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  • 99
    Thermo Fisher phosphate buffered saline pbs edta
    Surface markers of amastigote-stimulated B cells. Purified human B cells were incubated or not overnight with L . infantum amastigotes at a final parasite:host cell ratio of 3:1. Cells and the cell-parasite mixture were intensively washed with a galactose-modified <t>PBS/EDTA</t> solution and stained for CD27, CD24 and CD38. Dead cells were excluded by fixable viability dye staining. Representative histograms showing CD27 (panel A), CD24 (panel B) and CD38 expression (panel C) are shown on the left while percentages of positive cells are displayed on the right portion of the panel (n = 7). Dark lines on the histograms represent the FMO controls for each sample.
    Phosphate Buffered Saline Pbs Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore edta phosphate buffered saline pbs
    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as <t>PBS-EDTA,</t> to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.
    Edta Phosphate Buffered Saline Pbs, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Lonza pbs edta
    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as <t>PBS-EDTA,</t> to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.
    Pbs Edta, supplied by Lonza, used in various techniques. Bioz Stars score: 99/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Miltenyi Biotec pbs edta
    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as <t>PBS-EDTA,</t> to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.
    Pbs Edta, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 99/100, based on 156 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Eppendorf AG edta phosphate buffered saline pbs
    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as <t>PBS-EDTA,</t> to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.
    Edta Phosphate Buffered Saline Pbs, supplied by Eppendorf AG, used in various techniques. Bioz Stars score: 79/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Corning Life Sciences edta phosphate buffered saline pbs
    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as <t>PBS-EDTA,</t> to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.
    Edta Phosphate Buffered Saline Pbs, supplied by Corning Life Sciences, used in various techniques. Bioz Stars score: 82/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Becton Dickinson edta phosphate buffered saline pbs
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Edta Phosphate Buffered Saline Pbs, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 78/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Miltenyi Biotec edta phosphate buffered saline pbs detachment buffer
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Edta Phosphate Buffered Saline Pbs Detachment Buffer, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 87/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Roche pbs edta
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Pbs Edta, supplied by Roche, used in various techniques. Bioz Stars score: 97/100, based on 128 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Difco edta pbs
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Edta Pbs, supplied by Difco, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Teknova pbs edta
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Pbs Edta, supplied by Teknova, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore d8537 edta
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    D8537 Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Miltenyi Biotec clinimacs pbs edta
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Clinimacs Pbs Edta, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 98/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher sodium azide pbs edta
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Sodium Azide Pbs Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Miltenyi Biotec pbs edta buffer
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Pbs Edta Buffer, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 96/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Merck & Co trypsin edta pbs
    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with <t>PBS/EDTA,</t> incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated
    Trypsin Edta Pbs, supplied by Merck & Co, used in various techniques. Bioz Stars score: 89/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore pbs edta buffer
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    Pbs Edta Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Miltenyi Biotec clinimacs pbs edta buffer
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    Clinimacs Pbs Edta Buffer, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 99/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Millipore edta egta pbs
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    Edta Egta Pbs, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    81
    Miltenyi Biotec gmp grade pbs edta
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    Gmp Grade Pbs Edta, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 81/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore x saline sodium phosphate edta buffer
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    X Saline Sodium Phosphate Edta Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore trypsin edta pbs
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    Trypsin Edta Pbs, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher phosphate buffered saline pbs
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    Phosphate Buffered Saline Pbs, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 27245 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher 4x saline sodium phosphate edta buffer
    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in <t>PBS</t> buffer (a, c, e) without <t>Cu–EDTA</t> and (b, d, f) with 30 mM Cu–EDTA.
    4x Saline Sodium Phosphate Edta Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Santa Cruz Biotechnology pbs edta
    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with <t>PBS/EDTA</t> or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.
    Pbs Edta, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 89/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Thermo Fisher protease free phosphate buffered saline edetic acid solution
    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with <t>PBS/EDTA</t> or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.
    Protease Free Phosphate Buffered Saline Edetic Acid Solution, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Applichem edta pbs
    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with <t>PBS/EDTA</t> or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.
    Edta Pbs, supplied by Applichem, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Nacalai edta pbs
    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with <t>PBS/EDTA</t> or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.
    Edta Pbs, supplied by Nacalai, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    GE Healthcare edta pbs
    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with <t>PBS/EDTA</t> or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.
    Edta Pbs, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 79/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    83
    Thermo Fisher saline sodium phosphate edta buffer
    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with <t>PBS/EDTA</t> or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.
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    Surface markers of amastigote-stimulated B cells. Purified human B cells were incubated or not overnight with L . infantum amastigotes at a final parasite:host cell ratio of 3:1. Cells and the cell-parasite mixture were intensively washed with a galactose-modified PBS/EDTA solution and stained for CD27, CD24 and CD38. Dead cells were excluded by fixable viability dye staining. Representative histograms showing CD27 (panel A), CD24 (panel B) and CD38 expression (panel C) are shown on the left while percentages of positive cells are displayed on the right portion of the panel (n = 7). Dark lines on the histograms represent the FMO controls for each sample.

