fitc labelled ulex europaeus agglutinin i  (Vector Laboratories)

Journal: Transfusion

Article Title: Glycan‐binding specificities of anti‐ ABO (H) antibodies and lectins

doi: 10.1111/trf.70027

Figure Lengend Snippet: Normalized Relative Fluorescence Units (RFU) indicating the binding of (A) UEA‐I (red), (B) HPA (purple), (C) DBA (green), (D) anti‐A antibody (blue), and (E) anti‐B antibody (orange) to 117 glycans. Each of the 117 glycans is indicated as a hashmark on the X‐axis. Negative control spots contain buffer only instead of a glycan. Results are shown as mean ± 1 standard deviation ( n = 4 spots/glycan). The background colors were used across all panels to indicate glycans that have H structures (pink), A structures (light blue) and B structures (yellow). The glycan structures are represented using the Symbol Nomenclature for Glycans (SNFG). ¹⁷ The complete datasets are available in the Figure . Structures of certain glycans mentioned in the text are provided in Figure .

Article Snippet: Biotinylated UEA‐I (Cat# B‐1065‐2) and DBA (Cat# B‐1035‐5) were from Vector Labs, while HPA was from Sigma Aldrich (Cat# L6512).

Techniques: Fluorescence, Binding Assay, Negative Control, Glycoproteomics, Standard Deviation

Journal: Journal of Translational Autoimmunity

Article Title: Afucosylated IgG in idiopathic nephrotic syndrome patients with anti-nephrin autoantibodies correlate with disease activity

doi: 10.1016/j.jtauto.2025.100307

Figure Lengend Snippet: Evaluation of IgG fucosylation in healthy donor samples using biotinylated lectins under competitive and enzymatic treatments. Panel A shows a schematic representation of N-glycans linked to Asn297 of IgG, depicting core (α1,6-linked) and antennary (α1,2-linked) fucosylation. Panels B and C show the levels of fucosylated IgG from serum of healthy donors, either untreated or preincubated with L-fucose or D-lactose to compete for binding to AAL (Panel B) or UEA-I (Panel C) or pretreated with PNGase F to enzymatically remove N-glycans (Panels B and C). These experiments were performed to confirm lectin specificity in the detection of IgG fucosylation under defined conditions.

Article Snippet: After five washes, 100 μL of Aleuria Aurantia Lectin (AAL; Vector Laboratories Cat# B1395-1) or biotinylated Ulex Europaeus Agglutinin I (UEA-I; Vector Laboratories Cat# B1065-2), both diluted 1:1000 in SuperT, were added and incubated ON at 4 °C.

Techniques: Binding Assay

Journal: Journal of Translational Autoimmunity

Article Title: Afucosylated IgG in idiopathic nephrotic syndrome patients with anti-nephrin autoantibodies correlate with disease activity

doi: 10.1016/j.jtauto.2025.100307

Figure Lengend Snippet: Evaluation of fucose in IgG by enzyme-linked immunosorbent assay (ELISA) with biotinylated lectins. Panels A and B show the levels of core-fucosylated IgG (α1,6-linked fucose) and antennary-fucosylated IgG (α1,2-linked fucose), respectively, measured using AAL and UEA-I lectins in the serum of healthy donors and NS patients, stratified by circulating anti-nephrin autoantibodies. Panels C and D display the inverse correlation between 24-h proteinuria and serum IgG fucosylation levels, as measured by AAL (Panel C) and UEA-I (Panel D), in patients with anti-nephrin–associated MCD or FSGS. Panels E and F show the corresponding levels of core and antennary fucosylation in IgG from urine samples, measured by AAL and UEA-I, and stratified by anti-nephrin antibody status. Red dots indicate patients positive for anti-nephrin autoantibodies, as confirmed by both ELISA and immunoprecipitation.

Article Snippet: After five washes, 100 μL of Aleuria Aurantia Lectin (AAL; Vector Laboratories Cat# B1395-1) or biotinylated Ulex Europaeus Agglutinin I (UEA-I; Vector Laboratories Cat# B1065-2), both diluted 1:1000 in SuperT, were added and incubated ON at 4 °C.

Techniques: Enzyme-linked Immunosorbent Assay, Immunoprecipitation