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  • 99
    Millipore all trans retinoic acid
    All Trans Retinoic Acid, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3091 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad trans blot turbo transfer system
    Trans Blot Turbo Transfer System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 10224 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad mini trans blot cell
    Mini Trans Blot Cell, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 4287 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad trans blot turbo system
    Trans Blot Turbo System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 2911 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore fatty acid free bsa
    Fatty Acid Free Bsa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3869 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore all trans retinal
    All Trans Retinal, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 747 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Mirus Bio trans it lt1
    CAL reduces the expression level of mature Mrp2 in cotransfected COS-7 and LLC-PK1 cells. COS-7 ( A and B ) were cotransfected with fixed quantity of plasmid expressing full-length rMrp2 and different molar ratios of plasmids expressing HA-CAL or NHERF-1 to maintain equal quantity of total plasmid DNA in each transfection. Cells were transfected with <t>Trans-IT-LT1</t> and were incubated for 24 h before harvest. Whole cell lysates were extracted and subjected to immunoblotting (IB). Mrp2 and Hsp70 (served as the loading control) were detected with their respective antibodies. Note that only a high-molecular-mass band (∼200 kDa) of Mrp2 was detected in the lysates of cells cotransfected with Mrp2 and a vector control ( A , transfection 2 ). In contrast, both the high-molecular-mass band and a lower molecular-mass band (∼150 kDa) of Mrp2 were detected in cells cotransfected with Mrp2 and HA-CAL ( A , transfection 3 and transfection 4 ). C : similar results were obtained with LLC-PK1 cells transfected with Lipofectamine 2000. B : 8 μg of whole cell lysates of transfected COS-7 (from transfection 2 and transfection 3 in A ) were digested in vitro with PNGase F or Endo H without boiling the samples and then subjected to IB. Note that, while the high band of Mrp2 (∼200 kDa) shifted to the low band (∼150 kDa) of Mrp2 after PNGase F digestion, but remained unchanged after Endo H digestion, the low-molecular-mass band was sensitive to both PNGase F and Endo H treatment. Data are representative of 4 independent experiments.
    Trans It Lt1, supplied by Mirus Bio, used in various techniques. Bioz Stars score: 93/100, based on 1111 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Rad trans blot sd semi dry transfer cell
    CAL reduces the expression level of mature Mrp2 in cotransfected COS-7 and LLC-PK1 cells. COS-7 ( A and B ) were cotransfected with fixed quantity of plasmid expressing full-length rMrp2 and different molar ratios of plasmids expressing HA-CAL or NHERF-1 to maintain equal quantity of total plasmid DNA in each transfection. Cells were transfected with <t>Trans-IT-LT1</t> and were incubated for 24 h before harvest. Whole cell lysates were extracted and subjected to immunoblotting (IB). Mrp2 and Hsp70 (served as the loading control) were detected with their respective antibodies. Note that only a high-molecular-mass band (∼200 kDa) of Mrp2 was detected in the lysates of cells cotransfected with Mrp2 and a vector control ( A , transfection 2 ). In contrast, both the high-molecular-mass band and a lower molecular-mass band (∼150 kDa) of Mrp2 were detected in cells cotransfected with Mrp2 and HA-CAL ( A , transfection 3 and transfection 4 ). C : similar results were obtained with LLC-PK1 cells transfected with Lipofectamine 2000. B : 8 μg of whole cell lysates of transfected COS-7 (from transfection 2 and transfection 3 in A ) were digested in vitro with PNGase F or Endo H without boiling the samples and then subjected to IB. Note that, while the high band of Mrp2 (∼200 kDa) shifted to the low band (∼150 kDa) of Mrp2 after PNGase F digestion, but remained unchanged after Endo H digestion, the low-molecular-mass band was sensitive to both PNGase F and Endo H treatment. Data are representative of 4 independent experiments.
    Trans Blot Sd Semi Dry Transfer Cell, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 1234 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Bio-Rad trans blot nitrocellulose membranes
    CAL reduces the expression level of mature Mrp2 in cotransfected COS-7 and LLC-PK1 cells. COS-7 ( A and B ) were cotransfected with fixed quantity of plasmid expressing full-length rMrp2 and different molar ratios of plasmids expressing HA-CAL or NHERF-1 to maintain equal quantity of total plasmid DNA in each transfection. Cells were transfected with <t>Trans-IT-LT1</t> and were incubated for 24 h before harvest. Whole cell lysates were extracted and subjected to immunoblotting (IB). Mrp2 and Hsp70 (served as the loading control) were detected with their respective antibodies. Note that only a high-molecular-mass band (∼200 kDa) of Mrp2 was detected in the lysates of cells cotransfected with Mrp2 and a vector control ( A , transfection 2 ). In contrast, both the high-molecular-mass band and a lower molecular-mass band (∼150 kDa) of Mrp2 were detected in cells cotransfected with Mrp2 and HA-CAL ( A , transfection 3 and transfection 4 ). C : similar results were obtained with LLC-PK1 cells transfected with Lipofectamine 2000. B : 8 μg of whole cell lysates of transfected COS-7 (from transfection 2 and transfection 3 in A ) were digested in vitro with PNGase F or Endo H without boiling the samples and then subjected to IB. Note that, while the high band of Mrp2 (∼200 kDa) shifted to the low band (∼150 kDa) of Mrp2 after PNGase F digestion, but remained unchanged after Endo H digestion, the low-molecular-mass band was sensitive to both PNGase F and Endo H treatment. Data are representative of 4 independent experiments.