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Leishmania infantum Amastigotes Trigger a Subpopulation of Human B Cells with an Immunoregulatory Phenotype

    doi: 10.1371/journal.pntd.0003543

    Figure Lengend Snippet: Surface markers of amastigote-stimulated B cells. Purified human B cells were incubated or not overnight with L . infantum amastigotes at a final parasite:host cell ratio of 3:1. Cells and the cell-parasite mixture were intensively washed with a galactose-modified PBS/EDTA solution and stained for CD27, CD24 and CD38. Dead cells were excluded by fixable viability dye staining. Representative histograms showing CD27 (panel A), CD24 (panel B) and CD38 expression (panel C) are shown on the left while percentages of positive cells are displayed on the right portion of the panel (n = 7). Dark lines on the histograms represent the FMO controls for each sample.

    Article Snippet: Viability of B cells was assessed by staining with the Fixable Viability Dye eFluor 780 in PBS/EDTA 2 mM, following manufacturer’s instructions (eBiosciences, San Diego, CA).

    Techniques: Purification, Incubation, Modification, Staining, Expressing

    L . infantum amastigotes activate human B cells. Purified human B cells were either left alone (used as a control) or incubated overnight with L . infantum amastigotes (AMA) at a final parasite:host cell ratio of 3:1. Cells and the cell-parasite mixture were intensively washed with a galactose-modified PBS/EDTA solution and stained with the listed antibodies. Samples were read using a BD FACSCanto flow cytometer. A) Representative histograms displaying expression of each cell surface marker studied are shown in this panel. Dark lines on the histograms represent the fluorescence minus one (FMO) control for each sample. B) Results represent mean values of samples from 5 to 7 different healthy donors and are expressed as the percentages of positive cells for the indicated cell surface marker. C) Results represent mean values of samples from 5 to 7 different healthy donors and are expressed as the mean fluorescence intensities (MFI) for the indicated cell surface marker. P values were calculated by the two-tailed Student’s t-test (ns: not significant).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Leishmania infantum Amastigotes Trigger a Subpopulation of Human B Cells with an Immunoregulatory Phenotype

    doi: 10.1371/journal.pntd.0003543

    Figure Lengend Snippet: L . infantum amastigotes activate human B cells. Purified human B cells were either left alone (used as a control) or incubated overnight with L . infantum amastigotes (AMA) at a final parasite:host cell ratio of 3:1. Cells and the cell-parasite mixture were intensively washed with a galactose-modified PBS/EDTA solution and stained with the listed antibodies. Samples were read using a BD FACSCanto flow cytometer. A) Representative histograms displaying expression of each cell surface marker studied are shown in this panel. Dark lines on the histograms represent the fluorescence minus one (FMO) control for each sample. B) Results represent mean values of samples from 5 to 7 different healthy donors and are expressed as the percentages of positive cells for the indicated cell surface marker. C) Results represent mean values of samples from 5 to 7 different healthy donors and are expressed as the mean fluorescence intensities (MFI) for the indicated cell surface marker. P values were calculated by the two-tailed Student’s t-test (ns: not significant).

