canavalia ensiformis Search Results


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  • 99
    Millipore concanavalin a
    Absence of Ags1 alters the cell wall structure and composition and causes a lack of cell wall in the pole lateral region, which leads to lysis and cytoplasm release. (A) Ags1 depletion promotes general cell wall ultrastructure alterations, thicker and uniformly transparent in the absence (top-right panels) or multilayered in the presence of sorbitol (bottom-right panels). Cells were grown in EMM+T for 3 (−S, top panels) or 9 h (+S, bottom panels) and analyzed by transmission electron microscopy (TEM). ICW: internal cell wall layer. Bar, 1 µm. (B) Absence of Ags1 generates a reduction in the outer layer of mannoproteins. hht1 + - RFP (WT, RFP nuclei) and 81X- ags1 + (no RFP nuclei) cells were grown in EMM+T for 3 h, mixed, and visualized for <t>FITC-concanavalin</t> A (mannoproteins) and RFP fluorescence (nuclei, WT cells). FITC fluorescence (mannoproteins amount) was quantified by using arbitrary units (see Materials and methods). Bar, 5 µm. (C) Ags1 depletion causes irregular walls with cavities (open arrowhead) and/or attached sister wall fragments (closed arrowhead) at the pole side region. Cells were analyzed by TEM as in A. Bars, 1 µm. (D) Ags1 depletion promotes lysis and cytoplasm release from the pole side region. Cells were grown as in A. Arrowhead: lateral region of cell lysis. Elapsed time is shown in seconds. The percentage of lateral lysis was quantified. Bars, 5 µm.
    Concanavalin A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 14628 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore canavalia ensiformis
    Absence of Ags1 alters the cell wall structure and composition and causes a lack of cell wall in the pole lateral region, which leads to lysis and cytoplasm release. (A) Ags1 depletion promotes general cell wall ultrastructure alterations, thicker and uniformly transparent in the absence (top-right panels) or multilayered in the presence of sorbitol (bottom-right panels). Cells were grown in EMM+T for 3 (−S, top panels) or 9 h (+S, bottom panels) and analyzed by transmission electron microscopy (TEM). ICW: internal cell wall layer. Bar, 1 µm. (B) Absence of Ags1 generates a reduction in the outer layer of mannoproteins. hht1 + - RFP (WT, RFP nuclei) and 81X- ags1 + (no RFP nuclei) cells were grown in EMM+T for 3 h, mixed, and visualized for <t>FITC-concanavalin</t> A (mannoproteins) and RFP fluorescence (nuclei, WT cells). FITC fluorescence (mannoproteins amount) was quantified by using arbitrary units (see Materials and methods). Bar, 5 µm. (C) Ags1 depletion causes irregular walls with cavities (open arrowhead) and/or attached sister wall fragments (closed arrowhead) at the pole side region. Cells were analyzed by TEM as in A. Bars, 1 µm. (D) Ags1 depletion promotes lysis and cytoplasm release from the pole side region. Cells were grown as in A. Arrowhead: lateral region of cell lysis. Elapsed time is shown in seconds. The percentage of lateral lysis was quantified. Bars, 5 µm.
    Canavalia Ensiformis, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 384 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    canavalia ensiformis - by Bioz Stars, 2021-01
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    95
    Millipore α mannosidase
    SDS-PAGE analysis of the purified recombinant β-glucosidase Bgl3A with and without deglycosylation treatment. a Coomassie Blue staining. Lanes M, the standard protein molecular weight markers; 1 the Bgl3A produced in P. pastoris ; 2 the Bgl3A produced in P. pastoris and treated with PNGase F; 3 the Bgl3A produced in P. pastoris and treated with PNGase F followed by <t>α-mannosidase;</t> 4 the α-mannosidase; 5 the purified Bgl3A after sequential deglycosylation by PNGase F and α-mannosidase; 6 the Bgl3A produced in E. coli . b Periodic Acid-Schiff staining
    α Mannosidase, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 260 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore β n acetylglucosaminidase
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    β N Acetylglucosaminidase, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 125 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    EY Laboratories canavalia ensiformis
    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N <t>-acetylglucosaminidase</t> (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.
    Canavalia Ensiformis, supplied by EY Laboratories, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 91 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    canavalia ensiformis - by Bioz Stars, 2021-01
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    Image Search Results


    Absence of Ags1 alters the cell wall structure and composition and causes a lack of cell wall in the pole lateral region, which leads to lysis and cytoplasm release. (A) Ags1 depletion promotes general cell wall ultrastructure alterations, thicker and uniformly transparent in the absence (top-right panels) or multilayered in the presence of sorbitol (bottom-right panels). Cells were grown in EMM+T for 3 (−S, top panels) or 9 h (+S, bottom panels) and analyzed by transmission electron microscopy (TEM). ICW: internal cell wall layer. Bar, 1 µm. (B) Absence of Ags1 generates a reduction in the outer layer of mannoproteins. hht1 + - RFP (WT, RFP nuclei) and 81X- ags1 + (no RFP nuclei) cells were grown in EMM+T for 3 h, mixed, and visualized for FITC-concanavalin A (mannoproteins) and RFP fluorescence (nuclei, WT cells). FITC fluorescence (mannoproteins amount) was quantified by using arbitrary units (see Materials and methods). Bar, 5 µm. (C) Ags1 depletion causes irregular walls with cavities (open arrowhead) and/or attached sister wall fragments (closed arrowhead) at the pole side region. Cells were analyzed by TEM as in A. Bars, 1 µm. (D) Ags1 depletion promotes lysis and cytoplasm release from the pole side region. Cells were grown as in A. Arrowhead: lateral region of cell lysis. Elapsed time is shown in seconds. The percentage of lateral lysis was quantified. Bars, 5 µm.