    Trans Blot Nitrocellulose Membranes, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 89/100, based on 382 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Mirus Bio trans it lt1 transfection reagent
    <t>Transfection</t> into COS-1, HeLa S3, Dami, and HCT116 cells. a – c EGFP expression was examined by fluorescence microscopy. Scale bars , 10 μm. a COS-1 and HeLa S3 cells were transiently transfected with the polyplex formed by mixing 5 μg of pcDNA4-TO-EGFP with 25 μg of PEI in LBS (pH 4.0), and after 12 h of culture the medium was replaced with fresh serum-containing medium. b COS-1 cells were transiently transfected with the polyplex formed by mixing 1 μg of pcDNA4-TO-EGFP with 5 μg of PEI in LBS (pH 4.0) or an optimal amount of Trans <t>IT-LT1.</t> c ”, and transiently transfected with the polyplex formed by mixing 4 μg of pcDNA4-TO-EGFP with 26 μg of PEI in LBS (pH 4.0). d ”, and stained with anti-CD25 antibody. Representative histograms of control ( shaded areas ) and transfected cells ( solid line ) are shown for CD25 expression at low to high levels ( thin arrows ). e ”. Zeocin-resistant colonies were cloned in 2 weeks and observed by fluorescence microscopy. Scale bar , 10 μm
    Trans It Lt1 Transfection Reagent, supplied by Mirus Bio, used in various techniques. Bioz Stars score: 92/100, based on 979 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore trans resveratrol
    Initial cleavage sites in Aβ42 resulting from IDE-dependent degradation in the presence of <t>resveratrol.</t> (A) Mass spectrum of the primary N-terminal fragments (colored accordingly), which have retention times of 25–30 min. Peaks labeled in black correspond to secondary fragments. (B) Mass spectrum of the primary C-terminal fragments (colored accordingly), which have retention times of 40–43 min. Peaks labeled with asterisks correspond to Aβ42. (C) Peptide maps of Aβ42 depicting initial cleavages at the peptide bonds between Phe19 and Phe20, between Phe20 and Ala21, and between Lys28 and Gly29, corresponding to the color-coded fragments in (A) and (B). Residues in the CHC and loop region are italicized and underlined, respectively.
    Trans Resveratrol, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 401 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad pvdf membrane
    Initial cleavage sites in Aβ42 resulting from IDE-dependent degradation in the presence of <t>resveratrol.</t> (A) Mass spectrum of the primary N-terminal fragments (colored accordingly), which have retention times of 25–30 min. Peaks labeled in black correspond to secondary fragments. (B) Mass spectrum of the primary C-terminal fragments (colored accordingly), which have retention times of 40–43 min. Peaks labeled with asterisks correspond to Aβ42. (C) Peptide maps of Aβ42 depicting initial cleavages at the peptide bonds between Phe19 and Phe20, between Phe20 and Ala21, and between Lys28 and Gly29, corresponding to the color-coded fragments in (A) and (B). Residues in the CHC and loop region are italicized and underlined, respectively.
    Pvdf Membrane, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 30039 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    CAL reduces the expression level of mature Mrp2 in cotransfected COS-7 and LLC-PK1 cells. COS-7 ( A and B ) were cotransfected with fixed quantity of plasmid expressing full-length rMrp2 and different molar ratios of plasmids expressing HA-CAL or NHERF-1 to maintain equal quantity of total plasmid DNA in each transfection. Cells were transfected with Trans-IT-LT1 and were incubated for 24 h before harvest. Whole cell lysates were extracted and subjected to immunoblotting (IB). Mrp2 and Hsp70 (served as the loading control) were detected with their respective antibodies. Note that only a high-molecular-mass band (∼200 kDa) of Mrp2 was detected in the lysates of cells cotransfected with Mrp2 and a vector control ( A , transfection 2 ). In contrast, both the high-molecular-mass band and a lower molecular-mass band (∼150 kDa) of Mrp2 were detected in cells cotransfected with Mrp2 and HA-CAL ( A , transfection 3 and transfection 4 ). C : similar results were obtained with LLC-PK1 cells transfected with Lipofectamine 2000. B : 8 μg of whole cell lysates of transfected COS-7 (from transfection 2 and transfection 3 in A ) were digested in vitro with PNGase F or Endo H without boiling the samples and then subjected to IB. Note that, while the high band of Mrp2 (∼200 kDa) shifted to the low band (∼150 kDa) of Mrp2 after PNGase F digestion, but remained unchanged after Endo H digestion, the low-molecular-mass band was sensitive to both PNGase F and Endo H treatment. Data are representative of 4 independent experiments.

