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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 71 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphate buffered saline pbs edta/product/Thermo Fisher
    Average 99 stars, based on 71 article reviews
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    phosphate buffered saline pbs edta - by Bioz Stars, 2020-05
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    99
    Millipore 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 Millipore, used in various techniques. Bioz Stars score: 99/100, based on 370 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    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: 94/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Teknova 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 Teknova, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    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: 92/100, based on 156 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Miltenyi Biotec pbs edta buffer
    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 Buffer, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 88/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Miltenyi Biotec clinimacs 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.
    Clinimacs Pbs Edta, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 93/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore phosphate buffered saline 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.
    Phosphate Buffered Saline Pbs Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Miltenyi Biotec clinimacs pbs edta buffer
    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.
    Clinimacs Pbs Edta Buffer, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 88/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/clinimacs pbs edta buffer/product/Miltenyi Biotec
    Average 88 stars, based on 93 article reviews
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    88
    Miltenyi Biotec gmp grade 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.
    Gmp Grade Pbs Edta, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 88/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gmp grade pbs edta/product/Miltenyi Biotec
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    99
    Millipore pbs edta buffer
    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 Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Becton Dickinson 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 Becton Dickinson, used in various techniques. Bioz Stars score: 93/100, based on 336 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pbs edta/product/Becton Dickinson
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    91
    Eppendorf AG 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 Eppendorf AG, used in various techniques. Bioz Stars score: 91/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    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: 92/100, based on 127 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Thermo Fisher trypsin 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
    Trypsin Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 38677 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    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: 92/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    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

    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