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  • 92
    Bio-Rad chemidoc xrs system
    Selective labeling of sfGFPs that contained site-specifically incorporated NCAAs with strained alkene/alkyne functionalities with (A) FITC-TZ and (B) HZCL. In A and B, the top panels show denaturing SDS-PAGE analysis of proteins stained with Coomassie blue and the bottom panels are from fluorescent imaging of the same gels before Coomassie blue staining. In A, the fluorescent image was captured by a digital camera and displayed was real color of the emitting light. In B, the fluorescent image was captured by a Bio-Rad <t>ChemiDoc</t> <t>XRS</t> system.
    Chemidoc Xrs System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 21527 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad chemidoc xrs imaging system
    Western blot analysis of placenta homogenates using anti-ALDH3B2 and anti-GAPDH antibodies revealed bands corresponding to the molecular weight of 53 kDa (long isoform of ALDH3B2) and bands corresponding to molecular weight of 37 kDa (GAPDH). Proteins in homogenates were applied onto the polyacrylamide gel. After separation, they were transferred onto the PVDF membrane. Immunodetection of ALDH3B2 protein was performed using anti-ALDH3B2 antibody. After membrane stripping, the immunodetection was repeated with anti-GAPDH antibody. GAPDH detection was used as a loading control, as GAPDH gene is constitutively expressed at high levels in many tissues. The image was taken using <t>ChemiDoc</t> <t>XRS+</t> (Bio-Rad). Additionally, the image of the whole membrane was added into the Supplementary Materials (Supplementary Figure S1) .
    Chemidoc Xrs Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 8678 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Bio-Rad chemidoc xrs gel doc system
    Western blot analysis of placenta homogenates using anti-ALDH3B2 and anti-GAPDH antibodies revealed bands corresponding to the molecular weight of 53 kDa (long isoform of ALDH3B2) and bands corresponding to molecular weight of 37 kDa (GAPDH). Proteins in homogenates were applied onto the polyacrylamide gel. After separation, they were transferred onto the PVDF membrane. Immunodetection of ALDH3B2 protein was performed using anti-ALDH3B2 antibody. After membrane stripping, the immunodetection was repeated with anti-GAPDH antibody. GAPDH detection was used as a loading control, as GAPDH gene is constitutively expressed at high levels in many tissues. The image was taken using <t>ChemiDoc</t> <t>XRS+</t> (Bio-Rad). Additionally, the image of the whole membrane was added into the Supplementary Materials (Supplementary Figure S1) .
    Chemidoc Xrs Gel Doc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 86/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad chemidoc xrs gel imaging system
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemidoc Xrs Gel Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 644 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Bio-Rad molecular imager chemidoc xrs imaging system
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Molecular Imager Chemidoc Xrs Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 441 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Bio-Rad chemiluminescence detection system
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemiluminescence Detection System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 92/100, based on 1884 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Bio-Rad chemidoc xrs apparatus
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemidoc Xrs Apparatus, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 89/100, based on 216 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Rad chemidoc xrs image system
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemidoc Xrs Image System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 246 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Bio-Rad chemidoc xrs device
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemidoc Xrs Device, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 79 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Bio-Rad chemidoc xrs image analyzer
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemidoc Xrs Image Analyzer, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 185 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Rad chemidoc xrs documentation system
    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a <t>ChemiDoc</t> <t>XRS+</t> Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.
    Chemidoc Xrs Documentation System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 186 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Selective labeling of sfGFPs that contained site-specifically incorporated NCAAs with strained alkene/alkyne functionalities with (A) FITC-TZ and (B) HZCL. In A and B, the top panels show denaturing SDS-PAGE analysis of proteins stained with Coomassie blue and the bottom panels are from fluorescent imaging of the same gels before Coomassie blue staining. In A, the fluorescent image was captured by a digital camera and displayed was real color of the emitting light. In B, the fluorescent image was captured by a Bio-Rad ChemiDoc XRS system.

    Journal: Bioconjugate Chemistry

    Article Title: Two Rapid Catalyst-Free Click Reactions for In Vivo Protein Labeling of Genetically Encoded Strained Alkene/Alkyne Functionalities

    doi: 10.1021/bc500361d

    Figure Lengend Snippet: Selective labeling of sfGFPs that contained site-specifically incorporated NCAAs with strained alkene/alkyne functionalities with (A) FITC-TZ and (B) HZCL. In A and B, the top panels show denaturing SDS-PAGE analysis of proteins stained with Coomassie blue and the bottom panels are from fluorescent imaging of the same gels before Coomassie blue staining. In A, the fluorescent image was captured by a digital camera and displayed was real color of the emitting light. In B, the fluorescent image was captured by a Bio-Rad ChemiDoc XRS system.

