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Nacalai bsa
Virucidal activities of <t>MGDG</t> and sodium hypochlorite (NaClO) against FCV in the presence of bovine serum albumin <t>(BSA).</t> FCV (2 × 10 5 PFU/mL) was mixed with an equal volume of 0 and 100 μg/mL MGDG or NaClO in the presence of 0%, 2%, and 5% BSA and incubated for the indicated time at 37 °C. Results are expressed as the percentages of residual infectivity of MGDG-treated virus compared to the residual infectivity of the mock-treated virus control. Data are the means from independent duplicate assays.
Bsa, supplied by Nacalai, used in various techniques. Bioz Stars score: 88/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Images

1) Product Images from "Virucidal and Immunostimulating Activities of Monogalactosyl Diacylglyceride from Coccomyxa sp. KJ, a Green Microalga, against Murine Norovirus and Feline Calicivirus"

Article Title: Virucidal and Immunostimulating Activities of Monogalactosyl Diacylglyceride from Coccomyxa sp. KJ, a Green Microalga, against Murine Norovirus and Feline Calicivirus

Journal: Marine Drugs

doi: 10.3390/md20020131

Virucidal activities of MGDG and sodium hypochlorite (NaClO) against FCV in the presence of bovine serum albumin (BSA). FCV (2 × 10 5 PFU/mL) was mixed with an equal volume of 0 and 100 μg/mL MGDG or NaClO in the presence of 0%, 2%, and 5% BSA and incubated for the indicated time at 37 °C. Results are expressed as the percentages of residual infectivity of MGDG-treated virus compared to the residual infectivity of the mock-treated virus control. Data are the means from independent duplicate assays.
Figure Legend Snippet: Virucidal activities of MGDG and sodium hypochlorite (NaClO) against FCV in the presence of bovine serum albumin (BSA). FCV (2 × 10 5 PFU/mL) was mixed with an equal volume of 0 and 100 μg/mL MGDG or NaClO in the presence of 0%, 2%, and 5% BSA and incubated for the indicated time at 37 °C. Results are expressed as the percentages of residual infectivity of MGDG-treated virus compared to the residual infectivity of the mock-treated virus control. Data are the means from independent duplicate assays.

Techniques Used: Incubation, Infection

2) Product Images from "Significant role of host sialylated glycans in the infection and spread of severe acute respiratory syndrome coronavirus 2"

Article Title: Significant role of host sialylated glycans in the infection and spread of severe acute respiratory syndrome coronavirus 2

Journal: PLoS Pathogens

doi: 10.1371/journal.ppat.1010590

α2-6-linked sialosides interacted with S1 subunit of SARS-CoV-2 spike protein. (A) The attachment of compound-pretreated virus to cells. SARS-CoV-2 particles were pretreated with the compounds at 37°C for 60 min, then the free compounds were removed by ultrafiltration. The prepared viruses were treated to VeroE6/TMPRSS2 cells in the absence of compounds at 4°C for 30 min to examine virus-cell attachment. (B) The viral attachment to compound-pretreated cells. The indicated compounds were treated to VeroE6/TMPRSS2 cells at 37°C for 30 min and were then washed out extensively. The prepared cells were incubated with SARS-CoV-2 in the absence of compounds at 4°C for 30 min to examine virus-cell attachment. (A, B) Anti-ACE2 antibody, 100 μg/ml; heparin, 10 U/ml; α2-6SLN-lipo-PGA, 10 μM. (C) Schematic representation of glycan array. Glycan tip immobilized with sialylglycopeptides on a slide glass was incubated with recombinant SARS-CoV-2 S1 at room temperature for 1 h, and then the fluorescence signal was detected. Anti-SARS-CoV-2 S1 antibody was used as primary antibody, and Cy3-conjugated anti-rabbit IgG was used as secondary antibody. (D) The fluorescent response of the glycan array due to the interaction between recombinant SARS-CoV-2 S1 (aa 16–685, Sino Biological) and indicated protein or glycans. The amount of glycan on the neoglycoproteins were 10.8 mol (α2-6-SGP), 10.5 mol (α2-3-SGP) and 10.8 mol (asialo-SGP) of glycan per 1 mol of BSA. The dashed line indicates the nonspecific response level derived from negative control asialo-SGP. Asialo-SGP, 0.7 mg/ml; α2-3-SGP, 0.1 and 1 mg/ml; α2-6-SGP, 0.1 and 1 mg/ml; recombinant ACE2, 0.1 mg/ml.
Figure Legend Snippet: α2-6-linked sialosides interacted with S1 subunit of SARS-CoV-2 spike protein. (A) The attachment of compound-pretreated virus to cells. SARS-CoV-2 particles were pretreated with the compounds at 37°C for 60 min, then the free compounds were removed by ultrafiltration. The prepared viruses were treated to VeroE6/TMPRSS2 cells in the absence of compounds at 4°C for 30 min to examine virus-cell attachment. (B) The viral attachment to compound-pretreated cells. The indicated compounds were treated to VeroE6/TMPRSS2 cells at 37°C for 30 min and were then washed out extensively. The prepared cells were incubated with SARS-CoV-2 in the absence of compounds at 4°C for 30 min to examine virus-cell attachment. (A, B) Anti-ACE2 antibody, 100 μg/ml; heparin, 10 U/ml; α2-6SLN-lipo-PGA, 10 μM. (C) Schematic representation of glycan array. Glycan tip immobilized with sialylglycopeptides on a slide glass was incubated with recombinant SARS-CoV-2 S1 at room temperature for 1 h, and then the fluorescence signal was detected. Anti-SARS-CoV-2 S1 antibody was used as primary antibody, and Cy3-conjugated anti-rabbit IgG was used as secondary antibody. (D) The fluorescent response of the glycan array due to the interaction between recombinant SARS-CoV-2 S1 (aa 16–685, Sino Biological) and indicated protein or glycans. The amount of glycan on the neoglycoproteins were 10.8 mol (α2-6-SGP), 10.5 mol (α2-3-SGP) and 10.8 mol (asialo-SGP) of glycan per 1 mol of BSA. The dashed line indicates the nonspecific response level derived from negative control asialo-SGP. Asialo-SGP, 0.7 mg/ml; α2-3-SGP, 0.1 and 1 mg/ml; α2-6-SGP, 0.1 and 1 mg/ml; recombinant ACE2, 0.1 mg/ml.

Techniques Used: Cell Attachment Assay, Incubation, Recombinant, Fluorescence, Derivative Assay, Negative Control

3) Product Images from "Universal glass-forming behavior of in vitro and living cytoplasm"

Article Title: Universal glass-forming behavior of in vitro and living cytoplasm

Journal: Scientific Reports

doi: 10.1038/s41598-017-14883-y

Diffusion in living cytoplasm and in vitro cytoplasm measured by FRAP. ( a ) Fluorescent images of GFP-labeled living spheroplasts of E. coli before, immediately after ( t = 0 s), and 10 s after photobleaching. The photobleached region in a metabolically inactive spheroplast remained dark even at 10 s after photobleaching (lower panels), whereas the dark region was obscured already at t = 0 in normal spheroplasts (upper panels) because of rapid transport. ( b ) Inverse of diffusion coefficients D of GFP in IVCEs/liposomes (open triangles), IVCEs/emulsions (filled triangles) and BSA/liposomes (circles) measured with FRAP. These data were normalized to the value in water as D w / D . The broken and solid curves indicate η / η w in IVCEs and BSA solutions which are measured by PMR (same lines with that in Fig. 1 ), respectively. D w / D of GFP in normal (white bar) and metabolically inactive spheroplast cells (black bar) are also shown.
Figure Legend Snippet: Diffusion in living cytoplasm and in vitro cytoplasm measured by FRAP. ( a ) Fluorescent images of GFP-labeled living spheroplasts of E. coli before, immediately after ( t = 0 s), and 10 s after photobleaching. The photobleached region in a metabolically inactive spheroplast remained dark even at 10 s after photobleaching (lower panels), whereas the dark region was obscured already at t = 0 in normal spheroplasts (upper panels) because of rapid transport. ( b ) Inverse of diffusion coefficients D of GFP in IVCEs/liposomes (open triangles), IVCEs/emulsions (filled triangles) and BSA/liposomes (circles) measured with FRAP. These data were normalized to the value in water as D w / D . The broken and solid curves indicate η / η w in IVCEs and BSA solutions which are measured by PMR (same lines with that in Fig. 1 ), respectively. D w / D of GFP in normal (white bar) and metabolically inactive spheroplast cells (black bar) are also shown.