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: CFTR-associated ligand is a negative regulator of Mrp2 expression

    doi: 10.1152/ajpcell.00100.2016

    Figure Lengend Snippet: CAL reduces the expression level of mature Mrp2 in cotransfected COS-7 and LLC-PK1 cells. COS-7 ( A and B ) were cotransfected with fixed quantity of plasmid expressing full-length rMrp2 and different molar ratios of plasmids expressing HA-CAL or NHERF-1 to maintain equal quantity of total plasmid DNA in each transfection. Cells were transfected with Trans-IT-LT1 and were incubated for 24 h before harvest. Whole cell lysates were extracted and subjected to immunoblotting (IB). Mrp2 and Hsp70 (served as the loading control) were detected with their respective antibodies. Note that only a high-molecular-mass band (∼200 kDa) of Mrp2 was detected in the lysates of cells cotransfected with Mrp2 and a vector control ( A , transfection 2 ). In contrast, both the high-molecular-mass band and a lower molecular-mass band (∼150 kDa) of Mrp2 were detected in cells cotransfected with Mrp2 and HA-CAL ( A , transfection 3 and transfection 4 ). C : similar results were obtained with LLC-PK1 cells transfected with Lipofectamine 2000. B : 8 μg of whole cell lysates of transfected COS-7 (from transfection 2 and transfection 3 in A ) were digested in vitro with PNGase F or Endo H without boiling the samples and then subjected to IB. Note that, while the high band of Mrp2 (∼200 kDa) shifted to the low band (∼150 kDa) of Mrp2 after PNGase F digestion, but remained unchanged after Endo H digestion, the low-molecular-mass band was sensitive to both PNGase F and Endo H treatment. Data are representative of 4 independent experiments.

    Article Snippet: Cells in six-well plates (BD Falcon, Franklin Lakes, NJ) were transfected with plasmid DNA using Lipofectamine 2000 (Invitrogen; for HEK-293, LLCPK-1, and Huh-7 cells) or Trans-IT-LT1 (Mirus Bio LLC, Madison, WI; for COS-7 cells), in Opti-MEM I Reduced Serum Medium (Invitrogen), according to the manufacturer's instructions.

    Techniques: Expressing, Plasmid Preparation, Transfection, Incubation, In Vitro

    Mrp2 but not Bsep coprecipitates with HA-CAL in cotransfected COS-7 cells. COS-7 cells were cotransfected with plasmids expressing full-length rMrp2 or rBsep and HA-CAL using Trans-IT-LT1. The cell lysates were precipitated with anti-HA agarose beads, and the pull-down complexes were analyzed by immunoblotting (IB) with anti-Mrp2 or anti-Bsep antibody. Note that Mrp2 was detected only in the co-IP complex from cells cotransfected with plasmids expressing both Mrp2 and HA-CAL (arrow), but was not detected from cells cotransfected with the Mrp2 plasmid and a vector control. In contrast, rBsep was absent in the co-IP complex, although it was detected in the cell lysates. IP, immunoprecipitation. Data are representative of three independent experiments.

