector Laboratories)


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    Structured Review

    Vector Laboratories cona agarose beads
    Cona Agarose Beads, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/agarose+bound+concanavalin+a+%28con+a%29/pm41957353-561-10-12?v=Vector+Laboratories
    Average 94 stars, based on 75 article reviews
    cona agarose beads - by Bioz Stars, 2026-07
    94/100 stars

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    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.
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    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.
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    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.
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    Vector Laboratories concanavalin a cona agarose
    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.
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    Vector Laboratories un bound agarose beads
    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.
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    Vector Laboratories agarose bound concanavalin con
    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.
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    Image Search Results


    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