    Article Snippet: The fluorescence was detected in a Bio-Rad ChemiDoc XRS+ system under UV irradiation.

    Techniques: Labeling, SDS Page, Staining, Imaging

    Western Blot analysis of nNOS and eNOS. Cardiac left ventricle tissue homogenates from control animals with untreated cardiac arrest (C group), or after 180 min of untreated return of spontaneous circulation (ROSC180 group), after 180 min of mild therapeutic hypothermia (MTH group) or 180 min after S-PBN infusion (S-PBN group) were loaded on a 4–20% SDS-acrylamide gel. Bands for neuronal NOS (nNOS) (A), endothelial NOS (eNOS) (C) and β-actin (A and C) were detected at 160 kDa, 135 kDa and 42 kDa, respectively. Protein band intensities for nNOS (B) and eNOS (D) were quantified using a ChemiDoc XRS and Quantity One software and normalized to the loading control (β-actin). Error bars represent standard error of the mean (SEM). Significant results (p

    Journal: PLoS ONE

    Article Title: Therapeutic Hypothermia Activates the Endothelin and Nitric Oxide Systems after Cardiac Arrest in a Pig Model of Cardiopulmonary Resuscitation

    doi: 10.1371/journal.pone.0064792

    Figure Lengend Snippet: Western Blot analysis of nNOS and eNOS. Cardiac left ventricle tissue homogenates from control animals with untreated cardiac arrest (C group), or after 180 min of untreated return of spontaneous circulation (ROSC180 group), after 180 min of mild therapeutic hypothermia (MTH group) or 180 min after S-PBN infusion (S-PBN group) were loaded on a 4–20% SDS-acrylamide gel. Bands for neuronal NOS (nNOS) (A), endothelial NOS (eNOS) (C) and β-actin (A and C) were detected at 160 kDa, 135 kDa and 42 kDa, respectively. Protein band intensities for nNOS (B) and eNOS (D) were quantified using a ChemiDoc XRS and Quantity One software and normalized to the loading control (β-actin). Error bars represent standard error of the mean (SEM). Significant results (p

    Article Snippet: Protein band densities were digitally quantified and normalized to the loading control (β-actin) with a ChemiDoc XRS and Quantity One image analysis software (Bio-Rad laboratories, USA).

    Techniques: Western Blot, Acrylamide Gel Assay, Software

    Western Blot analysis of ETAR and ETBR. Cardiac left ventricle tissue homogenates from control animals with untreated cardiac arrest (C group), or after 180 min of untreated return of spontaneous circulation (ROSC180 group), after 180 min of mild therapeutic hypothermia (MTH group) or 180 min after S-PBN infusion (S-PBN group) were loaded on a 12% SDS-acrylamide gel. Bands for endothelin A receptor (ETAR), endothelin B receptor (ETBR) and β-actin were detected at 25 kDa, 50 kDa and 42 kDa, respectively (A). Protein band intensities were quantified using a ChemiDoc XRS and Quantity One software and normalized to the loading control (β-actin) (B). Error bars represent standard error of the mean (SEM). Significant results (p

    Journal: PLoS ONE

    Article Title: Therapeutic Hypothermia Activates the Endothelin and Nitric Oxide Systems after Cardiac Arrest in a Pig Model of Cardiopulmonary Resuscitation

    doi: 10.1371/journal.pone.0064792

    Figure Lengend Snippet: Western Blot analysis of ETAR and ETBR. Cardiac left ventricle tissue homogenates from control animals with untreated cardiac arrest (C group), or after 180 min of untreated return of spontaneous circulation (ROSC180 group), after 180 min of mild therapeutic hypothermia (MTH group) or 180 min after S-PBN infusion (S-PBN group) were loaded on a 12% SDS-acrylamide gel. Bands for endothelin A receptor (ETAR), endothelin B receptor (ETBR) and β-actin were detected at 25 kDa, 50 kDa and 42 kDa, respectively (A). Protein band intensities were quantified using a ChemiDoc XRS and Quantity One software and normalized to the loading control (β-actin) (B). Error bars represent standard error of the mean (SEM). Significant results (p

    Article Snippet: Protein band densities were digitally quantified and normalized to the loading control (β-actin) with a ChemiDoc XRS and Quantity One image analysis software (Bio-Rad laboratories, USA).

