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biotin wga lectin  (Vector Laboratories)


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    Structured Review

    Vector Laboratories biotin wga lectin
    Biotin Wga Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 245 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/biotin wga lectin/product/Vector Laboratories
    Average 94 stars, based on 245 article reviews
    biotin wga lectin - by Bioz Stars, 2026-03
    94/100 stars

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    Vector Laboratories biotin conjugated wheat germ agglutinin lectin
    Post-transfer processing of N-glycans in the Dictyostelium HL241 strain. A proposed scheme for the modification of N-glycans in the HL241 strain commencing after the transfer of Man 6 GlcNAc 2 (boxed). Whereas the anionic modifications and the intersecting N- acetylglucosamine residue can be found on both Man 5 GlcNAc 2 and Man 6 GlcNAc 2 scaffolds, the transfer of fucose and bisecting N- acetylglucosamine appears to be dependent on the prior removal of one terminal α1,2-mannose residue from the A branch. Reactions for which there is evidence from the literature are shown with solid arrows ; for some reactions involving fucosylated glycans, the order of processing is unclear and so these are indicated with dashed arrows . The predicted antibody or <t>lectin</t> reactivity status <t>(anti-Man6P,</t> <t>anti-HRP</t> or WGA) of the four glycans at the foot of the diagram is also indicated.
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    Vector Laboratories biotin conjugated wheat germ agglutinin wga lectin staining
    Post-transfer processing of N-glycans in the Dictyostelium HL241 strain. A proposed scheme for the modification of N-glycans in the HL241 strain commencing after the transfer of Man 6 GlcNAc 2 (boxed). Whereas the anionic modifications and the intersecting N- acetylglucosamine residue can be found on both Man 5 GlcNAc 2 and Man 6 GlcNAc 2 scaffolds, the transfer of fucose and bisecting N- acetylglucosamine appears to be dependent on the prior removal of one terminal α1,2-mannose residue from the A branch. Reactions for which there is evidence from the literature are shown with solid arrows ; for some reactions involving fucosylated glycans, the order of processing is unclear and so these are indicated with dashed arrows . The predicted antibody or <t>lectin</t> reactivity status <t>(anti-Man6P,</t> <t>anti-HRP</t> or WGA) of the four glycans at the foot of the diagram is also indicated.
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    Average 96 stars, based on 1 article reviews
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    Post-transfer processing of N-glycans in the Dictyostelium HL241 strain. A proposed scheme for the modification of N-glycans in the HL241 strain commencing after the transfer of Man 6 GlcNAc 2 (boxed). Whereas the anionic modifications and the intersecting N- acetylglucosamine residue can be found on both Man 5 GlcNAc 2 and Man 6 GlcNAc 2 scaffolds, the transfer of fucose and bisecting N- acetylglucosamine appears to be dependent on the prior removal of one terminal α1,2-mannose residue from the A branch. Reactions for which there is evidence from the literature are shown with solid arrows ; for some reactions involving fucosylated glycans, the order of processing is unclear and so these are indicated with dashed arrows . The predicted antibody or lectin reactivity status (anti-Man6P, anti-HRP or WGA) of the four glycans at the foot of the diagram is also indicated.

    Journal: Journal of Proteome Research

    Article Title: Mass Spectrometric Analysis of Neutral and Anionic N-Glycans from a Dictyostelium discoideum Model for Human Congenital Disorder of Glycosylation CDG IL

    doi: 10.1021/pr300806b

    Figure Lengend Snippet: Post-transfer processing of N-glycans in the Dictyostelium HL241 strain. A proposed scheme for the modification of N-glycans in the HL241 strain commencing after the transfer of Man 6 GlcNAc 2 (boxed). Whereas the anionic modifications and the intersecting N- acetylglucosamine residue can be found on both Man 5 GlcNAc 2 and Man 6 GlcNAc 2 scaffolds, the transfer of fucose and bisecting N- acetylglucosamine appears to be dependent on the prior removal of one terminal α1,2-mannose residue from the A branch. Reactions for which there is evidence from the literature are shown with solid arrows ; for some reactions involving fucosylated glycans, the order of processing is unclear and so these are indicated with dashed arrows . The predicted antibody or lectin reactivity status (anti-Man6P, anti-HRP or WGA) of the four glycans at the foot of the diagram is also indicated.

    Article Snippet: After blocking with 0.5% (w/v) bovine serum albumin in Tris-buffered saline, the membranes were incubated with rabbit antihorseradish peroxidase (anti-HRP, Sigma-Aldrich; 1:10 000) or biotin-conjugated wheat germ agglutinin lectin (WGA, Vector Laboratories; 1:2000).

    Techniques: Modification