fluorescein conjugated lectins  (Vector Laboratories)


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    Structured Review

    Vector Laboratories fluorescein conjugated lectins
    RCA I and tomato lectin blots of sVSG and sVSG-depleted cell lysate. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two-allele deleted clonal cell lines (A6 and B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blots, which were detected with biotinylated RCA I lectin ( A ) or tomato lectin ( B ), with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each <t>lectins</t> and subsequently reacted with HRP-conjugated streptavidin. C and D, the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western analyses. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.
    Fluorescein Conjugated Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein conjugated lectins/product/Vector Laboratories
    Average 94 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    fluorescein conjugated lectins - by Bioz Stars, 2022-10
    94/100 stars

    Images

    1) Product Images from "Inhibition of Nucleotide Sugar Transport in Trypanosoma brucei Alters Surface Glycosylation *"

    Article Title: Inhibition of Nucleotide Sugar Transport in Trypanosoma brucei Alters Surface Glycosylation *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M113.453597

    RCA I and tomato lectin blots of sVSG and sVSG-depleted cell lysate. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two-allele deleted clonal cell lines (A6 and B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blots, which were detected with biotinylated RCA I lectin ( A ) or tomato lectin ( B ), with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each lectins and subsequently reacted with HRP-conjugated streptavidin. C and D, the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western analyses. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.
    Figure Legend Snippet: RCA I and tomato lectin blots of sVSG and sVSG-depleted cell lysate. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two-allele deleted clonal cell lines (A6 and B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blots, which were detected with biotinylated RCA I lectin ( A ) or tomato lectin ( B ), with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each lectins and subsequently reacted with HRP-conjugated streptavidin. C and D, the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western analyses. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.

    Techniques Used: Isolation, SDS Page, Western Blot

    KO of tbnst4 causes defects in LacNAc- N -glycosylation. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two dKO clonal cell lines (A6 an d B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blotting, which was detected with biotinylated ECL ( A ) or ConA ( B ) lectins with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each of lectins and subsequently, reacted with HRP-conjugated streptavidin. C and D , the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western blotting. ECL ( C ) and Con A ( D ) blots are indicated. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.
    Figure Legend Snippet: KO of tbnst4 causes defects in LacNAc- N -glycosylation. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two dKO clonal cell lines (A6 an d B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blotting, which was detected with biotinylated ECL ( A ) or ConA ( B ) lectins with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each of lectins and subsequently, reacted with HRP-conjugated streptavidin. C and D , the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western blotting. ECL ( C ) and Con A ( D ) blots are indicated. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.

    Techniques Used: Isolation, SDS Page, Western Blot

    Deletion of the TbNST4 gene reduces surface lectin binding. Flow cytometric analysis of lectins bound to the surface of BSF T. brucei . ∼1 × 10 6 live cells of WT and two dKO clonal cell lines (A6 and B1) were incubated with FITC-conjugated lectins: ECL ( A ), RCA I ( B ), TL (tomato) ( C ), and ConA ( D ) at 4 °C for 0.5 h. Cells were analyzed with flow cytometry and histograms were generated with FlowJo 9.5.2 software. WT ( blue ), dKO-A6 ( green ), dKO-B1 ( yellow ), and unstained control cells ( red ) are indicated.
    Figure Legend Snippet: Deletion of the TbNST4 gene reduces surface lectin binding. Flow cytometric analysis of lectins bound to the surface of BSF T. brucei . ∼1 × 10 6 live cells of WT and two dKO clonal cell lines (A6 and B1) were incubated with FITC-conjugated lectins: ECL ( A ), RCA I ( B ), TL (tomato) ( C ), and ConA ( D ) at 4 °C for 0.5 h. Cells were analyzed with flow cytometry and histograms were generated with FlowJo 9.5.2 software. WT ( blue ), dKO-A6 ( green ), dKO-B1 ( yellow ), and unstained control cells ( red ) are indicated.

    Techniques Used: Binding Assay, Flow Cytometry, Incubation, Cytometry, Generated, Software

    2) Product Images from "Divergent Golgi Trafficking Limits B cell-Mediated IgG Sialylation"

    Article Title: Divergent Golgi Trafficking Limits B cell-Mediated IgG Sialylation

    Journal: bioRxiv

    doi: 10.1101/2022.01.25.477787

    Hybridoma IgG have limited α2,6 sialylation and abundant core fucose. (A) ELISA of hybridoma IgG samples compared to bovine fetuin at a range of target protein concentrations and using a panel of lectins, including ConA (mannose), LCA (core fucose), PHA-E (bisecting GlcNAc), PHA-L (β1,6 branching), and SNA (α2,6 sialylation). N = 3. (B) Comparison of 100 ng each IgG subclass and fetuin based on the lectin:ConA ratio to normalize to total N-glycan. N = 3 for LCA, PHA-E, and PHA-L. N = 14 for IgG SNA and N = 9 for fetuin SNA. (C) Multiplexed Western blot of IgG subclasses using SNA and antimurine Fc antibody. All error bars show SEM.
    Figure Legend Snippet: Hybridoma IgG have limited α2,6 sialylation and abundant core fucose. (A) ELISA of hybridoma IgG samples compared to bovine fetuin at a range of target protein concentrations and using a panel of lectins, including ConA (mannose), LCA (core fucose), PHA-E (bisecting GlcNAc), PHA-L (β1,6 branching), and SNA (α2,6 sialylation). N = 3. (B) Comparison of 100 ng each IgG subclass and fetuin based on the lectin:ConA ratio to normalize to total N-glycan. N = 3 for LCA, PHA-E, and PHA-L. N = 14 for IgG SNA and N = 9 for fetuin SNA. (C) Multiplexed Western blot of IgG subclasses using SNA and antimurine Fc antibody. All error bars show SEM.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    IgG poorly localizes to intracellular regions rich in α2,6 sialylation. (A) Hybridoma cells stained with a panel of lectins (green) and anti-IgG antibody (red) shown as individual channels and color overlay to illustrate colocalization (yellow). Two representative images for each lectin are shown. (B-D) Quantitation of colocalization between lectin-staining and IgG across many images for each hybridoma cell line, as indicated. N = 10-25. All error bars show SEM. **** P
    Figure Legend Snippet: IgG poorly localizes to intracellular regions rich in α2,6 sialylation. (A) Hybridoma cells stained with a panel of lectins (green) and anti-IgG antibody (red) shown as individual channels and color overlay to illustrate colocalization (yellow). Two representative images for each lectin are shown. (B-D) Quantitation of colocalization between lectin-staining and IgG across many images for each hybridoma cell line, as indicated. N = 10-25. All error bars show SEM. **** P

    Techniques Used: Staining, Quantitation Assay

    Hybridoma IgG glycans can be sialylated but differ from B cell surface glycans. (A) Hybridoma IgG subclasses were treated with recombinant ST6Gal1 and analyzed for the addition of sialic acid by SNA and ConA ELISA and expressed as a percent increase over the input IgG. N = 3-6. (B) Hybridoma ST6Gal1 mRNA level relative to β2 microglobulin transcript, as measured by quantitative PCR. N = 3. (C) SNA and ConA ELISA of whole cell extracts compared to IgG from each corresponding hybridoma cell line. N = 6 for each IgG; N = 21 for each whole cell extract. (D) Lectin:ConA ratios of the mean fluorescence intensities of each hybridoma cell line using a panel of lectins and flow cytometry. N = 3. (E) Raw flow cytometry histograms for each cell line and lectin used. N = 3. All error bars show SEM.
    Figure Legend Snippet: Hybridoma IgG glycans can be sialylated but differ from B cell surface glycans. (A) Hybridoma IgG subclasses were treated with recombinant ST6Gal1 and analyzed for the addition of sialic acid by SNA and ConA ELISA and expressed as a percent increase over the input IgG. N = 3-6. (B) Hybridoma ST6Gal1 mRNA level relative to β2 microglobulin transcript, as measured by quantitative PCR. N = 3. (C) SNA and ConA ELISA of whole cell extracts compared to IgG from each corresponding hybridoma cell line. N = 6 for each IgG; N = 21 for each whole cell extract. (D) Lectin:ConA ratios of the mean fluorescence intensities of each hybridoma cell line using a panel of lectins and flow cytometry. N = 3. (E) Raw flow cytometry histograms for each cell line and lectin used. N = 3. All error bars show SEM.

    Techniques Used: Recombinant, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Fluorescence, Flow Cytometry

    3) Product Images from "Divergent Golgi Trafficking Limits B cell-Mediated IgG Sialylation"

    Article Title: Divergent Golgi Trafficking Limits B cell-Mediated IgG Sialylation

    Journal: bioRxiv

    doi: 10.1101/2022.01.25.477787

    Hybridoma IgG have limited α2,6 sialylation and abundant core fucose. (A) ELISA of hybridoma IgG samples compared to bovine fetuin at a range of target protein concentrations and using a panel of lectins, including ConA (mannose), LCA (core fucose), PHA-E (bisecting GlcNAc), PHA-L (β1,6 branching), and SNA (α2,6 sialylation). N = 3. (B) Comparison of 100 ng each IgG subclass and fetuin based on the lectin:ConA ratio to normalize to total N-glycan. N = 3 for LCA, PHA-E, and PHA-L. N = 14 for IgG SNA and N = 9 for fetuin SNA. (C) Multiplexed Western blot of IgG subclasses using SNA and antimurine Fc antibody. All error bars show SEM.
    Figure Legend Snippet: Hybridoma IgG have limited α2,6 sialylation and abundant core fucose. (A) ELISA of hybridoma IgG samples compared to bovine fetuin at a range of target protein concentrations and using a panel of lectins, including ConA (mannose), LCA (core fucose), PHA-E (bisecting GlcNAc), PHA-L (β1,6 branching), and SNA (α2,6 sialylation). N = 3. (B) Comparison of 100 ng each IgG subclass and fetuin based on the lectin:ConA ratio to normalize to total N-glycan. N = 3 for LCA, PHA-E, and PHA-L. N = 14 for IgG SNA and N = 9 for fetuin SNA. (C) Multiplexed Western blot of IgG subclasses using SNA and antimurine Fc antibody. All error bars show SEM.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Western Blot

    IgG poorly localizes to intracellular regions rich in α2,6 sialylation. (A) Hybridoma cells stained with a panel of lectins (green) and anti-IgG antibody (red) shown as individual channels and color overlay to illustrate colocalization (yellow). Two representative images for each lectin are shown. (B-D) Quantitation of colocalization between lectin-staining and IgG across many images for each hybridoma cell line, as indicated. N = 10-25. All error bars show SEM. **** P
    Figure Legend Snippet: IgG poorly localizes to intracellular regions rich in α2,6 sialylation. (A) Hybridoma cells stained with a panel of lectins (green) and anti-IgG antibody (red) shown as individual channels and color overlay to illustrate colocalization (yellow). Two representative images for each lectin are shown. (B-D) Quantitation of colocalization between lectin-staining and IgG across many images for each hybridoma cell line, as indicated. N = 10-25. All error bars show SEM. **** P

    Techniques Used: Staining, Quantitation Assay

    Hybridoma IgG glycans can be sialylated but differ from B cell surface glycans. (A) Hybridoma IgG subclasses were treated with recombinant ST6Gal1 and analyzed for the addition of sialic acid by SNA and ConA ELISA and expressed as a percent increase over the input IgG. N = 3-6. (B) Hybridoma ST6Gal1 mRNA level relative to β2 microglobulin transcript, as measured by quantitative PCR. N = 3. (C) SNA and ConA ELISA of whole cell extracts compared to IgG from each corresponding hybridoma cell line. N = 6 for each IgG; N = 21 for each whole cell extract. (D) Lectin:ConA ratios of the mean fluorescence intensities of each hybridoma cell line using a panel of lectins and flow cytometry. N = 3. (E) Raw flow cytometry histograms for each cell line and lectin used. N = 3. All error bars show SEM.
    Figure Legend Snippet: Hybridoma IgG glycans can be sialylated but differ from B cell surface glycans. (A) Hybridoma IgG subclasses were treated with recombinant ST6Gal1 and analyzed for the addition of sialic acid by SNA and ConA ELISA and expressed as a percent increase over the input IgG. N = 3-6. (B) Hybridoma ST6Gal1 mRNA level relative to β2 microglobulin transcript, as measured by quantitative PCR. N = 3. (C) SNA and ConA ELISA of whole cell extracts compared to IgG from each corresponding hybridoma cell line. N = 6 for each IgG; N = 21 for each whole cell extract. (D) Lectin:ConA ratios of the mean fluorescence intensities of each hybridoma cell line using a panel of lectins and flow cytometry. N = 3. (E) Raw flow cytometry histograms for each cell line and lectin used. N = 3. All error bars show SEM.

    Techniques Used: Recombinant, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Fluorescence, Flow Cytometry

    4) Product Images from "PNA lectin for purifying mouse acinar cells from the inflamed pancreas"

    Article Title: PNA lectin for purifying mouse acinar cells from the inflamed pancreas

    Journal: Scientific Reports

    doi: 10.1038/srep21127

    Two lectins appear to have specific affinity for acinar cells in the mouse pancreas. ( a,b ) C57/BL6 mouse pancreas was labeled with 2 specific lectins (UEA-I, a; and PNA, ( b ), and counterstained with synaptophysin (SYN), CD31, and DBA. ( c ) The PNA lectin was pre-treated with 200 mmol/l galactose for 15 minutes and then used to label C57/BL6 mouse pancreas prior to staining with SYN and CD31. Scale bars are 50 μm.
    Figure Legend Snippet: Two lectins appear to have specific affinity for acinar cells in the mouse pancreas. ( a,b ) C57/BL6 mouse pancreas was labeled with 2 specific lectins (UEA-I, a; and PNA, ( b ), and counterstained with synaptophysin (SYN), CD31, and DBA. ( c ) The PNA lectin was pre-treated with 200 mmol/l galactose for 15 minutes and then used to label C57/BL6 mouse pancreas prior to staining with SYN and CD31. Scale bars are 50 μm.

    Techniques Used: Labeling, Staining

    5) Product Images from "Human Organotypic Airway and Lung Organoid Cells of Bronchiolar and Alveolar Differentiation Are Permissive to Infection by Influenza and SARS-CoV-2 Respiratory Virus"

    Article Title: Human Organotypic Airway and Lung Organoid Cells of Bronchiolar and Alveolar Differentiation Are Permissive to Infection by Influenza and SARS-CoV-2 Respiratory Virus

    Journal: Frontiers in Cellular and Infection Microbiology

    doi: 10.3389/fcimb.2022.841447

    Detection of essential influenza virus receptors entry factors in organoids and infection by influenza pseudotype H5N1 and viral replication by H7N1 virus. (A) Sialic acids (SAs) of cell surface glycoproteins and glycolipids are the receptors for influenza virus. The presence of SAs and galactose on bronchiolar (BRON, left histograms) and alveolar (ALV, right histograms) were detected by flow cytometry using the fluorescein-conjugated lectins, MAL I, recognizing galactose, and SNA, recognizing α 2,6-linked sialic acids. CTRL histogram represents the unstained control cells. The representative flow cytometry histograms shown here were from stained dissociated organoids from patient L2. (B) In situ detection of cells infected by the pseudotyped luciferase expressing H5N1 influenza virus was done by immunostaining to detect luciferase (LUC) and keratin 5 (KRT5) in formalin fixed paraffin embedded (FFPE) sections of infected organoids. Organoids of BRON (upper panel) and ALV (lower panel) organoid cultures are shown. Sections are counterstained with DAPI. Scale bar in all images equals 100 µm. (C) Organoids were infected with the replicating influenza virus H7N1 strain at an estimated multiplicity of infection (MOI) of 7. Plaque assay was used to confirm efficient replication of pseudotyped influenza virus in the organoid cultures. Infected MDCK cells were used as a positive control in this assay. Plaques are visible in MDCK cell cultures inoculated with conditioned media harvested from infected bronchiolar and alveolar organoid cultures, as well as conditioned media harvested from the positive control MDCK cells. Conditioned media from uninfected controls showed no sign of plaque formation (lower row). Counterstaining by crystal violet. Magnification equals 4x.
    Figure Legend Snippet: Detection of essential influenza virus receptors entry factors in organoids and infection by influenza pseudotype H5N1 and viral replication by H7N1 virus. (A) Sialic acids (SAs) of cell surface glycoproteins and glycolipids are the receptors for influenza virus. The presence of SAs and galactose on bronchiolar (BRON, left histograms) and alveolar (ALV, right histograms) were detected by flow cytometry using the fluorescein-conjugated lectins, MAL I, recognizing galactose, and SNA, recognizing α 2,6-linked sialic acids. CTRL histogram represents the unstained control cells. The representative flow cytometry histograms shown here were from stained dissociated organoids from patient L2. (B) In situ detection of cells infected by the pseudotyped luciferase expressing H5N1 influenza virus was done by immunostaining to detect luciferase (LUC) and keratin 5 (KRT5) in formalin fixed paraffin embedded (FFPE) sections of infected organoids. Organoids of BRON (upper panel) and ALV (lower panel) organoid cultures are shown. Sections are counterstained with DAPI. Scale bar in all images equals 100 µm. (C) Organoids were infected with the replicating influenza virus H7N1 strain at an estimated multiplicity of infection (MOI) of 7. Plaque assay was used to confirm efficient replication of pseudotyped influenza virus in the organoid cultures. Infected MDCK cells were used as a positive control in this assay. Plaques are visible in MDCK cell cultures inoculated with conditioned media harvested from infected bronchiolar and alveolar organoid cultures, as well as conditioned media harvested from the positive control MDCK cells. Conditioned media from uninfected controls showed no sign of plaque formation (lower row). Counterstaining by crystal violet. Magnification equals 4x.

    Techniques Used: Infection, Flow Cytometry, Staining, In Situ, Luciferase, Expressing, Immunostaining, Formalin-fixed Paraffin-Embedded, Plaque Assay, Positive Control

    6) Product Images from "N-glycome and N-glycoproteome of a hematophagous parasitic nematode Haemonchus"

    Article Title: N-glycome and N-glycoproteome of a hematophagous parasitic nematode Haemonchus

    Journal: Computational and Structural Biotechnology Journal

    doi: 10.1016/j.csbj.2021.04.038

    Anatomical distribution of glycoconjugates in Haemonchus contortus . Paraffin-embedded sections of the adult female (A) and male (B) worms were probed with fluorescein-labeled lectins, as indicated (green). Nuclei were stained by DAPI (blue). Major tissues are outlined. Images shown here represent three independent assays. (C) The intensity of fluorescence signals from lectin-stained images in panel A-B . Graphs show the mean fluorescence intensity, as quantified using the ImageJ program (NIH, USA). Abbreviations: ic, intestinal cytoplasm; mv, microvilli; int, intestine; ov, ovaries; gn, male gonad; cg, cement gland; cu, cuticle (outer). Scale bars: 50 µm. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: Anatomical distribution of glycoconjugates in Haemonchus contortus . Paraffin-embedded sections of the adult female (A) and male (B) worms were probed with fluorescein-labeled lectins, as indicated (green). Nuclei were stained by DAPI (blue). Major tissues are outlined. Images shown here represent three independent assays. (C) The intensity of fluorescence signals from lectin-stained images in panel A-B . Graphs show the mean fluorescence intensity, as quantified using the ImageJ program (NIH, USA). Abbreviations: ic, intestinal cytoplasm; mv, microvilli; int, intestine; ov, ovaries; gn, male gonad; cg, cement gland; cu, cuticle (outer). Scale bars: 50 µm. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Labeling, Staining, Fluorescence

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    Vector Laboratories fitc conjugated sambucus nigra sna lectin
    Mass spectrometry analysis of <t>SNA-binding</t> proteins isolated from DCs reveals key immune-related proteins. ( A ) The reactivity of <t>Sambucus</t> <t>nigra</t> (SNA) <t>lectin</t> to α2,6-sialylated glycans on the surface of human DCs was quantified by flow cytometry after different maturation stimuli: IFN-γ, IL-1β, TNF-α and LPS. Unstimulated DCs were used as control. Values presented are mean ± SEM (N = 6). Statistically significant differences are indicated by asterisks (* p ≤ 0.05). ( B ) Schematic representation of the steps followed to identify α2,6-sialylated proteins from DCs. Whole cell lysates of human DCs were immunoprecipitated through a SNA-binding column. The eluted proteins were analyzed by mass spectrometry and the corresponding identified scores were matched and associated with Gene Ontology (GO) entries. ( C ) Distribution of the identified sialylated proteins by their molecular function. Pie chart represents different molecular functions of the identified proteins, according to the GO entries. Immune system processes were highlighted.
    Fitc Conjugated Sambucus Nigra Sna Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fitc conjugated sambucus nigra sna lectin/product/Vector Laboratories
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fitc conjugated sambucus nigra sna lectin - by Bioz Stars, 2022-10
    96/100 stars
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    94
    Vector Laboratories fluorescein isothiocyanate conjugated tomato lectin
    Histologic specimens of 4T1 and 67NR tumors. Tumor blood vessels were visualized by immunocytochemistry for VEGFR2 ( A , B , E , and F ) and by intravital labeling with fluorescein <t>isothiocyanate—conjugated</t> endothelium-binding tomato <t>lectin</t> ( C , D ,
    Fluorescein Isothiocyanate Conjugated Tomato Lectin, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein isothiocyanate conjugated tomato lectin/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fluorescein isothiocyanate conjugated tomato lectin - by Bioz Stars, 2022-10
    94/100 stars
      Buy from Supplier

    94
    Vector Laboratories fluorescein conjugated lectins
    RCA I and tomato lectin blots of sVSG and sVSG-depleted cell lysate. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two-allele deleted clonal cell lines (A6 and B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blots, which were detected with biotinylated RCA I lectin ( A ) or tomato lectin ( B ), with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each <t>lectins</t> and subsequently reacted with HRP-conjugated streptavidin. C and D, the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western analyses. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.
    Fluorescein Conjugated Lectins, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein conjugated lectins/product/Vector Laboratories
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    fluorescein conjugated lectins - by Bioz Stars, 2022-10
    94/100 stars
      Buy from Supplier

    95
    Vector Laboratories fluorescein labeled peanut agglutinin pna
    Glycans present within the acinar cells of SMGs. Immunofluorescent staining of 8-week WT female ( A ) and male ( B ) SMGs with the lectin <t>MAA</t> ( green ), which detects α2,3-linked sialic acid on O - and N -linked glycans. Samples were either untreated ( No NM ) or treated with neuraminidase ( NM ), which removes sialic acid to show specificity. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 20 μm. Shown is immunofluorescent staining of 8-week WT female ( C ) and male ( D ) SMGs with the lectin <t>PNA</t> ( green ), which detects the nonsialylated core 1 O -glycan Galβ1,3GalNAc. Samples were either untreated ( No NM ) or treated with neuraminidase ( NM ). No PNA staining is seen in untreated female SMGs, whereas PNA staining is seen in both treated and untreated male SMGs. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 10 μm. Shown are western blots of WT female ( E ) and male ( F ) SMG extracts either untreated (−) or treated with NM (+) and probed with PNA. Molecular mass markers (kDa) are shown to the left of each blot.
    Fluorescein Labeled Peanut Agglutinin Pna, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fluorescein labeled peanut agglutinin pna/product/Vector Laboratories
    Average 95 stars, based on 1 article reviews
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    Mass spectrometry analysis of SNA-binding proteins isolated from DCs reveals key immune-related proteins. ( A ) The reactivity of Sambucus nigra (SNA) lectin to α2,6-sialylated glycans on the surface of human DCs was quantified by flow cytometry after different maturation stimuli: IFN-γ, IL-1β, TNF-α and LPS. Unstimulated DCs were used as control. Values presented are mean ± SEM (N = 6). Statistically significant differences are indicated by asterisks (* p ≤ 0.05). ( B ) Schematic representation of the steps followed to identify α2,6-sialylated proteins from DCs. Whole cell lysates of human DCs were immunoprecipitated through a SNA-binding column. The eluted proteins were analyzed by mass spectrometry and the corresponding identified scores were matched and associated with Gene Ontology (GO) entries. ( C ) Distribution of the identified sialylated proteins by their molecular function. Pie chart represents different molecular functions of the identified proteins, according to the GO entries. Immune system processes were highlighted.

    Journal: Pharmaceutics

    Article Title: MHC Class I Stability is Modulated by Cell Surface Sialylation in Human Dendritic Cells

    doi: 10.3390/pharmaceutics12030249

    Figure Lengend Snippet: Mass spectrometry analysis of SNA-binding proteins isolated from DCs reveals key immune-related proteins. ( A ) The reactivity of Sambucus nigra (SNA) lectin to α2,6-sialylated glycans on the surface of human DCs was quantified by flow cytometry after different maturation stimuli: IFN-γ, IL-1β, TNF-α and LPS. Unstimulated DCs were used as control. Values presented are mean ± SEM (N = 6). Statistically significant differences are indicated by asterisks (* p ≤ 0.05). ( B ) Schematic representation of the steps followed to identify α2,6-sialylated proteins from DCs. Whole cell lysates of human DCs were immunoprecipitated through a SNA-binding column. The eluted proteins were analyzed by mass spectrometry and the corresponding identified scores were matched and associated with Gene Ontology (GO) entries. ( C ) Distribution of the identified sialylated proteins by their molecular function. Pie chart represents different molecular functions of the identified proteins, according to the GO entries. Immune system processes were highlighted.

    Article Snippet: For flow cytometry analysis, we also stained cells with FITC-conjugated Sambucus nigra (SNA) lectin (Vector Labs) and the fluorescently FITC-labeled peptides NLVPKFITCVATV and SIINFEKFITCL (Genecust).

    Techniques: Mass Spectrometry, Binding Assay, Isolation, Flow Cytometry, Immunoprecipitation

    Histologic specimens of 4T1 and 67NR tumors. Tumor blood vessels were visualized by immunocytochemistry for VEGFR2 ( A , B , E , and F ) and by intravital labeling with fluorescein isothiocyanate—conjugated endothelium-binding tomato lectin ( C , D ,

    Journal:

    Article Title: Molecular Imaging of Vascular Endothelial Growth Factor Receptor 2 Expression Using Targeted Contrast-Enhanced High-Frequency Ultrasonography

    doi:

    Figure Lengend Snippet: Histologic specimens of 4T1 and 67NR tumors. Tumor blood vessels were visualized by immunocytochemistry for VEGFR2 ( A , B , E , and F ) and by intravital labeling with fluorescein isothiocyanate—conjugated endothelium-binding tomato lectin ( C , D ,

    Article Snippet: To assess the function of tumor vasculature, fluorescein isothiocyanate—conjugated tomato lectin ( Lycopersicon esculentum , 1 mg/mL; Vector Laboratories, Inc, Burlingame, CA) was injected into the jugular vein (0.1 mL/mouse) 24 hours after ultrasonography.

    Techniques: Immunocytochemistry, Labeling, Binding Assay

    RCA I and tomato lectin blots of sVSG and sVSG-depleted cell lysate. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two-allele deleted clonal cell lines (A6 and B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blots, which were detected with biotinylated RCA I lectin ( A ) or tomato lectin ( B ), with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each lectins and subsequently reacted with HRP-conjugated streptavidin. C and D, the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western analyses. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.

    Journal: The Journal of Biological Chemistry

    Article Title: Inhibition of Nucleotide Sugar Transport in Trypanosoma brucei Alters Surface Glycosylation *

    doi: 10.1074/jbc.M113.453597

    Figure Lengend Snippet: RCA I and tomato lectin blots of sVSG and sVSG-depleted cell lysate. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two-allele deleted clonal cell lines (A6 and B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blots, which were detected with biotinylated RCA I lectin ( A ) or tomato lectin ( B ), with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each lectins and subsequently reacted with HRP-conjugated streptavidin. C and D, the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western analyses. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.

    Article Snippet: Cells were incubated with mouse anti-EP-FITC (10 μg/ml) (Cedarlane, USA), or fluorescein-conjugated lectins: Erythrina cristagalli (ECL) (20 μg/ml), Concanavalin A (ConA) (10 μg/ml), Ricinus communis agglutinin I (RCA I) (20 μg/ml), and Lycopersicon esculentum , tomato lectin (TL, 20 μg/ml) (Vector Laboratories), in 3% BSA in PBS at 4 °C for 0.5 h. After washing with 0.3% BSA in PBS, cells were resuspended in 350 μl of PBS and analyzed in a flow cytometer (BD Biosciences FACScan) using detector FL1 (530 ± 30 nm).

    Techniques: Isolation, SDS Page, Western Blot

    KO of tbnst4 causes defects in LacNAc- N -glycosylation. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two dKO clonal cell lines (A6 an d B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blotting, which was detected with biotinylated ECL ( A ) or ConA ( B ) lectins with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each of lectins and subsequently, reacted with HRP-conjugated streptavidin. C and D , the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western blotting. ECL ( C ) and Con A ( D ) blots are indicated. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.

    Journal: The Journal of Biological Chemistry

    Article Title: Inhibition of Nucleotide Sugar Transport in Trypanosoma brucei Alters Surface Glycosylation *

    doi: 10.1074/jbc.M113.453597

    Figure Lengend Snippet: KO of tbnst4 causes defects in LacNAc- N -glycosylation. A and B, isolated sVSG from WT ( lanes 1 and 4 ) and two dKO clonal cell lines (A6 an d B1, lanes 2 and 3 or 5 and 6 ) were separated by SDS-PAGE and subjected to Western blotting, which was detected with biotinylated ECL ( A ) or ConA ( B ) lectins with ( right panels ) or without ( left panels ) the corresponding sugar inhibitors for each of lectins and subsequently, reacted with HRP-conjugated streptavidin. C and D , the same procedure as A and B was applied except that sVSG-depleted cell lysates were used for Western blotting. ECL ( C ) and Con A ( D ) blots are indicated. 1 × 10 6 and 7 × 10 6 cell equivalents per lane were loaded for sVSG and sVSG-depleted cell lysates, respectively. VSG was used as loading controls.

    Article Snippet: Cells were incubated with mouse anti-EP-FITC (10 μg/ml) (Cedarlane, USA), or fluorescein-conjugated lectins: Erythrina cristagalli (ECL) (20 μg/ml), Concanavalin A (ConA) (10 μg/ml), Ricinus communis agglutinin I (RCA I) (20 μg/ml), and Lycopersicon esculentum , tomato lectin (TL, 20 μg/ml) (Vector Laboratories), in 3% BSA in PBS at 4 °C for 0.5 h. After washing with 0.3% BSA in PBS, cells were resuspended in 350 μl of PBS and analyzed in a flow cytometer (BD Biosciences FACScan) using detector FL1 (530 ± 30 nm).

    Techniques: Isolation, SDS Page, Western Blot

    Deletion of the TbNST4 gene reduces surface lectin binding. Flow cytometric analysis of lectins bound to the surface of BSF T. brucei . ∼1 × 10 6 live cells of WT and two dKO clonal cell lines (A6 and B1) were incubated with FITC-conjugated lectins: ECL ( A ), RCA I ( B ), TL (tomato) ( C ), and ConA ( D ) at 4 °C for 0.5 h. Cells were analyzed with flow cytometry and histograms were generated with FlowJo 9.5.2 software. WT ( blue ), dKO-A6 ( green ), dKO-B1 ( yellow ), and unstained control cells ( red ) are indicated.

    Journal: The Journal of Biological Chemistry

    Article Title: Inhibition of Nucleotide Sugar Transport in Trypanosoma brucei Alters Surface Glycosylation *

    doi: 10.1074/jbc.M113.453597

    Figure Lengend Snippet: Deletion of the TbNST4 gene reduces surface lectin binding. Flow cytometric analysis of lectins bound to the surface of BSF T. brucei . ∼1 × 10 6 live cells of WT and two dKO clonal cell lines (A6 and B1) were incubated with FITC-conjugated lectins: ECL ( A ), RCA I ( B ), TL (tomato) ( C ), and ConA ( D ) at 4 °C for 0.5 h. Cells were analyzed with flow cytometry and histograms were generated with FlowJo 9.5.2 software. WT ( blue ), dKO-A6 ( green ), dKO-B1 ( yellow ), and unstained control cells ( red ) are indicated.

    Article Snippet: Cells were incubated with mouse anti-EP-FITC (10 μg/ml) (Cedarlane, USA), or fluorescein-conjugated lectins: Erythrina cristagalli (ECL) (20 μg/ml), Concanavalin A (ConA) (10 μg/ml), Ricinus communis agglutinin I (RCA I) (20 μg/ml), and Lycopersicon esculentum , tomato lectin (TL, 20 μg/ml) (Vector Laboratories), in 3% BSA in PBS at 4 °C for 0.5 h. After washing with 0.3% BSA in PBS, cells were resuspended in 350 μl of PBS and analyzed in a flow cytometer (BD Biosciences FACScan) using detector FL1 (530 ± 30 nm).

    Techniques: Binding Assay, Flow Cytometry, Incubation, Cytometry, Generated, Software

    Glycans present within the acinar cells of SMGs. Immunofluorescent staining of 8-week WT female ( A ) and male ( B ) SMGs with the lectin MAA ( green ), which detects α2,3-linked sialic acid on O - and N -linked glycans. Samples were either untreated ( No NM ) or treated with neuraminidase ( NM ), which removes sialic acid to show specificity. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 20 μm. Shown is immunofluorescent staining of 8-week WT female ( C ) and male ( D ) SMGs with the lectin PNA ( green ), which detects the nonsialylated core 1 O -glycan Galβ1,3GalNAc. Samples were either untreated ( No NM ) or treated with neuraminidase ( NM ). No PNA staining is seen in untreated female SMGs, whereas PNA staining is seen in both treated and untreated male SMGs. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 10 μm. Shown are western blots of WT female ( E ) and male ( F ) SMG extracts either untreated (−) or treated with NM (+) and probed with PNA. Molecular mass markers (kDa) are shown to the left of each blot.

    Journal: The Journal of Biological Chemistry

    Article Title: Loss of the disease-associated glycosyltransferase Galnt3 alters Muc10 glycosylation and the composition of the oral microbiome

    doi: 10.1074/jbc.RA119.009807

    Figure Lengend Snippet: Glycans present within the acinar cells of SMGs. Immunofluorescent staining of 8-week WT female ( A ) and male ( B ) SMGs with the lectin MAA ( green ), which detects α2,3-linked sialic acid on O - and N -linked glycans. Samples were either untreated ( No NM ) or treated with neuraminidase ( NM ), which removes sialic acid to show specificity. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 20 μm. Shown is immunofluorescent staining of 8-week WT female ( C ) and male ( D ) SMGs with the lectin PNA ( green ), which detects the nonsialylated core 1 O -glycan Galβ1,3GalNAc. Samples were either untreated ( No NM ) or treated with neuraminidase ( NM ). No PNA staining is seen in untreated female SMGs, whereas PNA staining is seen in both treated and untreated male SMGs. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 10 μm. Shown are western blots of WT female ( E ) and male ( F ) SMG extracts either untreated (−) or treated with NM (+) and probed with PNA. Molecular mass markers (kDa) are shown to the left of each blot.

    Article Snippet: After washing, sections were incubated for 1.5 h at room temperature with either TRITC-conjugated MAA (EY Laboratories #R-7801-2; 1:100) or FITC-conjugated PNA (Vector Laboratories #FL-1071; 1:200), CyTM 3-conjugated anti-goat IgG (Jackson ImmunoResearch; 1:400), and Alexa Fluor 647®-conjugated anti-rat IgG (Jackson ImmunoResearch; 1:400).

    Techniques: Staining, Marker, Western Blot

    Loss of Galnt3 results in diminished O-glycans in male acinar cells. Immunofluorescent staining of 8-week WT and Galnt3 −/− male ( A ) and female ( B ) SMGs with the lectin MAA ( green ), which detects α2,3-linked sialic acid on O - and N -linked glycans. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 10 μm. C , immunofluorescent staining of 8-week male SMGs shows a dramatic reduction in O -glycans (detected by PNA, red ) specifically in the acinar cells (detected by acinar-1, cyan ) of Galnt3 −/− SMGs as compared with WT. D , immunofluorescent staining of neuraminidase-treated 8-week female SMGs reveals no obvious differences in PNA-reactive O -glycans between WT and Galnt3 −/− SMGs. Nuclear staining is shown in blue. Scale bars , 20 μm.

    Journal: The Journal of Biological Chemistry

    Article Title: Loss of the disease-associated glycosyltransferase Galnt3 alters Muc10 glycosylation and the composition of the oral microbiome

    doi: 10.1074/jbc.RA119.009807

    Figure Lengend Snippet: Loss of Galnt3 results in diminished O-glycans in male acinar cells. Immunofluorescent staining of 8-week WT and Galnt3 −/− male ( A ) and female ( B ) SMGs with the lectin MAA ( green ), which detects α2,3-linked sialic acid on O - and N -linked glycans. Acinar cells are shown with the marker acinar-1 ( red ). Nuclei are shown in blue. Scale bars , 10 μm. C , immunofluorescent staining of 8-week male SMGs shows a dramatic reduction in O -glycans (detected by PNA, red ) specifically in the acinar cells (detected by acinar-1, cyan ) of Galnt3 −/− SMGs as compared with WT. D , immunofluorescent staining of neuraminidase-treated 8-week female SMGs reveals no obvious differences in PNA-reactive O -glycans between WT and Galnt3 −/− SMGs. Nuclear staining is shown in blue. Scale bars , 20 μm.

    Article Snippet: After washing, sections were incubated for 1.5 h at room temperature with either TRITC-conjugated MAA (EY Laboratories #R-7801-2; 1:100) or FITC-conjugated PNA (Vector Laboratories #FL-1071; 1:200), CyTM 3-conjugated anti-goat IgG (Jackson ImmunoResearch; 1:400), and Alexa Fluor 647®-conjugated anti-rat IgG (Jackson ImmunoResearch; 1:400).

    Techniques: Staining, Marker