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fluorescein labeled soybean lectin  (Vector Laboratories)


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    Structured Review

    Vector Laboratories fluorescein labeled soybean lectin
    Heat map displaying <t>lectin</t> binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .
    Fluorescein Labeled Soybean Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 93/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein labeled soybean lectin/product/Vector Laboratories
    Average 93 stars, based on 26 article reviews
    fluorescein labeled soybean lectin - by Bioz Stars, 2026-02
    93/100 stars

    Images

    1) Product Images from "Enzymatic tailoring of anionic glycans for characterizing lectin and antibody specificities in a microarray format"

    Article Title: Enzymatic tailoring of anionic glycans for characterizing lectin and antibody specificities in a microarray format

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2025.110915

    Heat map displaying lectin binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .
    Figure Legend Snippet: Heat map displaying lectin binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .

    Techniques Used: Binding Assay, Generated

    Heat map displaying Gal-specific lectin binding to all structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Terminal modifications (of either one or both antennae) are shown. Unmodified β4Gal is indicated as x (no modification) while free terminal β3Gal is marked (compounds 21 and 38 ). For complete structures please refer to .
    Figure Legend Snippet: Heat map displaying Gal-specific lectin binding to all structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Terminal modifications (of either one or both antennae) are shown. Unmodified β4Gal is indicated as x (no modification) while free terminal β3Gal is marked (compounds 21 and 38 ). For complete structures please refer to .

    Techniques Used: Binding Assay, Generated, Modification



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    Heat map displaying <t>lectin</t> binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .
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    Heat map displaying <t>lectin</t> binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .
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    Image Search Results


    Heat map displaying lectin binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .

    Journal: The Journal of Biological Chemistry

    Article Title: Enzymatic tailoring of anionic glycans for characterizing lectin and antibody specificities in a microarray format

    doi: 10.1016/j.jbc.2025.110915

    Figure Lengend Snippet: Heat map displaying lectin binding to selected sialylated and sulfated structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Relevant epitopes are shown, structures including either Neu5Ac or Neu5Gc as terminal sialic acid or different linkages are indicated with a slash. For complete structures, please refer to .

    Article Snippet: Biotinylated lectins concanavalin A (ConA, 5 mg/ml), Erythrina cristagalli lectin (ECL, 5 mg/ml), Griffonia simplicifolia isolectin B4 (GSL-I, 0.5 mg/ml) and II (GSL-II, 2 mg/ml), Lens culinaris lectin (LCA, 5 mg/ml), Maackia amurensis lectin I and II (MAA-I, 2 mg/ml; MAA-II, 1 mg/ml), peanut lectin (PNA 5 mg/ml), Ricinus communis lectin I (RCA, 5 mg/ml), Sambucus nigra /Elderberry Bark lectin (SNA, 2 mg/ml), Vicia villosa lectin (VVA, 2 mg/ml), Wisteria floribunda agglutinin (WFA, 2 mg/ml) and wheat germ agglutinin (WGA, 5 mg/ml), as well as fluorescein-labeled soybean lectin (SBA, 2 mg/ml) were purchased from Vector Laboratories.

    Techniques: Binding Assay, Generated

    Heat map displaying Gal-specific lectin binding to all structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Terminal modifications (of either one or both antennae) are shown. Unmodified β4Gal is indicated as x (no modification) while free terminal β3Gal is marked (compounds 21 and 38 ). For complete structures please refer to .

    Journal: The Journal of Biological Chemistry

    Article Title: Enzymatic tailoring of anionic glycans for characterizing lectin and antibody specificities in a microarray format

    doi: 10.1016/j.jbc.2025.110915

    Figure Lengend Snippet: Heat map displaying Gal-specific lectin binding to all structures . The heat map was generated using the GLAD tool and represents the relative fluorescent units (RFU) normalized to 70,000 as the maximum value. Terminal modifications (of either one or both antennae) are shown. Unmodified β4Gal is indicated as x (no modification) while free terminal β3Gal is marked (compounds 21 and 38 ). For complete structures please refer to .

    Article Snippet: Biotinylated lectins concanavalin A (ConA, 5 mg/ml), Erythrina cristagalli lectin (ECL, 5 mg/ml), Griffonia simplicifolia isolectin B4 (GSL-I, 0.5 mg/ml) and II (GSL-II, 2 mg/ml), Lens culinaris lectin (LCA, 5 mg/ml), Maackia amurensis lectin I and II (MAA-I, 2 mg/ml; MAA-II, 1 mg/ml), peanut lectin (PNA 5 mg/ml), Ricinus communis lectin I (RCA, 5 mg/ml), Sambucus nigra /Elderberry Bark lectin (SNA, 2 mg/ml), Vicia villosa lectin (VVA, 2 mg/ml), Wisteria floribunda agglutinin (WFA, 2 mg/ml) and wheat germ agglutinin (WGA, 5 mg/ml), as well as fluorescein-labeled soybean lectin (SBA, 2 mg/ml) were purchased from Vector Laboratories.

    Techniques: Binding Assay, Generated, Modification