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gnl fluorescein vector cat  (Vector Laboratories)


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    Structured Review

    Vector Laboratories gnl fluorescein vector cat
    Gnl Fluorescein Vector Cat, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/FL-1241-2/Fluorescein+labeled+Galanthus+Nivalis+Lectin+(GNL)/pm40609542-715-46-47
    Average 94 stars, based on 26 article reviews
    gnl fluorescein vector cat - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Flow Cytometry:

    Article Title: CRISPR screens and lectin microarrays identify high mannose N-glycan regulators.
    Article Snippet: .. Other lectins used in flow cytometry experiments include: GNL (Vector Laboratories, FL-1241-2), Lch (EY Laboratories, F-1401-5), SNA (Bioworld 21500045-1), PNA (XXXX),CSA (EY Laboratories, BA3201-1), PHA-L, SLBR-H, and SLBR-N (made in-house in the Mahal Lab). .. UPLC Quantification of high mannose N-glycan structures Proteins were harvested from A549s with or without XBP1s-induction using 1% NP-40 lysis buffer -− 1% NP-40, 150mMNaCl, and 50mMTris- Cl pH 8) supplemented with cOmplete protease inhibitor (Roche, 11836170001).

    Article Title: CRISPR screens and lectin microarrays identify high mannose N-glycan regulators
    Article Snippet: .. Other lectins used in flow cytometry experiments include: GNL (Vector Laboratories, FL-1241-2), Lch (EY Laboratories, F-1401-5), SNA (Bioworld 21500045-1), PNA (XXXX),CSA (EY Laboratories, BA-3201-1), PHA-L, SLBR-H, and SLBR-N (made in-house in the Mahal Lab). .. Proteins were harvested from A549s with or without XBP1s-induction using 1% NP-40 lysis buffer -− 1% NP-40, 150 mM NaCl, and 50 mM Tris-Cl pH 8) supplemented with cOmplete protease inhibitor (Roche, 11836170001).

    Incubation:

    Article Title: Detection of Aggressive Mesenchymal Glioblastoma by Mannose-Weighted CEST MRI
    Article Snippet: .. Cells were first incubated in cold PBS containing 20 μg/ml GNL-FITC (FL-1241, Vector Laboratories) at 4 °C for 50 minutes for the presence of mannose, then washed three times with PBS. .. They were fixed with 4% paraformaldehyde for 20 min at room temperature (RT) and permeabilized using 0.1% Triton X-100 in PBS for 10 min. After blocking non-specific binding sites with 5% normal goat serum (NGS), cells were incubated with primary Alexa Fluor® 647 anti-CD44 antibody (1:250, Abcam, EPR18668) according to the manufacturer’s protocol (3 h at RT in the dark).

    other:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al, 2025, Developmental Cell 60, 1–18 December 15, 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies

    Staining:

    Article Title: Non-cellular root canal filler and non-cellular dental tissue regeneration promotion kit
    Article Snippet: .. Angiogenesis was evaluated by staining day 28 specimens with Fluorescein labeled Griffonia simplicifolia (Bandeiraea simplicifolia) Lectin I (GSL I, BSL I) and Fluorescein labeled Galanthus nivalis (Snowdrop) Lectin (GNL) (Vector Laboratories) (20 μg/ml) for 15 minutes, followed by comparative examination. ..

    Labeling:

    Article Title: Non-cellular root canal filler and non-cellular dental tissue regeneration promotion kit
    Article Snippet: .. Angiogenesis was evaluated by staining day 28 specimens with Fluorescein labeled Griffonia simplicifolia (Bandeiraea simplicifolia) Lectin I (GSL I, BSL I) and Fluorescein labeled Galanthus nivalis (Snowdrop) Lectin (GNL) (Vector Laboratories) (20 μg/ml) for 15 minutes, followed by comparative examination. ..

    Recombinant:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Whole Genome Amplification:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Transfection:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Real-time Polymerase Chain Reaction:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    CCK-8 Assay:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Western Blot:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Mass Spectrometry:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Quantitative Proteomics:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll

    Multiple Displacement Amplification:

    Article Title: TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy.
    Article Snippet: Article TM9SF3 is a Golgi-resident ATG8-binding protein essential for Golgi-selective autophagy Graphical abstract Highlights • TM9SF3 is a receptor required for Golgiphagy induced by nutrient and Golgi stress • TM9SF3 promotes Golgi fragmentation and directs fragments to autophagosomes • TM9SF3 degrades misglycosylated proteins to maintain glycosylation homeostasis • TM9SF3 promotes breast cancer cell growth and predicts poor patient prognosis Authors Jiejie Yang, Yang Dong, Jiaxin Xu, ..., Ding Gao, Zongqiang Cui, Yixian Cui Correspondence yixian.cui@whu.edu.cn In brief Yang et al. identify TM9SF3 as a Golgi- resident receptor essential for selective autophagy of the Golgi (Golgiphagy).. TM9SF3 binds ATG8 proteins via its LIR motifs and controls the degradation of Golgi fragments—including incompletely glycosylated proteins—supporting Golgi homeostasis and breast cancer progression.. Yang et al., 2025, Developmental Cell 60, 1–18 December 15, 2025 © 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies. https://doi.org/10.1016/j.devcel.2025.06.017 ll



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