    Article Snippet: Viability of B cells was assessed by staining with the Fixable Viability Dye eFluor 780 in PBS/EDTA 2 mM, following manufacturer’s instructions (eBiosciences, San Diego, CA).

    Techniques: Purification, Incubation, Modification, Staining, Flow Cytometry, Cytometry, Expressing, Marker, Fluorescence, Two Tailed Test

    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as PBS-EDTA, to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as PBS-EDTA, to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.

    Article Snippet: All samples dispersed in PBS-EDTA were 0.22 μm-filtered (Millipore) prior to column injection.

    Techniques: Concentration Assay, Buffer Exchange

    (A) Reverse phase chromatogram of AMB-PEG and unconjugated AMB, with eluted peaks detected at 406 nm. 50 μL of AMB-PEG 1 and 2, and 10 μL of unconjugated AMB dispersed in PBS-EDTA and 48% ACN respectively were injected into a C18 reverse phase column and eluted isocratically in a 48% ACN buffer at a flow rate of 0.5 ml/min for 40 minutes. Peaks were detected at 406 nm. The AMB-PEG conjugate has a shorter retention time, implying that it is more hydrophilic. From the AMB-PEG samples, AMB-PEG conjugate and free AMB (based on the retention time of unconjugated AMB) fractions were collected for further analysis via size exclusion chromatography. (B) Size exclusion chromatogram of AMB-PEG 2 and unconjugated AMB, as well as the relevant fractions collected from RPC, in a 20% ACN mobile phase. 20 mM of AMB-PEG 2 formulations and unconjugated AMB in DMSO were prepared and resuspended at 2 mM in a 20% ACN buffer. 50 μL of these samples (unconjugated AMB diluted tenfold prior to analysis) and the peak fractions collected previously from RPC were passed through a size exclusion column and eluted peaks were detected at 406 nm. Unconjugated AMB was eluted later compared to the AMB-PEG conjugate, implying that it has a smaller hydrodynamic volume compared to AMB-PEG in 20% ACN. The previously collected AMB-PEG conjugate and free AMB peak fractions had similar retention times as the AMB-PEG 2 formulation and unconjugated AMB samples respectively, thus verifying their respective peak identities. AMB-PEG 1 and 2 have identical elution profiles. (C) Size exclusion chromatogram of AMB-PEG and unconjugated AMB dispersed in PBS-EDTA. 3 μL of 2 mM AMB-PEG formulations that have been retained by 10 kDa centrifugal filters (Millipore) and 50 μL of the supernatant obtained from unconjugated AMB were analysed using a Superdex 75 size exclusion column and eluted peaks detected at 406 nm. In a PBS-EDTA mobile phase, unconjugated AMB has a shorter retention time of 20 minutes compared to AMB-PEG at 40 minutes, implying that AMB-PEG has a smaller hydrodynamic volume under these experimental conditions.