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: CFTR-associated ligand is a negative regulator of Mrp2 expression

    doi: 10.1152/ajpcell.00100.2016

    Figure Lengend Snippet: Mrp2 but not Bsep coprecipitates with HA-CAL in cotransfected COS-7 cells. COS-7 cells were cotransfected with plasmids expressing full-length rMrp2 or rBsep and HA-CAL using Trans-IT-LT1. The cell lysates were precipitated with anti-HA agarose beads, and the pull-down complexes were analyzed by immunoblotting (IB) with anti-Mrp2 or anti-Bsep antibody. Note that Mrp2 was detected only in the co-IP complex from cells cotransfected with plasmids expressing both Mrp2 and HA-CAL (arrow), but was not detected from cells cotransfected with the Mrp2 plasmid and a vector control. In contrast, rBsep was absent in the co-IP complex, although it was detected in the cell lysates. IP, immunoprecipitation. Data are representative of three independent experiments.

    Article Snippet: Cells in six-well plates (BD Falcon, Franklin Lakes, NJ) were transfected with plasmid DNA using Lipofectamine 2000 (Invitrogen; for HEK-293, LLCPK-1, and Huh-7 cells) or Trans-IT-LT1 (Mirus Bio LLC, Madison, WI; for COS-7 cells), in Opti-MEM I Reduced Serum Medium (Invitrogen), according to the manufacturer's instructions.

    Techniques: Expressing, Co-Immunoprecipitation Assay, Plasmid Preparation, Immunoprecipitation

    Transfection into COS-1, HeLa S3, Dami, and HCT116 cells. a – c EGFP expression was examined by fluorescence microscopy. Scale bars , 10 μm. a COS-1 and HeLa S3 cells were transiently transfected with the polyplex formed by mixing 5 μg of pcDNA4-TO-EGFP with 25 μg of PEI in LBS (pH 4.0), and after 12 h of culture the medium was replaced with fresh serum-containing medium. b COS-1 cells were transiently transfected with the polyplex formed by mixing 1 μg of pcDNA4-TO-EGFP with 5 μg of PEI in LBS (pH 4.0) or an optimal amount of Trans IT-LT1. c ”, and transiently transfected with the polyplex formed by mixing 4 μg of pcDNA4-TO-EGFP with 26 μg of PEI in LBS (pH 4.0). d ”, and stained with anti-CD25 antibody. Representative histograms of control ( shaded areas ) and transfected cells ( solid line ) are shown for CD25 expression at low to high levels ( thin arrows ). e ”. Zeocin-resistant colonies were cloned in 2 weeks and observed by fluorescence microscopy. Scale bar , 10 μm

    Journal: Cytotechnology

    Article Title: Cost-effective gene transfection by DNA compaction at pH 4.0 using acidified, long shelf-life polyethylenimine

    doi: 10.1007/s10616-010-9259-z

    Figure Lengend Snippet: Transfection into COS-1, HeLa S3, Dami, and HCT116 cells. a – c EGFP expression was examined by fluorescence microscopy. Scale bars , 10 μm. a COS-1 and HeLa S3 cells were transiently transfected with the polyplex formed by mixing 5 μg of pcDNA4-TO-EGFP with 25 μg of PEI in LBS (pH 4.0), and after 12 h of culture the medium was replaced with fresh serum-containing medium. b COS-1 cells were transiently transfected with the polyplex formed by mixing 1 μg of pcDNA4-TO-EGFP with 5 μg of PEI in LBS (pH 4.0) or an optimal amount of Trans IT-LT1. c ”, and transiently transfected with the polyplex formed by mixing 4 μg of pcDNA4-TO-EGFP with 26 μg of PEI in LBS (pH 4.0). d ”, and stained with anti-CD25 antibody. Representative histograms of control ( shaded areas ) and transfected cells ( solid line ) are shown for CD25 expression at low to high levels ( thin arrows ). e ”. Zeocin-resistant colonies were cloned in 2 weeks and observed by fluorescence microscopy. Scale bar , 10 μm

    Article Snippet: The Trans IT-LT1 transfection reagent was purchased from Mirus Bio LLC (cat. no. MIR 2306).