    Techniques: Western Blot, Acrylamide Gel Assay, Software

    Cell cycle recurrence is abrogated by anti-estrogen ICI 182780. Cells were seeded at 200 cells per well and treated with combinations of IPTG, ICI 182780, E2 and vehicle over a period of 4 and 12 weeks and colonies were visualised with methylene blue staining. A. Colonies (+) were counted using a Bio-Rad ChemiDoc XRS + imager in biological triplicate. B. Representative wells showing IPTG and ICI 182780 and vehicle (control) treated colonies at week 4. C. IPTG treated cells at week 12.

    Journal: PLoS ONE

    Article Title: p14ARF Post-Transcriptional Regulation of Nuclear Cyclin D1 in MCF-7 Breast Cancer Cells: Discrimination between a Good and Bad Prognosis?

    doi: 10.1371/journal.pone.0042246

    Figure Lengend Snippet: Cell cycle recurrence is abrogated by anti-estrogen ICI 182780. Cells were seeded at 200 cells per well and treated with combinations of IPTG, ICI 182780, E2 and vehicle over a period of 4 and 12 weeks and colonies were visualised with methylene blue staining. A. Colonies (+) were counted using a Bio-Rad ChemiDoc XRS + imager in biological triplicate. B. Representative wells showing IPTG and ICI 182780 and vehicle (control) treated colonies at week 4. C. IPTG treated cells at week 12.

    Article Snippet: Colonies were imaged and analysed using a Bio-Rad ChemiDoc XRS + imager (Bio-Rad).

    Techniques: Staining

    Zinkicide detection and concentration measurements. (a) Representative 2D SDS-PAGE image of Zinkicide at varying concentrations in deionized water. The image was acquired using UV gel imaging protocol with the Bio-Rad ChemiDoc XRS+ device. (b) 3D rendering of SDS-PAGE gel of Zinkicide NPs is obtained through Bio-Rad Image Lab software. The 3D image is identical to the 2D image. (c) Fluorescence intensity as a function of Zinkicide concentrations. The loading and imaging conditions of Zinkicide were recorded at the following concentrations: lane 1: 445 ppm, lane 2: 890 ppm, lane 3: 1781 ppm, lane 4: 3562 ppm, lane 5: 7125 ppm, lane 6: 14,250 ppm, and lane 7: 28,500 ppm.

    Journal: ACS Omega

    Article Title: SDS-PAGE for Monitoring the Dissolution of Zinc Oxide Bactericidal Nanoparticles (Zinkicide) in Aqueous Solutions

    doi: 10.1021/acsomega.9b02893

    Figure Lengend Snippet: Zinkicide detection and concentration measurements. (a) Representative 2D SDS-PAGE image of Zinkicide at varying concentrations in deionized water. The image was acquired using UV gel imaging protocol with the Bio-Rad ChemiDoc XRS+ device. (b) 3D rendering of SDS-PAGE gel of Zinkicide NPs is obtained through Bio-Rad Image Lab software. The 3D image is identical to the 2D image. (c) Fluorescence intensity as a function of Zinkicide concentrations. The loading and imaging conditions of Zinkicide were recorded at the following concentrations: lane 1: 445 ppm, lane 2: 890 ppm, lane 3: 1781 ppm, lane 4: 3562 ppm, lane 5: 7125 ppm, lane 6: 14,250 ppm, and lane 7: 28,500 ppm.

    Article Snippet: The slides were placed in the Bio-Rad ChemiDoc XRS+ and captured using the UV preset in Bio-Rad Image Lab Software.

    Techniques: Concentration Assay, SDS Page, Imaging, Software, Fluorescence

    Interaction of mRELT with mHsc70. A. Immunoblot of RELT immunoprecipitations (IP) from RAW264.7 cells grown under standard culture conditions. Hsc70 and RELT were immunoblotted (IB) separately and proteins are indicated with arrows. MWM: molecular weight marker; No Ab: elution of non-antibody-conjugated Protein G beads; FT: flow-through of lysate after antibody/bead complex addition; elution: 70 °C, 10 minutes in SDS-PAGE buffer. Images were captured with a Bio-Rad Molecular Imager ChemiDoc XRS+ using Image Lab 5.2.1. For each blot, the image was captured twice, first using white epi-illumination to capture the Broad Range Color Protein Standard (New England Biolabs) followed by chemiluminescence to capture the sample bands. The saved imaged where overlaid in Image Lab 5.2.1 using the Merge Image function. B. Representative fragment ion series of the D 160 AGTIAGLNVLR 171 (observed m/z 600.340, observed mass (+H) 1199.673 Da, +2 charge, −0.8 ppm mass error, Byonic score 376.5)and C. F 302 EELNADLFR 311 (observed m/z 627.314, observed mass (+H) 1253.620 Da, +2 charge, +3.0 ppm mass error, Byonic score 319.4) peptides. Isotopic distributions for peaks labeled with (*) were unable to be extracted from the data results.

    Journal: bioRxiv

    Article Title: Lipopolysaccharide stimulation of RAW264.7 cells is a model for identifying novel clients of Hsc70

    doi: 10.1101/2020.05.15.098525

    Figure Lengend Snippet: Interaction of mRELT with mHsc70. A. Immunoblot of RELT immunoprecipitations (IP) from RAW264.7 cells grown under standard culture conditions. Hsc70 and RELT were immunoblotted (IB) separately and proteins are indicated with arrows. MWM: molecular weight marker; No Ab: elution of non-antibody-conjugated Protein G beads; FT: flow-through of lysate after antibody/bead complex addition; elution: 70 °C, 10 minutes in SDS-PAGE buffer. Images were captured with a Bio-Rad Molecular Imager ChemiDoc XRS+ using Image Lab 5.2.1. For each blot, the image was captured twice, first using white epi-illumination to capture the Broad Range Color Protein Standard (New England Biolabs) followed by chemiluminescence to capture the sample bands. The saved imaged where overlaid in Image Lab 5.2.1 using the Merge Image function. B. Representative fragment ion series of the D 160 AGTIAGLNVLR 171 (observed m/z 600.340, observed mass (+H) 1199.673 Da, +2 charge, −0.8 ppm mass error, Byonic score 376.5)and C. F 302 EELNADLFR 311 (observed m/z 627.314, observed mass (+H) 1253.620 Da, +2 charge, +3.0 ppm mass error, Byonic score 319.4) peptides. Isotopic distributions for peaks labeled with (*) were unable to be extracted from the data results.

    Article Snippet: After washing with TBS-T three times for five minutes and TBS three times for five minutes, blots were imaged using either WestPico ECL (ThermoFisher) and Molecular Imager ChemiDoc XRS+ (BioRad, Hercules, CA) for HRP-conjugated secondary antibodies.

    Techniques: Molecular Weight, Marker, SDS Page, Labeling

    Western blot analysis of placenta homogenates using anti-ALDH3B2 and anti-GAPDH antibodies revealed bands corresponding to the molecular weight of 53 kDa (long isoform of ALDH3B2) and bands corresponding to molecular weight of 37 kDa (GAPDH). Proteins in homogenates were applied onto the polyacrylamide gel. After separation, they were transferred onto the PVDF membrane. Immunodetection of ALDH3B2 protein was performed using anti-ALDH3B2 antibody. After membrane stripping, the immunodetection was repeated with anti-GAPDH antibody. GAPDH detection was used as a loading control, as GAPDH gene is constitutively expressed at high levels in many tissues. The image was taken using ChemiDoc XRS+ (Bio-Rad). Additionally, the image of the whole membrane was added into the Supplementary Materials (Supplementary Figure S1) .

    Journal: International Journal of Molecular Sciences

    Article Title: Detection of ALDH3B2 in Human Placenta

    doi: 10.3390/ijms20246292

    Figure Lengend Snippet: Western blot analysis of placenta homogenates using anti-ALDH3B2 and anti-GAPDH antibodies revealed bands corresponding to the molecular weight of 53 kDa (long isoform of ALDH3B2) and bands corresponding to molecular weight of 37 kDa (GAPDH). Proteins in homogenates were applied onto the polyacrylamide gel. After separation, they were transferred onto the PVDF membrane. Immunodetection of ALDH3B2 protein was performed using anti-ALDH3B2 antibody. After membrane stripping, the immunodetection was repeated with anti-GAPDH antibody. GAPDH detection was used as a loading control, as GAPDH gene is constitutively expressed at high levels in many tissues. The image was taken using ChemiDoc XRS+ (Bio-Rad). Additionally, the image of the whole membrane was added into the Supplementary Materials (Supplementary Figure S1) .

    Article Snippet: Human ALDH3B2 protein was detected using goat anti-human ALDH3B2 antibody (1:200, v/v ) (Santa Cruz Biotechnology, Inc., Dallas, TX, USA) by incubation at 4 °C for 12 h. After being washed three times, membranes were incubated with horseradish peroxidase-conjugated (HRP) anti-goat antibody (1:40,000) (Sigma-Aldrich) for 1 h. Finally, proteins bound with antibody were visualized using chemiluminescence (Pierce ECL Western Blotting Substrate, Thermo Scientific, Waltham, MA, USA) and ChemiDoc XRS+ imaging system (Bio-Rad).

    Techniques: Western Blot, Molecular Weight, Immunodetection, Stripping Membranes

    Western blot analysis using anti-ALDH3B2 antibody confirmed the expression of both short and long isoforms of recombinant ALDH3B2 protein in E. coli . Purified recombinant proteins were applied onto the polyacrylamide gel. After separation, they were transferred onto the PVDF membrane. Their immunodetection was performed using anti-ALDH3B2 antibody. The image was taken using ChemiDoc XRS+ (Bio-Rad).

    Journal: International Journal of Molecular Sciences

    Article Title: Detection of ALDH3B2 in Human Placenta

    doi: 10.3390/ijms20246292

    Figure Lengend Snippet: Western blot analysis using anti-ALDH3B2 antibody confirmed the expression of both short and long isoforms of recombinant ALDH3B2 protein in E. coli . Purified recombinant proteins were applied onto the polyacrylamide gel. After separation, they were transferred onto the PVDF membrane. Their immunodetection was performed using anti-ALDH3B2 antibody. The image was taken using ChemiDoc XRS+ (Bio-Rad).

    Article Snippet: Human ALDH3B2 protein was detected using goat anti-human ALDH3B2 antibody (1:200, v/v ) (Santa Cruz Biotechnology, Inc., Dallas, TX, USA) by incubation at 4 °C for 12 h. After being washed three times, membranes were incubated with horseradish peroxidase-conjugated (HRP) anti-goat antibody (1:40,000) (Sigma-Aldrich) for 1 h. Finally, proteins bound with antibody were visualized using chemiluminescence (Pierce ECL Western Blotting Substrate, Thermo Scientific, Waltham, MA, USA) and ChemiDoc XRS+ imaging system (Bio-Rad).

    Techniques: Western Blot, Expressing, Recombinant, Purification, Immunodetection

    Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a ChemiDoc XRS+ Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.

    Journal: PLoS ONE

    Article Title: Identification of a Short Cell-Penetrating Peptide from Bovine Lactoferricin for Intracellular Delivery of DNA in Human A549 Cells

    doi: 10.1371/journal.pone.0150439

    Figure Lengend Snippet: Noncovalent interactions between CPPs and plasmid DNA in vitro . (A) Gel retardation assay indicating the formation of CPP/DNA complexes. Various amounts of L6 or L5a were mixed with DNA at molecular N/P ratios of 0 (DNA only), 3, 6, 9, 12, 15, and 18. These complexes were analyzed by electrophoresis on a 0.5% agarose gel, followed by SYBR Safe staining. DNA images were captured using a ChemiDoc XRS+ Gel Imaging System (Bio-Rad). (B) The relative mobility of CPP/DNA complexes. The mobility of CPP/DNA complexes is indicated. Data are presented as mean ± SD from five independent experiments in each treatment group.

    Article Snippet: Gels were stained with the SYBR Safe DNA gel stain (Life Technologies), and images were captured using the ChemiDoc XRS+ gel imaging system (Bio-Rad, Hercules, CA, USA) with an excitation wavelength at 302 nm of trans-UV light and with an emission wavelength at 548–630 nm of the standard filter.

    Techniques: Plasmid Preparation, In Vitro, Electrophoretic Mobility Shift Assay, Conditioned Place Preference, Electrophoresis, Agarose Gel Electrophoresis, Staining, Imaging