    Journal: The Journal of Cell Biology

    Article Title: Fission yeast Ags1 confers the essential septum strength needed for safe gradual cell abscission

    doi: 10.1083/jcb.201202015

    Figure Lengend Snippet: Absence of Ags1 alters the cell wall structure and composition and causes a lack of cell wall in the pole lateral region, which leads to lysis and cytoplasm release. (A) Ags1 depletion promotes general cell wall ultrastructure alterations, thicker and uniformly transparent in the absence (top-right panels) or multilayered in the presence of sorbitol (bottom-right panels). Cells were grown in EMM+T for 3 (−S, top panels) or 9 h (+S, bottom panels) and analyzed by transmission electron microscopy (TEM). ICW: internal cell wall layer. Bar, 1 µm. (B) Absence of Ags1 generates a reduction in the outer layer of mannoproteins. hht1 + - RFP (WT, RFP nuclei) and 81X- ags1 + (no RFP nuclei) cells were grown in EMM+T for 3 h, mixed, and visualized for FITC-concanavalin A (mannoproteins) and RFP fluorescence (nuclei, WT cells). FITC fluorescence (mannoproteins amount) was quantified by using arbitrary units (see Materials and methods). Bar, 5 µm. (C) Ags1 depletion causes irregular walls with cavities (open arrowhead) and/or attached sister wall fragments (closed arrowhead) at the pole side region. Cells were analyzed by TEM as in A. Bars, 1 µm. (D) Ags1 depletion promotes lysis and cytoplasm release from the pole side region. Cells were grown as in A. Arrowhead: lateral region of cell lysis. Elapsed time is shown in seconds. The percentage of lateral lysis was quantified. Bars, 5 µm.

    Article Snippet: For FITC-conjugated concanavalin A staining, equal amounts of log-phasehht1 + -RFP (control wild type, nucleus labeling) and 81X-ags1 + cells were mixed, washed with PBS (3,000 g for 1 min), suspended in 0.5 ml PBS containing 100 µg/ml FITC-conjugated concanavalin A (C7642; Sigma-Aldrich), and incubated at 28°C for 20 min in the dark.

    Techniques: Lysis, Transmission Assay, Electron Microscopy, Transmission Electron Microscopy, Fluorescence

    ADAM12 expression is upregulated in claudin-low breast cancer cells and in subpopulations enriched for CSCs. a . Cell surface expression of ADAM12 protein in breast cancer cell lines was evaluated by flow cytometry. Red, anti-ADAM12 antibody staining; gray, isotype control antibody staining. b Total cellular expression of ADAM12 was analyzed by Western blotting after partial purification of ADAM12 on concanavalin A (conA) agarose, as described [ 42 ]. GAPDH in the input fractions shows comparable conA agarose loading for all cells. Arrow, the nascent full length ADAM12; arrowhead, the processed form lacking the N-terminal pro-domain. c CSC signature score versus ADAM12 mRNA expression in 51 breast cancer cell lines. The CSC signature scores were calculated based on ref. [ 22 ] and microarray expression data retrieved from GEO:GSE69017, as described in Methods. Cell lines analyzed in panels a and b are shown in red. d ADAM12 protein levels in total lysates of SUM159PT cells grown as attached monolayers or as mammospheres, analyzed by Western blotting. Arrow, the nascent full length ADAM12; arrowhead, the processed form lacking the N-terminal pro-domain; *, a non-specific band. Positive control represents ADAM12 after partial purification on conA agarose. e Cell surface expression of ADAM12 in SUM159PT cells treated for 6 days with DMSO (control) or with 10 nM paclitaxel (PTX), and then allowed to recover for 6 days without PTX, was examined by flow cytometry. The population of cells with the highest expression of ADAM12 is shown in red. FSC, forward scatter

    Journal: Molecular Cancer

    Article Title: Metalloprotease-disintegrin ADAM12 actively promotes the stem cell-like phenotype in claudin-low breast cancer

    doi: 10.1186/s12943-017-0599-6

    Figure Lengend Snippet: ADAM12 expression is upregulated in claudin-low breast cancer cells and in subpopulations enriched for CSCs. a . Cell surface expression of ADAM12 protein in breast cancer cell lines was evaluated by flow cytometry. Red, anti-ADAM12 antibody staining; gray, isotype control antibody staining. b Total cellular expression of ADAM12 was analyzed by Western blotting after partial purification of ADAM12 on concanavalin A (conA) agarose, as described [ 42 ]. GAPDH in the input fractions shows comparable conA agarose loading for all cells. Arrow, the nascent full length ADAM12; arrowhead, the processed form lacking the N-terminal pro-domain. c CSC signature score versus ADAM12 mRNA expression in 51 breast cancer cell lines. The CSC signature scores were calculated based on ref. [ 22 ] and microarray expression data retrieved from GEO:GSE69017, as described in Methods. Cell lines analyzed in panels a and b are shown in red. d ADAM12 protein levels in total lysates of SUM159PT cells grown as attached monolayers or as mammospheres, analyzed by Western blotting. Arrow, the nascent full length ADAM12; arrowhead, the processed form lacking the N-terminal pro-domain; *, a non-specific band. Positive control represents ADAM12 after partial purification on conA agarose. e Cell surface expression of ADAM12 in SUM159PT cells treated for 6 days with DMSO (control) or with 10 nM paclitaxel (PTX), and then allowed to recover for 6 days without PTX, was examined by flow cytometry. The population of cells with the highest expression of ADAM12 is shown in red. FSC, forward scatter

    Article Snippet: Total cell lysates were directly analyzed by Western blotting or incubated with concanavalin A agarose (Sigma; 50 μl resin per 1 ml cell lysate) for 2 h at 4 °C to enrich for glycoproteins.

    Techniques: Expressing, Flow Cytometry, Cytometry, Staining, Western Blot, Purification, Microarray, Positive Control

    SDS-PAGE analysis of the purified recombinant β-glucosidase Bgl3A with and without deglycosylation treatment. a Coomassie Blue staining. Lanes M, the standard protein molecular weight markers; 1 the Bgl3A produced in P. pastoris ; 2 the Bgl3A produced in P. pastoris and treated with PNGase F; 3 the Bgl3A produced in P. pastoris and treated with PNGase F followed by α-mannosidase; 4 the α-mannosidase; 5 the purified Bgl3A after sequential deglycosylation by PNGase F and α-mannosidase; 6 the Bgl3A produced in E. coli . b Periodic Acid-Schiff staining

    Journal: Biotechnology for Biofuels

    Article Title: Engineering a highly active thermophilic β-glucosidase to enhance its pH stability and saccharification performance

    doi: 10.1186/s13068-016-0560-8

    Figure Lengend Snippet: SDS-PAGE analysis of the purified recombinant β-glucosidase Bgl3A with and without deglycosylation treatment. a Coomassie Blue staining. Lanes M, the standard protein molecular weight markers; 1 the Bgl3A produced in P. pastoris ; 2 the Bgl3A produced in P. pastoris and treated with PNGase F; 3 the Bgl3A produced in P. pastoris and treated with PNGase F followed by α-mannosidase; 4 the α-mannosidase; 5 the purified Bgl3A after sequential deglycosylation by PNGase F and α-mannosidase; 6 the Bgl3A produced in E. coli . b Periodic Acid-Schiff staining

    Article Snippet: To remove O -glycans, 4 ml of PNGase F-treated Bgl3A was incubated with 10 µl of α-mannosidase (M7257, Sigma-Aldrich) for 24 h, followed by purification through anion exchange chromatography.

    Techniques: SDS Page, Purification, Recombinant, Staining, Molecular Weight, Produced

    Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N -acetylglucosaminidase (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.

    Journal: PLoS ONE

    Article Title: Chemical Characterization of N-Linked Oligosaccharide As the Antigen Epitope Recognized by an Anti-Sperm Auto-Monoclonal Antibody, Ts4

    doi: 10.1371/journal.pone.0133784

    Figure Lengend Snippet: Western blot analysis of the testicular TS fraction after endo- or exo-glycosidase digestion. Aliquots containing 20 μg of testicular TS extract were digested with various kinds of endo- or exoglycosidase. After the reaction mixture was incubated for 24 h at 37°C, 5 μg of proteins was applied to each lane of the 10% SDS-PAGE gel under reducing conditions and then was probed with the Ts4 mAb (upper panel) or the 6035 mAb (lower panel). Lane 1: N -glycanase (0.1 unit/ml), lane 2: endoglycosidase F1 (0.1 unit/ml), lane 3: endoglycosidase F2 (0.05 unit/ml), lane 4: endoglycosidase F3 (0.05 unit/ml), lane 5: endoglycosidase H (0.05 unit/ml), lane 6: in absent of endoglycosidase, lane 7: α-mannosidase (7 unit/ml), lane 8: β-mannosidase (0.03 unit/ml), lane 9: β- N -acetylglucosaminidase (2 unit/ml), lane 10: neuraminidase (0.16 unit/ml), lane 11: α-L-fucosidase (0.6 unit/ml), lane 12: in absent of exoglycosidase.

    Article Snippet: On the other hand, the immunoreactivity of Ts4 against TEX101 was completely abrogated by pre-treating with β-N -acetylglucosaminidase from Canavalia ensiformis (Sigma-Aldrich) ( , lane 9 in upper panel). β-N -acetylglucosaminidase is a highly specific exoglycosidase that catalyzes the hydrolysis of terminal non-reducing GlcNAc residues [ ].

    Techniques: Western Blot, Incubation, SDS Page