    Techniques: Transfection, Expressing, Fluorescence, Microscopy, Staining, Clone Assay

    Initial cleavage sites in Aβ42 resulting from IDE-dependent degradation in the presence of resveratrol. (A) Mass spectrum of the primary N-terminal fragments (colored accordingly), which have retention times of 25–30 min. Peaks labeled in black correspond to secondary fragments. (B) Mass spectrum of the primary C-terminal fragments (colored accordingly), which have retention times of 40–43 min. Peaks labeled with asterisks correspond to Aβ42. (C) Peptide maps of Aβ42 depicting initial cleavages at the peptide bonds between Phe19 and Phe20, between Phe20 and Ala21, and between Lys28 and Gly29, corresponding to the color-coded fragments in (A) and (B). Residues in the CHC and loop region are italicized and underlined, respectively.

    Journal: ACS Omega

    Article Title: Resveratrol Sustains Insulin-Degrading Enzyme Activity toward Aβ42

    doi: 10.1021/acsomega.8b01913

    Figure Lengend Snippet: Initial cleavage sites in Aβ42 resulting from IDE-dependent degradation in the presence of resveratrol. (A) Mass spectrum of the primary N-terminal fragments (colored accordingly), which have retention times of 25–30 min. Peaks labeled in black correspond to secondary fragments. (B) Mass spectrum of the primary C-terminal fragments (colored accordingly), which have retention times of 40–43 min. Peaks labeled with asterisks correspond to Aβ42. (C) Peptide maps of Aβ42 depicting initial cleavages at the peptide bonds between Phe19 and Phe20, between Phe20 and Ala21, and between Lys28 and Gly29, corresponding to the color-coded fragments in (A) and (B). Residues in the CHC and loop region are italicized and underlined, respectively.

    Article Snippet: A stock solution (0.5 mg/mL) of trans -resveratrol ( > 99% pure by GC, Sigma-Aldrich, St. Louis MO) was prepared in 100% ethanol.

    Techniques: Labeling

    Resveratrol has two isomers. trans -Resveratrol (left) is more stable and potent than cis -resveratrol (right).

    Journal: ACS Omega

    Article Title: Resveratrol Sustains Insulin-Degrading Enzyme Activity toward Aβ42

    doi: 10.1021/acsomega.8b01913

    Figure Lengend Snippet: Resveratrol has two isomers. trans -Resveratrol (left) is more stable and potent than cis -resveratrol (right).

    Article Snippet: A stock solution (0.5 mg/mL) of trans -resveratrol ( > 99% pure by GC, Sigma-Aldrich, St. Louis MO) was prepared in 100% ethanol.

    Techniques:

    Primary fragments of Aβ42 were degraded significantly by IDE in the presence of resveratrol at pH 7.4 and 4 °C. (A) Total mass spectrum of the 2 h digest shows the presence of peaks due to primary Aβ42 fragments resulting from initial cleavages and peaks corresponding to secondary fragments resulting from further degradation of the primary fragments. (B) Total mass spectrum of the 6 h digest shows significant changes relative to the spectrum in (A), including alterations in peak intensities and the appearance of new peaks. Dominant peaks in (A) and (B) are identified by their m / z ).

    Journal: ACS Omega

    Article Title: Resveratrol Sustains Insulin-Degrading Enzyme Activity toward Aβ42

    doi: 10.1021/acsomega.8b01913

    Figure Lengend Snippet: Primary fragments of Aβ42 were degraded significantly by IDE in the presence of resveratrol at pH 7.4 and 4 °C. (A) Total mass spectrum of the 2 h digest shows the presence of peaks due to primary Aβ42 fragments resulting from initial cleavages and peaks corresponding to secondary fragments resulting from further degradation of the primary fragments. (B) Total mass spectrum of the 6 h digest shows significant changes relative to the spectrum in (A), including alterations in peak intensities and the appearance of new peaks. Dominant peaks in (A) and (B) are identified by their m / z ).

    Article Snippet: A stock solution (0.5 mg/mL) of trans -resveratrol ( > 99% pure by GC, Sigma-Aldrich, St. Louis MO) was prepared in 100% ethanol.

    Techniques: