Structured Review

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.
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Images

1) Product Images from "Two Rapid Catalyst-Free Click Reactions for In Vivo Protein Labeling of Genetically Encoded Strained Alkene/Alkyne Functionalities"

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

Journal: Bioconjugate Chemistry

doi: 10.1021/bc500361d

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.
Figure Legend 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.

Techniques Used: Labeling, SDS Page, Staining, Imaging

2) Product Images from "Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level"

Article Title: Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level

Journal: Scientific Reports

doi: 10.1038/srep35537

Pseudotyped particle protein density analysis. Quantification of intensities of HA, NA and VSV M protein by Western Blot ( A ). The HA 1 ( B ) and NA ( C ) band intensities were directly detected by Chemidoc XRS+ imager and normalized to corresponding M band intensity to obtain the relative HA and NA expression levels on different VSV pseudotyped particles. Each error bar represents the mean ± SD of three independent experiments. NA protein was also detected except for HA only particles.
Figure Legend Snippet: Pseudotyped particle protein density analysis. Quantification of intensities of HA, NA and VSV M protein by Western Blot ( A ). The HA 1 ( B ) and NA ( C ) band intensities were directly detected by Chemidoc XRS+ imager and normalized to corresponding M band intensity to obtain the relative HA and NA expression levels on different VSV pseudotyped particles. Each error bar represents the mean ± SD of three independent experiments. NA protein was also detected except for HA only particles.

Techniques Used: Western Blot, Expressing

3) Product Images from "Bacterial periplasmic nitrate and trimethylamine-N-oxide respiration coupled to menaquinol-cytochrome c reductase (Qcr): Implications for electrogenic reduction of alternative electron acceptors"

Article Title: Bacterial periplasmic nitrate and trimethylamine-N-oxide respiration coupled to menaquinol-cytochrome c reductase (Qcr): Implications for electrogenic reduction of alternative electron acceptors

Journal: Scientific Reports

doi: 10.1038/s41598-018-33857-2

Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.
Figure Legend Snippet: Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.

Techniques Used: Mutagenesis, Reverse Transcription Polymerase Chain Reaction, Expressing, SDS Page, Staining, Activity Assay

4) Product Images from "Muscle Tissue Damage Induced by the Venom of Bothrops asper: Identification of Early and Late Pathological Events through Proteomic Analysis"

Article Title: Muscle Tissue Damage Induced by the Venom of Bothrops asper: Identification of Early and Late Pathological Events through Proteomic Analysis

Journal: PLoS Neglected Tropical Diseases

doi: 10.1371/journal.pntd.0004599

Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).
Figure Legend Snippet: Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

Techniques Used: Western Blot, Mouse Assay, Injection, SDS Page, Immunodetection

5) Product Images from "Rapid Regeneration and Reuse of Silica Columns from PCR Purification and Gel Extraction Kits"

Article Title: Rapid Regeneration and Reuse of Silica Columns from PCR Purification and Gel Extraction Kits

Journal: Scientific Reports

doi: 10.1038/s41598-018-30316-w

Regenerated PCR purification kit columns have a comparable capacity for DNA purification as fresh columns. ( A ) A scheme showing the workflow and duration for the published regeneration methods and for the 1 M phosphoric acid method. PM: published method. ( B ) Comparison of DNA elimination using 1 M phosphoric acid and the published methods. The used columns were cleaned with the protocol as shown in A. Thirty microlitres of eluate was obtained from the regenerated columns, 1 μL of which was used for qPCR. The data were processed as shown in Fig. 1C . ( C ) Comparison of DNA purification efficacy between the regenerated and fresh columns. A 50 μL Tbox 5 PCR reaction was purified with the regenerated or fresh columns, and the DNA concentrations were measured with a Nanophotometer (Thermo Scientific) and then subjected to a statistical analysis. The DNA quality was verified by agarose gel electrophoresis and imaged using a Bio-Rad ChemiDoc XRS + System. Data acquisition and settings are described as in the materials and methods section. The full-length image is presented in Supplementary Fig. S2 . The DNA concentration for each sample is shown beneath the gel picture. ( D ) The regenerated columns showed a similar capacity for purifying different sizes of DNA as the fresh columns. DNA from a 50 μL PCR reaction was purified and quantified as in C. Luc shRNA, Luciferase shRNA cDNA, 70 bp; Hand2, 654 bp, Tbox 5, 1557 bp; pLV-FLNB, 17360 bp. ( E ) Comparison of DNA purification efficacy between the regenerated and fresh columns from different PCR purification kits. DNA from a 50 μL LIF PCR reaction was purified using regenerated or fresh columns, and the data were processed and presented as in C. Each column in B and D represents the mean ± SD of three independent experiments. * p
Figure Legend Snippet: Regenerated PCR purification kit columns have a comparable capacity for DNA purification as fresh columns. ( A ) A scheme showing the workflow and duration for the published regeneration methods and for the 1 M phosphoric acid method. PM: published method. ( B ) Comparison of DNA elimination using 1 M phosphoric acid and the published methods. The used columns were cleaned with the protocol as shown in A. