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biotinylated sambucus nigra lectin sna  (Vector Laboratories)


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    Structured Review

    Vector Laboratories biotinylated sambucus nigra lectin sna
    Biotinylated Sambucus Nigra Lectin Sna, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 749 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/biotinylated+sambucus+nigra+lectin/Biotinylated+Sambucus+Nigra+Lectin+(SNA%2C+EBL)/pm42863691-56-0-13
    Average 96 stars, based on 749 article reviews
    biotinylated sambucus nigra lectin sna - by Bioz Stars, 2026-11
    96/100 stars

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    Related Articles

    Clinical Proteomics:

    Article Title: Amphotericin B promotes respiratory viral entry by enhancing late endosomal maturation and fusion via glucocerebrosidase-mediated ceramide remodeling
    Article Snippet: .. For the latter, cells were co‐stained with mouse anti‐IAV NP antibody (Cat# ab20343, 1:100; Abcam, USA) and biotinylated Sambucus nigra lectin (Cat# B-1305-2, 1:200; Vector, Germany) to label sialic acid residues on the plasma membrane. .. As a negative control, parallel cell samples were pretreated with 50 mU/mL neuraminidase (Cat# 11080725001, Merck, Germany) for 1 h at 37 °C before virus binding.

    Article Title: Amphotericin B promotes respiratory viral entry by enhancing late endosomal maturation and fusion via glucocerebrosidase-mediated ceramide remodeling.
    Article Snippet: .. For the latter, cells were co‐stained with mouse anti‐IAV NP antibody (Cat# ab20343, 1:100; Abcam, USA) and biotinylated Sambucus nigra lectin (Cat# B-1305-2, 1:200; Vector, Germany) to label sialic acid residues on the plasma membrane. .. As a negative control, parallel cell samples were pretreated with 50 mU/mL neuraminidase (Cat# 11080725001; Merck, Germany) for 1 h at 37°C before virus binding.

    Membrane:

    Article Title: Amphotericin B promotes respiratory viral entry by enhancing late endosomal maturation and fusion via glucocerebrosidase-mediated ceramide remodeling
    Article Snippet: .. For the latter, cells were co‐stained with mouse anti‐IAV NP antibody (Cat# ab20343, 1:100; Abcam, USA) and biotinylated Sambucus nigra lectin (Cat# B-1305-2, 1:200; Vector, Germany) to label sialic acid residues on the plasma membrane. .. As a negative control, parallel cell samples were pretreated with 50 mU/mL neuraminidase (Cat# 11080725001, Merck, Germany) for 1 h at 37 °C before virus binding.

    Article Title: Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach
    Article Snippet: HEK293T cells were lysed for analysis of whole cell protein expression by adding 50 μL (12 well format) or 100 μL (6 well format) of Laemmli buffer 2× (Sigma-Aldrich) supplemented with 250 U/mL Benzonase (Merck Millipore, part of Merck KGaA, Darmstadt, Germany) and protease Halt inhibitor 100× (Thermo Fisher). .. After blocking, the membrane was washed and incubated for 2 h with biotinylated Sambucus nigra lectin (SNA, Vector Laboratories, Biozol, Hamburg, Germany) at a concentration of 5 μg/mL in 3% BSA. .. Prepared protein extracts were separated by SDS-PAGE by using 4-15% Protean TGX gels (Biorad, Munich, Germany).

    Article Title: Amphotericin B promotes respiratory viral entry by enhancing late endosomal maturation and fusion via glucocerebrosidase-mediated ceramide remodeling.
    Article Snippet: .. For the latter, cells were co‐stained with mouse anti‐IAV NP antibody (Cat# ab20343, 1:100; Abcam, USA) and biotinylated Sambucus nigra lectin (Cat# B-1305-2, 1:200; Vector, Germany) to label sialic acid residues on the plasma membrane. .. As a negative control, parallel cell samples were pretreated with 50 mU/mL neuraminidase (Cat# 11080725001; Merck, Germany) for 1 h at 37°C before virus binding.

    other:

    Article Title: Integrated transcriptome and proteome analyses unveil cytoskeletal alterations in an endothelial model of monogenic diabetes.
    Article Snippet: After two days, cells were fixed with 4 % paraformaldehyde (Sigma) at room temperature (RT) for 15 minutes.

    Article Title: Amphotericin B promotes respiratory viral entry by enhancing late endosomal maturation and fusion via glucocerebrosidase-mediated ceramide remodeling.
    Article Snippet: Cells grown on coverslips were fixed in 4% PFA (Beyotime, China) for 10 min.

    Incubation:

    Article Title: Integrated transcriptome and proteome analyses unveil cytoskeletal alterations in an endothelial model of monogenic diabetes
    Article Snippet: .. To recognize sialic acid, cells were incubated overnight at 4 °C with biotinylated Sambucus Nigra Lectin (EBL, Vector Laboratories) in 3% BSA in PBS. ..

    Article Title: Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach
    Article Snippet: HEK293T cells were lysed for analysis of whole cell protein expression by adding 50 μL (12 well format) or 100 μL (6 well format) of Laemmli buffer 2× (Sigma-Aldrich) supplemented with 250 U/mL Benzonase (Merck Millipore, part of Merck KGaA, Darmstadt, Germany) and protease Halt inhibitor 100× (Thermo Fisher). .. After blocking, the membrane was washed and incubated for 2 h with biotinylated Sambucus nigra lectin (SNA, Vector Laboratories, Biozol, Hamburg, Germany) at a concentration of 5 μg/mL in 3% BSA. .. Prepared protein extracts were separated by SDS-PAGE by using 4-15% Protean TGX gels (Biorad, Munich, Germany).

    Blocking Assay:

    Article Title: Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach
    Article Snippet: HEK293T cells were lysed for analysis of whole cell protein expression by adding 50 μL (12 well format) or 100 μL (6 well format) of Laemmli buffer 2× (Sigma-Aldrich) supplemented with 250 U/mL Benzonase (Merck Millipore, part of Merck KGaA, Darmstadt, Germany) and protease Halt inhibitor 100× (Thermo Fisher). .. After blocking, the membrane was washed and incubated for 2 h with biotinylated Sambucus nigra lectin (SNA, Vector Laboratories, Biozol, Hamburg, Germany) at a concentration of 5 μg/mL in 3% BSA. .. Prepared protein extracts were separated by SDS-PAGE by using 4-15% Protean TGX gels (Biorad, Munich, Germany).

    Concentration Assay:

    Article Title: Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach
    Article Snippet: HEK293T cells were lysed for analysis of whole cell protein expression by adding 50 μL (12 well format) or 100 μL (6 well format) of Laemmli buffer 2× (Sigma-Aldrich) supplemented with 250 U/mL Benzonase (Merck Millipore, part of Merck KGaA, Darmstadt, Germany) and protease Halt inhibitor 100× (Thermo Fisher). .. After blocking, the membrane was washed and incubated for 2 h with biotinylated Sambucus nigra lectin (SNA, Vector Laboratories, Biozol, Hamburg, Germany) at a concentration of 5 μg/mL in 3% BSA. .. Prepared protein extracts were separated by SDS-PAGE by using 4-15% Protean TGX gels (Biorad, Munich, Germany).

    Article Title: Spatial differences in the ovine cervical microenvironment at the follicular and luteal phases of the oestrous cycle; Implications for sperm transport.
    Article Snippet: .. Biotinylated Sambucus nigra lectin (Vector Laboratories, California, USA) was prepared at a working concentration of 10 μg/mL in PBS (10 mM sodium phosphate, 150 mM NaCl, pH 7.4), and 100 μL was applied per section. ..



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    Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in wild-type and ST6GAL1 −/− /ST3GAL4 −/− pig fibroblasts/respiratory tissues. A: Quantitative reverse transcription-PCR analysis of ST6GAL1 and ST3GAL4 gene expression levels in ST6GAL1 −/− / ST3GAL4 −/− knockout (KO) and wild-type (WT) pig fibroblasts. Data are presented as mean ± standard deviation (SD); n = 3 independent biological replicates, representing fibroblasts isolated from three separate pigs for each genotype group. Statistical significance between WT and KO groups was assessed by unpaired two-sided Student's t -test, with *** P < 0.001. B: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in WT and KO pig fibroblasts. C and D: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in WT and KO pig respiratory tract. Panels show the upper respiratory tract including larynx, trachea, bronchus (C), and lung tissue (D). Red indicates <t>SNA</t> (α2,6) <t>or</t> <t>MAL</t> Ⅱ (α2,3) staining, and blue indicates nuclei. White arrows indicate sialylated glycan-positive regions in WT samples (B and C). In panel D, WT pigs exhibited a strong α2,6-linked sialylated glycan signal (white arrow) in bronchiolar epithelium, lacking an α2,3-linked sialylated glycan signal (red arrow); both sialylated glycans were present in WT alveoli (green arrows), but absent in KO pig alveoli; weak signals of both sialylated glycans were detected in the bronchiolar epithelium of KO pigs (yellow arrows). Scale bars, 100 μm (B) and 500 μm (C and D).
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    Analysis of de novo RBD expression, secretion, and intracellular TEVp-mediated cleavage in co-transfected HEK293T cells (A) Overview of the experimental set-up to analyze the total RBD-V5-His release and TEVp- c -Myc-His secretion (left side) and de novo RBD-V5-His release (right side) from co-transfected HEK293T cells. (B) Western blot analysis of the samples derived from experiment (A) by detection of V5 or c -Myc tag. (C) Western blot analysis of the secreted and residual intracellular RBD-V5-His (top) and TEVp N23Q,C130S,T173G,S219V - c -Myc-His (bottom) isolated using His-tag from 1 mL of supernatant (left lanes) or lysed co-transfected HEK293T cells from one well of a 6-well plate in 1 mL (right lanes). Cells were lysed with 1% of IGEPAL CA-630, which was also added to the supernatant. (D) Coomassie Brilliant blue-stained polyacrylamide gel quantified by comparison with a bovine serum albumin standard curve (left) and subsequent western blot probed by anti-V5 antibodies (right) of the protein released from the supernatant of co-transfected HEK293T cells obtained by co-expression of tANCHORed RBD-V5-His (top) or CD63LEL-V5-His (bottom) with or without TEVp N23Q,C130S,T173G,S219V - c -Myc-His. Highly glycosylated CD63LEL-V5-His was treated with PNGase F (peptide N-glycosidase F). (E) <t>Lectin</t> blot of the released RBD-V5-His protein, probed with <t>biotinylated</t> <t>Sambucus</t> <t>nigra</t> agglutinin (SNA) and detected using streptavidin-HRP. (F and G) Western blot analysis of the cell lysates for the expression of CD63-mCherry (F) or CD82-tANCHOR-CD63LEL-mCherry (G), with or without modified TEVp expression. Control contains untransfected cells, and TEVp was captured from the supernatant.
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    Image Search Results


    Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in wild-type and ST6GAL1 −/− /ST3GAL4 −/− pig fibroblasts/respiratory tissues. A: Quantitative reverse transcription-PCR analysis of ST6GAL1 and ST3GAL4 gene expression levels in ST6GAL1 −/− / ST3GAL4 −/− knockout (KO) and wild-type (WT) pig fibroblasts. Data are presented as mean ± standard deviation (SD); n = 3 independent biological replicates, representing fibroblasts isolated from three separate pigs for each genotype group. Statistical significance between WT and KO groups was assessed by unpaired two-sided Student's t -test, with *** P < 0.001. B: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in WT and KO pig fibroblasts. C and D: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in WT and KO pig respiratory tract. Panels show the upper respiratory tract including larynx, trachea, bronchus (C), and lung tissue (D). Red indicates SNA (α2,6) or MAL Ⅱ (α2,3) staining, and blue indicates nuclei. White arrows indicate sialylated glycan-positive regions in WT samples (B and C). In panel D, WT pigs exhibited a strong α2,6-linked sialylated glycan signal (white arrow) in bronchiolar epithelium, lacking an α2,3-linked sialylated glycan signal (red arrow); both sialylated glycans were present in WT alveoli (green arrows), but absent in KO pig alveoli; weak signals of both sialylated glycans were detected in the bronchiolar epithelium of KO pigs (yellow arrows). Scale bars, 100 μm (B) and 500 μm (C and D).

    Journal: Journal of Biomedical Research

    Article Title: Generation of ST6GAL1/ST3GAL4 double-knockout Landrace pigs with reduced respiratory sialylated glycans and decreased influenza A virus susceptibility of derived fibroblasts in vitro

    doi: 10.7555/JBR.39.20250300

    Figure Lengend Snippet: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in wild-type and ST6GAL1 −/− /ST3GAL4 −/− pig fibroblasts/respiratory tissues. A: Quantitative reverse transcription-PCR analysis of ST6GAL1 and ST3GAL4 gene expression levels in ST6GAL1 −/− / ST3GAL4 −/− knockout (KO) and wild-type (WT) pig fibroblasts. Data are presented as mean ± standard deviation (SD); n = 3 independent biological replicates, representing fibroblasts isolated from three separate pigs for each genotype group. Statistical significance between WT and KO groups was assessed by unpaired two-sided Student's t -test, with *** P < 0.001. B: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in WT and KO pig fibroblasts. C and D: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in WT and KO pig respiratory tract. Panels show the upper respiratory tract including larynx, trachea, bronchus (C), and lung tissue (D). Red indicates SNA (α2,6) or MAL Ⅱ (α2,3) staining, and blue indicates nuclei. White arrows indicate sialylated glycan-positive regions in WT samples (B and C). In panel D, WT pigs exhibited a strong α2,6-linked sialylated glycan signal (white arrow) in bronchiolar epithelium, lacking an α2,3-linked sialylated glycan signal (red arrow); both sialylated glycans were present in WT alveoli (green arrows), but absent in KO pig alveoli; weak signals of both sialylated glycans were detected in the bronchiolar epithelium of KO pigs (yellow arrows). Scale bars, 100 μm (B) and 500 μm (C and D).

    Article Snippet: Cells and tissues were then incubated with biotinylated lectins MAL II (1∶200, Cat. #B-1265-1, Vector Laboratories, Burlingame, CA, USA) or SNA (1∶200, Cat. #B-1305-2, Vector Laboratories) for 1 h, followed by three washes with PBS containing 0.05% Tween-20 (PBST).

    Techniques: Reverse Transcription, Analysis, Gene Expression, Knock-Out, Standard Deviation, Isolation, Tissue, Staining, Glycoproteomics

    Restoration of influenza virus susceptibility in ST6GAL1 −/− / ST3GAL4 −/− Landrace pig cells through complementation. A: Quantitative reverse transcription-PCR (RT-qPCR) analysis of ST6GAL1 and ST3GAL4 gene expression levels in wild-type (WT), knockout (KO), and complemented (KO + ST) cells. B: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in wild-type (WT), knockout (KO), and complemented (KO + ST) Landrace pig cells. Red indicates SNA (α2,6) or MAL Ⅱ (α2,3) staining, and blue indicates nuclei. The KO group showed nearly undetectable signals for both SNA and MAL Ⅱ. In contrast, the WT and KO + ST groups exhibited strong fluorescence for both lectins, indicating successful restoration of both α2,6- and α2,3-linked sialylated glycans in complemented cells. Scale bars, 100 μm. C: Cytopathic effects induced by H1N1 influenza virus infection at 0, 24, and 48 h post-infection (HPI). Scale bars, 500 μm. D: Immunofluorescent detection of IAV nucleoprotein (NP) in cells post-infection with H1N1 influenza virus at 48 HPI. NP-Alexa Fluor 488, green; DAPI, blue. Scale bars, 100 μm. E: RT-qPCR analysis of influenza viral M gene expression levels. F: Plaque assay measurement of infectious IAV (H1N1) virus titers (lg PFU/mL). Data are presented as mean ± standard deviation (A, E, and F); n = 3 independent cell culture experiments conducted on separate days with identical cell batches. Statistical significance was determined by one-way ANOVA followed by Tukey's multiple comparisons test. * P < 0.05, ** P < 0.01, and *** P < 0.001.

    Journal: Journal of Biomedical Research

    Article Title: Generation of ST6GAL1/ST3GAL4 double-knockout Landrace pigs with reduced respiratory sialylated glycans and decreased influenza A virus susceptibility of derived fibroblasts in vitro

    doi: 10.7555/JBR.39.20250300

    Figure Lengend Snippet: Restoration of influenza virus susceptibility in ST6GAL1 −/− / ST3GAL4 −/− Landrace pig cells through complementation. A: Quantitative reverse transcription-PCR (RT-qPCR) analysis of ST6GAL1 and ST3GAL4 gene expression levels in wild-type (WT), knockout (KO), and complemented (KO + ST) cells. B: Immunofluorescent detection of α2,6-linked and α2,3-linked sialylated glycans in wild-type (WT), knockout (KO), and complemented (KO + ST) Landrace pig cells. Red indicates SNA (α2,6) or MAL Ⅱ (α2,3) staining, and blue indicates nuclei. The KO group showed nearly undetectable signals for both SNA and MAL Ⅱ. In contrast, the WT and KO + ST groups exhibited strong fluorescence for both lectins, indicating successful restoration of both α2,6- and α2,3-linked sialylated glycans in complemented cells. Scale bars, 100 μm. C: Cytopathic effects induced by H1N1 influenza virus infection at 0, 24, and 48 h post-infection (HPI). Scale bars, 500 μm. D: Immunofluorescent detection of IAV nucleoprotein (NP) in cells post-infection with H1N1 influenza virus at 48 HPI. NP-Alexa Fluor 488, green; DAPI, blue. Scale bars, 100 μm. E: RT-qPCR analysis of influenza viral M gene expression levels. F: Plaque assay measurement of infectious IAV (H1N1) virus titers (lg PFU/mL). Data are presented as mean ± standard deviation (A, E, and F); n = 3 independent cell culture experiments conducted on separate days with identical cell batches. Statistical significance was determined by one-way ANOVA followed by Tukey's multiple comparisons test. * P < 0.05, ** P < 0.01, and *** P < 0.001.

    Article Snippet: Cells and tissues were then incubated with biotinylated lectins MAL II (1∶200, Cat. #B-1265-1, Vector Laboratories, Burlingame, CA, USA) or SNA (1∶200, Cat. #B-1305-2, Vector Laboratories) for 1 h, followed by three washes with PBS containing 0.05% Tween-20 (PBST).

    Techniques: Virus, Reverse Transcription, Quantitative RT-PCR, Analysis, Gene Expression, Knock-Out, Staining, Fluorescence, Infection, Plaque Assay, Standard Deviation, Cell Culture

    Analysis of de novo RBD expression, secretion, and intracellular TEVp-mediated cleavage in co-transfected HEK293T cells (A) Overview of the experimental set-up to analyze the total RBD-V5-His release and TEVp- c -Myc-His secretion (left side) and de novo RBD-V5-His release (right side) from co-transfected HEK293T cells. (B) Western blot analysis of the samples derived from experiment (A) by detection of V5 or c -Myc tag. (C) Western blot analysis of the secreted and residual intracellular RBD-V5-His (top) and TEVp N23Q,C130S,T173G,S219V - c -Myc-His (bottom) isolated using His-tag from 1 mL of supernatant (left lanes) or lysed co-transfected HEK293T cells from one well of a 6-well plate in 1 mL (right lanes). Cells were lysed with 1% of IGEPAL CA-630, which was also added to the supernatant. (D) Coomassie Brilliant blue-stained polyacrylamide gel quantified by comparison with a bovine serum albumin standard curve (left) and subsequent western blot probed by anti-V5 antibodies (right) of the protein released from the supernatant of co-transfected HEK293T cells obtained by co-expression of tANCHORed RBD-V5-His (top) or CD63LEL-V5-His (bottom) with or without TEVp N23Q,C130S,T173G,S219V - c -Myc-His. Highly glycosylated CD63LEL-V5-His was treated with PNGase F (peptide N-glycosidase F). (E) Lectin blot of the released RBD-V5-His protein, probed with biotinylated Sambucus nigra agglutinin (SNA) and detected using streptavidin-HRP. (F and G) Western blot analysis of the cell lysates for the expression of CD63-mCherry (F) or CD82-tANCHOR-CD63LEL-mCherry (G), with or without modified TEVp expression. Control contains untransfected cells, and TEVp was captured from the supernatant.

    Journal: iScience

    Article Title: Enzymatically controlled release of proteins and peptides: A promising, alternative secretion approach

    doi: 10.1016/j.isci.2026.115185

    Figure Lengend Snippet: Analysis of de novo RBD expression, secretion, and intracellular TEVp-mediated cleavage in co-transfected HEK293T cells (A) Overview of the experimental set-up to analyze the total RBD-V5-His release and TEVp- c -Myc-His secretion (left side) and de novo RBD-V5-His release (right side) from co-transfected HEK293T cells. (B) Western blot analysis of the samples derived from experiment (A) by detection of V5 or c -Myc tag. (C) Western blot analysis of the secreted and residual intracellular RBD-V5-His (top) and TEVp N23Q,C130S,T173G,S219V - c -Myc-His (bottom) isolated using His-tag from 1 mL of supernatant (left lanes) or lysed co-transfected HEK293T cells from one well of a 6-well plate in 1 mL (right lanes). Cells were lysed with 1% of IGEPAL CA-630, which was also added to the supernatant. (D) Coomassie Brilliant blue-stained polyacrylamide gel quantified by comparison with a bovine serum albumin standard curve (left) and subsequent western blot probed by anti-V5 antibodies (right) of the protein released from the supernatant of co-transfected HEK293T cells obtained by co-expression of tANCHORed RBD-V5-His (top) or CD63LEL-V5-His (bottom) with or without TEVp N23Q,C130S,T173G,S219V - c -Myc-His. Highly glycosylated CD63LEL-V5-His was treated with PNGase F (peptide N-glycosidase F). (E) Lectin blot of the released RBD-V5-His protein, probed with biotinylated Sambucus nigra agglutinin (SNA) and detected using streptavidin-HRP. (F and G) Western blot analysis of the cell lysates for the expression of CD63-mCherry (F) or CD82-tANCHOR-CD63LEL-mCherry (G), with or without modified TEVp expression. Control contains untransfected cells, and TEVp was captured from the supernatant.

    Article Snippet: After blocking, the membrane was washed and incubated for 2 h with biotinylated Sambucus nigra lectin (SNA, Vector Laboratories, Biozol, Hamburg, Germany) at a concentration of 5 μg/mL in 3% BSA.

    Techniques: Expressing, Transfection, Western Blot, Derivative Assay, Isolation, Staining, Comparison, Modification, Control