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: (A) Reverse phase chromatogram of AMB-PEG and unconjugated AMB, with eluted peaks detected at 406 nm. 50 μL of AMB-PEG 1 and 2, and 10 μL of unconjugated AMB dispersed in PBS-EDTA and 48% ACN respectively were injected into a C18 reverse phase column and eluted isocratically in a 48% ACN buffer at a flow rate of 0.5 ml/min for 40 minutes. Peaks were detected at 406 nm. The AMB-PEG conjugate has a shorter retention time, implying that it is more hydrophilic. From the AMB-PEG samples, AMB-PEG conjugate and free AMB (based on the retention time of unconjugated AMB) fractions were collected for further analysis via size exclusion chromatography. (B) Size exclusion chromatogram of AMB-PEG 2 and unconjugated AMB, as well as the relevant fractions collected from RPC, in a 20% ACN mobile phase. 20 mM of AMB-PEG 2 formulations and unconjugated AMB in DMSO were prepared and resuspended at 2 mM in a 20% ACN buffer. 50 μL of these samples (unconjugated AMB diluted tenfold prior to analysis) and the peak fractions collected previously from RPC were passed through a size exclusion column and eluted peaks were detected at 406 nm. Unconjugated AMB was eluted later compared to the AMB-PEG conjugate, implying that it has a smaller hydrodynamic volume compared to AMB-PEG in 20% ACN. The previously collected AMB-PEG conjugate and free AMB peak fractions had similar retention times as the AMB-PEG 2 formulation and unconjugated AMB samples respectively, thus verifying their respective peak identities. AMB-PEG 1 and 2 have identical elution profiles. (C) Size exclusion chromatogram of AMB-PEG and unconjugated AMB dispersed in PBS-EDTA. 3 μL of 2 mM AMB-PEG formulations that have been retained by 10 kDa centrifugal filters (Millipore) and 50 μL of the supernatant obtained from unconjugated AMB were analysed using a Superdex 75 size exclusion column and eluted peaks detected at 406 nm. In a PBS-EDTA mobile phase, unconjugated AMB has a shorter retention time of 20 minutes compared to AMB-PEG at 40 minutes, implying that AMB-PEG has a smaller hydrodynamic volume under these experimental conditions.

    Article Snippet: All samples dispersed in PBS-EDTA were 0.22 μm-filtered (Millipore) prior to column injection.

    Techniques: Injection, Flow Cytometry, Size-exclusion Chromatography

    (A) AMB-PEG reaction scheme. The NHS ester on MS(PEG) 4 reacts with the primary amine (–NH2) group on AMB at a 1:1 molar ratio, generating conjugated AMB-PEG via amide bond formation. (B) Solubility of AMB-PEG at varying AMB:PEG molar ratios. AMB-PEG mixtures and unreacted AMB were prepared in DMSO, incubated for 2 hours and then (i) dispersed to a final concentration of 2 mM in PBS-EDTA, containing 10% DMSO by volume. (ii) The mixtures were then centrifuged to facilitate the observation of insoluble precipitates. Higher molar ratios yielded a suspension of yellow particles that precipitated upon centrifugation, similar to what was observed with unconjugated AMB.

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: (A) AMB-PEG reaction scheme. The NHS ester on MS(PEG) 4 reacts with the primary amine (–NH2) group on AMB at a 1:1 molar ratio, generating conjugated AMB-PEG via amide bond formation. (B) Solubility of AMB-PEG at varying AMB:PEG molar ratios. AMB-PEG mixtures and unreacted AMB were prepared in DMSO, incubated for 2 hours and then (i) dispersed to a final concentration of 2 mM in PBS-EDTA, containing 10% DMSO by volume. (ii) The mixtures were then centrifuged to facilitate the observation of insoluble precipitates. Higher molar ratios yielded a suspension of yellow particles that precipitated upon centrifugation, similar to what was observed with unconjugated AMB.

    Article Snippet: All samples dispersed in PBS-EDTA were 0.22 μm-filtered (Millipore) prior to column injection.

    Techniques: Mass Spectrometry, Solubility, Incubation, Concentration Assay, Centrifugation

    Aqueous solubility of AMB-PEG 1 and 2. Increasing amounts of AMB-PEG formulations were added to PBS-EDTA, and post-centrifugation, the concentration of soluble AMB-PEG in the supernatants quantified based on their absorbance at 365 nm. Error bars denote the standard deviation between 3 independent formulations. Dotted line represents the theoretical condition where AMB formulation is completely soluble (i.e. concentration of total AMB = concentration of soluble AMB).

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: Aqueous solubility of AMB-PEG 1 and 2. Increasing amounts of AMB-PEG formulations were added to PBS-EDTA, and post-centrifugation, the concentration of soluble AMB-PEG in the supernatants quantified based on their absorbance at 365 nm. Error bars denote the standard deviation between 3 independent formulations. Dotted line represents the theoretical condition where AMB formulation is completely soluble (i.e. concentration of total AMB = concentration of soluble AMB).

    Article Snippet: All samples dispersed in PBS-EDTA were 0.22 μm-filtered (Millipore) prior to column injection.

    Techniques: Solubility, Centrifugation, Concentration Assay, Standard Deviation

    ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with PBS/EDTA, incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated

    Journal: Alcoholism, clinical and experimental research

    Article Title: Upregulation of Serotonin Transporter by Alcohol in Human Dendritic Cells: Possible Implication in Neuroimmune Deregulation

    doi: 10.1111/j.1530-0277.2009.01010.x

    Figure Lengend Snippet: ( A ) Flow cytometric analysis of SERT protein expression. Dendritic cells (DC) treated with 0.1% alcohol for 24 hours were harvested, washed with PBS/EDTA, incubated with mouse monoclonal antibody to SERT and stained with donkey anti-mouse IgG conjugated

    Article Snippet: After washing with PBS/EDTA, the cell pellet was resuspended in 2% paraformaldehyde and analyzed using FACSCalibur flow cytometer through CellQuest software (BD Biosciences, San Jose, CA).

    Techniques: Flow Cytometry, Expressing, Incubation, Staining

    1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in PBS buffer (a, c, e) without Cu–EDTA and (b, d, f) with 30 mM Cu–EDTA.

    Journal: The journal of physical chemistry. B

    Article Title: High-Resolution Structural Insights into Bone: A Solid-State NMR Relaxation Study Utilizing Paramagnetic Doping

    doi: 10.1021/jp307935g

    Figure Lengend Snippet: 1 H inversion recovery spectra of 13 C Ramp-CP MAS NMR experiments of (a, b) type I collagen, (c, d) cortical bone, and (e, f) demineralized bone. Samples were soaked in PBS buffer (a, c, e) without Cu–EDTA and (b, d, f) with 30 mM Cu–EDTA.

    Article Snippet: 30 mM Cu–EDTA PBS solution was prepared by dissolving Cu(II)(NH4 )2 EDTA powder (Sigma Aldrich, St. Louis, MO, USA) in standard PBS buffer.

    Techniques: Nuclear Magnetic Resonance

    Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with PBS/EDTA or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.

    Journal: Oncotarget

    Article Title: Phage display library selection of a hypoxia-binding scFv antibody for liver cancer metabolic marker discovery

    doi: 10.18632/oncotarget.9460

    Figure Lengend Snippet: Internalization and binding analysis of the H103 scFv Ab ( A ) Normoxic or hypoxicc treated HCCLM3 cells were incubated with H103 scFv Ab either in phage-display form or soluble form. After washing with PBST, the binding and uptake of the H103 scFv Ab was detected with AF488 conjugated anti-M13 (PVIII) or anti-His Abs under a confocal microscope. E4B7S scFv was used as the control. ( B ) The uptakes of the H103 scFv Ab at different time points in hypoxic HCCLM3 cells were measured by flow cytometric analysis. ( C ) After detachment with PBS/EDTA or T/E, the binding of the H103 scFv Ab on HCCLM3 cells was analyzed by flow cytometry.

    Article Snippet: After washing with PBS-glycine (50 mM), cells were PBS/EDTA detached and the lysates were depleted by incubation with either protein L (Santa Cruz) or Ni-NTA-agarose (Quiagen) for 1 h. Depleted lysates were incubated with the scFv Ab (4 ug per ml) at 4°C overnight and the immune complexes were captured by protein L or Ni-NTA agarose.

    Techniques: Binding Assay, Incubation, Microscopy, Flow Cytometry, Cytometry