Techniques Used: Diffusion-based Assay, In Vitro, Labeling, Metabolic Labelling

4) Product Images from "Reliable and sensitive detection of glycosaminoglycan chains with immunoblots"

Article Title: Reliable and sensitive detection of glycosaminoglycan chains with immunoblots

Journal: Glycobiology

doi: 10.1093/glycob/cwaa060

Optimization of Immunoblot with CS-56 with a rapid method. ( A ) Amount of antigen required for CS-56 immunoblot. Different amounts of brain lysates obtained from 7-week-old mice prepared in SDS were separated and transferred to a PVDF membrane, followed by blocking with 10% skim milk in PBS-T for 22 h. CS-56 was diluted (1:5000) with 10% CGS-1 containing skim milk solution and incubated with PVDF membrane for 30 min with CDR method. ( B ) Incubation time required for CS-56 immunoblot. Brain lysates (10 μg/lane) prepared in SDS were separated and transferred to PVDF membrane, followed by blocking with 10% skim milk in PBS-T for 22 h at 4°C with agitation. (1) Traditional incubation (2 h) and CDR incubation for (2) 2 h, (3) 30 min and (4) 10 min were performed with CS-56 (1:5000 dilution with 10% CGS-1 containing skim milk solution). The membranes were imaged as a single image and dotted lines indicate the border of individual membranes. L, brain lysates; M, protein marker. ( C ) Effect of diluent for CS-56. Brain lysates (10 μg/lane) prepared in SDS were subjected to CS-56 immunoblot with CDR method. CS-56 was diluted (1:5000) in (1) 2.8 mL of 10% GCS-1 containing 0.2 mL of 5% skim milk in PBS-T, (2) 2.8 mL of 10% GCS-1 containing 0.2 mL of 5% gelatin from cold water fish in PBS-T, (3) 3 mL of 10% CGS-1 and (4) 3 mL of 100% CGS-1. The membranes were imaged as a single image and dotted lines indicate the border of individual membranes. L, brain lysates; M, protein marker. ( D ) Effect of blocking solution. Brain lysates (10 μg/lane) prepared in SDS were separated and transferred to a PVDF membrane. Membranes were blocked for 22 h at 4°C with agitation with (1) 10% skim milk in PBS-T, (2) 5% BSA in PBS-T, (3) PVDF Blocking Reagent for Can Get Signal, and (4) 5% gelatin from cold water fish in PBS-T. Immunoblot was performed as A. The membranes were imaged as a single image and dotted lines indicate the border of individual membranes. L, brain lysates; M, protein marker.
Figure Legend Snippet: Optimization of Immunoblot with CS-56 with a rapid method. ( A ) Amount of antigen required for CS-56 immunoblot. Different amounts of brain lysates obtained from 7-week-old mice prepared in SDS were separated and transferred to a PVDF membrane, followed by blocking with 10% skim milk in PBS-T for 22 h. CS-56 was diluted (1:5000) with 10% CGS-1 containing skim milk solution and incubated with PVDF membrane for 30 min with CDR method. ( B ) Incubation time required for CS-56 immunoblot. Brain lysates (10 μg/lane) prepared in SDS were separated and transferred to PVDF membrane, followed by blocking with 10% skim milk in PBS-T for 22 h at 4°C with agitation. (1) Traditional incubation (2 h) and CDR incubation for (2) 2 h, (3) 30 min and (4) 10 min were performed with CS-56 (1:5000 dilution with 10% CGS-1 containing skim milk solution). The membranes were imaged as a single image and dotted lines indicate the border of individual membranes. L, brain lysates; M, protein marker. ( C ) Effect of diluent for CS-56. Brain lysates (10 μg/lane) prepared in SDS were subjected to CS-56 immunoblot with CDR method. CS-56 was diluted (1:5000) in (1) 2.8 mL of 10% GCS-1 containing 0.2 mL of 5% skim milk in PBS-T, (2) 2.8 mL of 10% GCS-1 containing 0.2 mL of 5% gelatin from cold water fish in PBS-T, (3) 3 mL of 10% CGS-1 and (4) 3 mL of 100% CGS-1. The membranes were imaged as a single image and dotted lines indicate the border of individual membranes. L, brain lysates; M, protein marker. ( D ) Effect of blocking solution. Brain lysates (10 μg/lane) prepared in SDS were separated and transferred to a PVDF membrane. Membranes were blocked for 22 h at 4°C with agitation with (1) 10% skim milk in PBS-T, (2) 5% BSA in PBS-T, (3) PVDF Blocking Reagent for Can Get Signal, and (4) 5% gelatin from cold water fish in PBS-T. Immunoblot was performed as A. The membranes were imaged as a single image and dotted lines indicate the border of individual membranes. L, brain lysates; M, protein marker.

Techniques Used: Mouse Assay, Blocking Assay, Incubation, Marker, Fluorescence In Situ Hybridization

5) Product Images from "The Increased Expression of Integrin ?6 (ITGA6) Enhances Drug Resistance in EVI1high Leukemia"

Article Title: The Increased Expression of Integrin ?6 (ITGA6) Enhances Drug Resistance in EVI1high Leukemia

Journal: PLoS ONE

doi: 10.1371/journal.pone.0030706

Higher cell adhesion ability in AML cell lines with EVI1 high expression. A . The expression of four integrin genes (ITGB1, ITGB4, ITGA4 and ITGA6), EVI1 and b-actin as a control was determined by semiquantitative RT-PCR in three different EVI1 low and EVI1 high AML cell lines and two primary AML cells lines with high EVI1 expression (PT9 and PT11). B . Six AML cell lines with low or high EVI1expression, as indicated in the figure, were incubated in culture medium on BSA, collagen, fibronectin, laminin or matrigel-coated plates; the percentage of the total number of incubated cells that adhered to the plates was designated as the binding activity (%). Each experiment was performed in triplicate, and the experiments were independently repeated at least three times. The data are given the as the mean ± standard error (S.E). The statistical analysis was performed using the Student's t-test (* p
Figure Legend Snippet: Higher cell adhesion ability in AML cell lines with EVI1 high expression. A . The expression of four integrin genes (ITGB1, ITGB4, ITGA4 and ITGA6), EVI1 and b-actin as a control was determined by semiquantitative RT-PCR in three different EVI1 low and EVI1 high AML cell lines and two primary AML cells lines with high EVI1 expression (PT9 and PT11). B . Six AML cell lines with low or high EVI1expression, as indicated in the figure, were incubated in culture medium on BSA, collagen, fibronectin, laminin or matrigel-coated plates; the percentage of the total number of incubated cells that adhered to the plates was designated as the binding activity (%). Each experiment was performed in triplicate, and the experiments were independently repeated at least three times. The data are given the as the mean ± standard error (S.E). The statistical analysis was performed using the Student's t-test (* p

Techniques Used: Expressing, Reverse Transcription Polymerase Chain Reaction, Incubation, Binding Assay, Activity Assay

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    Nacalai bsa
    Virucidal activities of <t>MGDG</t> and sodium hypochlorite (NaClO) against FCV in the presence of bovine serum albumin <t>(BSA).</t> FCV (2 × 10 5 PFU/mL) was mixed with an equal volume of 0 and 100 μg/mL MGDG or NaClO in the presence of 0%, 2%, and 5% BSA and incubated for the indicated time at 37 °C. Results are expressed as the percentages of residual infectivity of MGDG-treated virus compared to the residual infectivity of the mock-treated virus control. Data are the means from independent duplicate assays.
    Bsa, supplied by Nacalai, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bsa/product/Nacalai
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    bsa - by Bioz Stars, 2022-10
    88/100 stars
      Buy from Supplier

    80
    Nacalai aqueous solution of bsa
    Treatment of <t>SG/BSA</t> dispersions at 37 °C with solutions containing different concentrations of NaClO (0.22 wt%, 0.45 wt%, 1.13 wt%, 2.26 wt%, and 4.52 wt%). ( A ) Changes in the amount of SG-CNTs during treatment, estimated from the absorbance at 700 nm. Curves were fitted using the formula Y = Y 0 + A 1 e −x/t1 + A 2 e −x/t2 (Origin software). ( B ) The degradation half-life time of SG-CNTs. SG/BSA is a <t>CNT-dispersion</t> that was obtained by dispersing SG-CNTs in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).
    Aqueous Solution Of Bsa, supplied by Nacalai, used in various techniques. Bioz Stars score: 80/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/aqueous solution of bsa/product/Nacalai
    Average 80 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    aqueous solution of bsa - by Bioz Stars, 2022-10
    80/100 stars
      Buy from Supplier

    92
    Nacalai serum albumin bsa
    Characteristics of large-diameter carbon nanotubes (Ld-CNTs) and small-diameter carbon nanotubes (Sd-CNTs). Transmission electron microscopy (TEM) images of Ld-CNTs (a), Sd-CNTs (b), and dispersions of Ld-CNTs (c) and Sd-CNTs (d) in <t>BSA.</t>
    Serum Albumin Bsa, supplied by Nacalai, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/serum albumin bsa/product/Nacalai
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    serum albumin bsa - by Bioz Stars, 2022-10
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    Virucidal activities of MGDG and sodium hypochlorite (NaClO) against FCV in the presence of bovine serum albumin (BSA). FCV (2 × 10 5 PFU/mL) was mixed with an equal volume of 0 and 100 μg/mL MGDG or NaClO in the presence of 0%, 2%, and 5% BSA and incubated for the indicated time at 37 °C. Results are expressed as the percentages of residual infectivity of MGDG-treated virus compared to the residual infectivity of the mock-treated virus control. Data are the means from independent duplicate assays.

    Journal: Marine Drugs

    Article Title: Virucidal and Immunostimulating Activities of Monogalactosyl Diacylglyceride from Coccomyxa sp. KJ, a Green Microalga, against Murine Norovirus and Feline Calicivirus

    doi: 10.3390/md20020131

    Figure Lengend Snippet: Virucidal activities of MGDG and sodium hypochlorite (NaClO) against FCV in the presence of bovine serum albumin (BSA). FCV (2 × 10 5 PFU/mL) was mixed with an equal volume of 0 and 100 μg/mL MGDG or NaClO in the presence of 0%, 2%, and 5% BSA and incubated for the indicated time at 37 °C. Results are expressed as the percentages of residual infectivity of MGDG-treated virus compared to the residual infectivity of the mock-treated virus control. Data are the means from independent duplicate assays.

    Article Snippet: The virucidal effects of MGDG on FCV were examined in the presence of an organic substance, BSA (Nacalai Tesque), and compared with those of NaClO, which is frequently used as a disinfectant.

    Techniques: Incubation, Infection

    Higher cell adhesion ability in AML cell lines with EVI1 high expression. A . The expression of four integrin genes (ITGB1, ITGB4, ITGA4 and ITGA6), EVI1 and b-actin as a control was determined by semiquantitative RT-PCR in three different EVI1 low and EVI1 high AML cell lines and two primary AML cells lines with high EVI1 expression (PT9 and PT11). B . Six AML cell lines with low or high EVI1expression, as indicated in the figure, were incubated in culture medium on BSA, collagen, fibronectin, laminin or matrigel-coated plates; the percentage of the total number of incubated cells that adhered to the plates was designated as the binding activity (%). Each experiment was performed in triplicate, and the experiments were independently repeated at least three times. The data are given the as the mean ± standard error (S.E). The statistical analysis was performed using the Student's t-test (* p

    Journal: PLoS ONE

    Article Title: The Increased Expression of Integrin ?6 (ITGA6) Enhances Drug Resistance in EVI1high Leukemia

    doi: 10.1371/journal.pone.0030706

    Figure Lengend Snippet: Higher cell adhesion ability in AML cell lines with EVI1 high expression. A . The expression of four integrin genes (ITGB1, ITGB4, ITGA4 and ITGA6), EVI1 and b-actin as a control was determined by semiquantitative RT-PCR in three different EVI1 low and EVI1 high AML cell lines and two primary AML cells lines with high EVI1 expression (PT9 and PT11). B . Six AML cell lines with low or high EVI1expression, as indicated in the figure, were incubated in culture medium on BSA, collagen, fibronectin, laminin or matrigel-coated plates; the percentage of the total number of incubated cells that adhered to the plates was designated as the binding activity (%). Each experiment was performed in triplicate, and the experiments were independently repeated at least three times. The data are given the as the mean ± standard error (S.E). The statistical analysis was performed using the Student's t-test (* p

    Article Snippet: A culture plate was coated overnight with a 1/40 dilution of Growth Factor Reduced-Matrigel (BD Falcon), 5 mg/cm2 of fibronectin (BD Falcon), 5 mg/cm2 of laminin (BD Falcon), 0.3 mg/ml of collagen (Nitta Gelatin) or 5% w/v BSA (Nacalai Tesque).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Incubation, Binding Assay, Activity Assay

    Treatment of SG/BSA dispersions at 37 °C with solutions containing different concentrations of NaClO (0.22 wt%, 0.45 wt%, 1.13 wt%, 2.26 wt%, and 4.52 wt%). ( A ) Changes in the amount of SG-CNTs during treatment, estimated from the absorbance at 700 nm. Curves were fitted using the formula Y = Y 0 + A 1 e −x/t1 + A 2 e −x/t2 (Origin software). ( B ) The degradation half-life time of SG-CNTs. SG/BSA is a CNT-dispersion that was obtained by dispersing SG-CNTs in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).

    Journal: Toxics

    Article Title: Removal of Carbon Nanotubes from Aqueous Solutions by Sodium Hypochlorite: Effects of Treatment Conditions

    doi: 10.3390/toxics9090223

    Figure Lengend Snippet: Treatment of SG/BSA dispersions at 37 °C with solutions containing different concentrations of NaClO (0.22 wt%, 0.45 wt%, 1.13 wt%, 2.26 wt%, and 4.52 wt%). ( A ) Changes in the amount of SG-CNTs during treatment, estimated from the absorbance at 700 nm. Curves were fitted using the formula Y = Y 0 + A 1 e −x/t1 + A 2 e −x/t2 (Origin software). ( B ) The degradation half-life time of SG-CNTs. SG/BSA is a CNT-dispersion that was obtained by dispersing SG-CNTs in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).

    Article Snippet: To obtain CNT dispersions, SG-CNTs were dispersed in an aqueous solution of BSA (fatty acid-free; Nacalai Tesque Inc., Kyoto, Japan) following a standard process (ISO/TS 19337), as reported previously [ , ].

    Techniques: Software

    Degradation of SG/BSA by NaClO solution at different pH values. ( A ) Absorbance SG-CNTs at 700 nm in treatments with different pH values. ( B ) Close-up view of the red framed part in ( A ). SG/BSA is a CNT-dispersion that was obtained by dispersing SG-CNT in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).

    Journal: Toxics

    Article Title: Removal of Carbon Nanotubes from Aqueous Solutions by Sodium Hypochlorite: Effects of Treatment Conditions

    doi: 10.3390/toxics9090223

    Figure Lengend Snippet: Degradation of SG/BSA by NaClO solution at different pH values. ( A ) Absorbance SG-CNTs at 700 nm in treatments with different pH values. ( B ) Close-up view of the red framed part in ( A ). SG/BSA is a CNT-dispersion that was obtained by dispersing SG-CNT in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).

    Article Snippet: To obtain CNT dispersions, SG-CNTs were dispersed in an aqueous solution of BSA (fatty acid-free; Nacalai Tesque Inc., Kyoto, Japan) following a standard process (ISO/TS 19337), as reported previously [ , ].

    Techniques:

    The effect of BSA dispersant on the degradation of SG-CNTs by 2.26 wt% NaClO at 70 °C. The absorbance at 700 nm indicates the change in the amount of SG-CNTs during treatment with different concentrations of SG/BSA ( A ) and ox-SG ( B ). The inset figures in A and B are close-up views of the light-yellow parts in each figure. Images of glass bottles containing SG/BSA ( C ) and ox-SG ( D ) dispersions with different concentration of CNTs following treatment with NaClO for 0−24 h. The concentrations in the legend represent the concentrations of ox-SG (µg/mL) and SG/BSA (µg or mg/mL).

    Journal: Toxics

    Article Title: Removal of Carbon Nanotubes from Aqueous Solutions by Sodium Hypochlorite: Effects of Treatment Conditions

    doi: 10.3390/toxics9090223

    Figure Lengend Snippet: The effect of BSA dispersant on the degradation of SG-CNTs by 2.26 wt% NaClO at 70 °C. The absorbance at 700 nm indicates the change in the amount of SG-CNTs during treatment with different concentrations of SG/BSA ( A ) and ox-SG ( B ). The inset figures in A and B are close-up views of the light-yellow parts in each figure. Images of glass bottles containing SG/BSA ( C ) and ox-SG ( D ) dispersions with different concentration of CNTs following treatment with NaClO for 0−24 h. The concentrations in the legend represent the concentrations of ox-SG (µg/mL) and SG/BSA (µg or mg/mL).

    Article Snippet: To obtain CNT dispersions, SG-CNTs were dispersed in an aqueous solution of BSA (fatty acid-free; Nacalai Tesque Inc., Kyoto, Japan) following a standard process (ISO/TS 19337), as reported previously [ , ].

    Techniques: Concentration Assay

    Degradation of SG/BSA with NaClO solution (2.26 wt%) at different temperatures (25 °C, 37 °C, 50 °C, 70 °C, and 80 °C). ( A ) Absorbance of SG/BSA dispersions at 700 nm during treatment, revealing changes in the amount of SG/BSA. ( B ) Close-up view of the red framed part in ( A ). ( C ) Degradation half-life of SG/BSA. ( D ) Changes in the amount of f-Cl in NaClO solution (2.26 wt%) at different treatment temperatures. The inset graph is a close-up view of the yellow framed part. SG/BSA is a CNT-dispersion that was obtained by dispersing SG-CNTs in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).

    Journal: Toxics

    Article Title: Removal of Carbon Nanotubes from Aqueous Solutions by Sodium Hypochlorite: Effects of Treatment Conditions

    doi: 10.3390/toxics9090223

    Figure Lengend Snippet: Degradation of SG/BSA with NaClO solution (2.26 wt%) at different temperatures (25 °C, 37 °C, 50 °C, 70 °C, and 80 °C). ( A ) Absorbance of SG/BSA dispersions at 700 nm during treatment, revealing changes in the amount of SG/BSA. ( B ) Close-up view of the red framed part in ( A ). ( C ) Degradation half-life of SG/BSA. ( D ) Changes in the amount of f-Cl in NaClO solution (2.26 wt%) at different treatment temperatures. The inset graph is a close-up view of the yellow framed part. SG/BSA is a CNT-dispersion that was obtained by dispersing SG-CNTs in BSA solution (CNTs: 10 µg/mL; BSA: 0.1 mg/mL).

    Article Snippet: To obtain CNT dispersions, SG-CNTs were dispersed in an aqueous solution of BSA (fatty acid-free; Nacalai Tesque Inc., Kyoto, Japan) following a standard process (ISO/TS 19337), as reported previously [ , ].

    Techniques:

    The amounts of free available chlorine (f-Cl) remaining in NaClO solutions (2.26 wt%) after 0–5 h incubation at 70 °C. ( A ) for SG/BS, in which the concentrations of CNTs/BSA were 10/0.1, 30/0.3, 50/0.5, 100/0.1. and 200/0.2 (µg/mg)/mL; ( B ) for BSA at concentrations of 0.1–2 mg/mL; and ( C ) for ox-SG at CNT-concentrations of 0–200 µg/mL. The total amounts of consumed f-Cl after five hours for SG/BSA (blue) at CNT-concentrations of 10–200 µg/mL and BSA only (grey) are shown ( D ). The concentrations of BSA in the SG-BSA samples (blue) were the same as those in the BSA samples (grey). SG/BSA dispersions were obtained by dispersing SG-CNTs in BSA solution (CNTs: 0–200 µg/mL; BSA: 0–2.0 mg/mL).

    Journal: Toxics

    Article Title: Removal of Carbon Nanotubes from Aqueous Solutions by Sodium Hypochlorite: Effects of Treatment Conditions

    doi: 10.3390/toxics9090223

    Figure Lengend Snippet: The amounts of free available chlorine (f-Cl) remaining in NaClO solutions (2.26 wt%) after 0–5 h incubation at 70 °C. ( A ) for SG/BS, in which the concentrations of CNTs/BSA were 10/0.1, 30/0.3, 50/0.5, 100/0.1. and 200/0.2 (µg/mg)/mL; ( B ) for BSA at concentrations of 0.1–2 mg/mL; and ( C ) for ox-SG at CNT-concentrations of 0–200 µg/mL. The total amounts of consumed f-Cl after five hours for SG/BSA (blue) at CNT-concentrations of 10–200 µg/mL and BSA only (grey) are shown ( D ). The concentrations of BSA in the SG-BSA samples (blue) were the same as those in the BSA samples (grey). SG/BSA dispersions were obtained by dispersing SG-CNTs in BSA solution (CNTs: 0–200 µg/mL; BSA: 0–2.0 mg/mL).

    Article Snippet: To obtain CNT dispersions, SG-CNTs were dispersed in an aqueous solution of BSA (fatty acid-free; Nacalai Tesque Inc., Kyoto, Japan) following a standard process (ISO/TS 19337), as reported previously [ , ].

    Techniques: Incubation

    Characteristics of large-diameter carbon nanotubes (Ld-CNTs) and small-diameter carbon nanotubes (Sd-CNTs). Transmission electron microscopy (TEM) images of Ld-CNTs (a), Sd-CNTs (b), and dispersions of Ld-CNTs (c) and Sd-CNTs (d) in BSA.

    Journal: Nanoscale Advances

    Article Title: Clearance of single-wall carbon nanotubes from the mouse lung: a quantitative evaluation †

    doi: 10.1039/d0na00040j

    Figure Lengend Snippet: Characteristics of large-diameter carbon nanotubes (Ld-CNTs) and small-diameter carbon nanotubes (Sd-CNTs). Transmission electron microscopy (TEM) images of Ld-CNTs (a), Sd-CNTs (b), and dispersions of Ld-CNTs (c) and Sd-CNTs (d) in BSA.

    Article Snippet: Ld-CNTs or Sd-CNTs were dispersed in aqueous solutions of bovine serum albumin (BSA) (Nacalai Tesque, Kyoto, Japan).

    Techniques: Transmission Assay, Electron Microscopy, Transmission Electron Microscopy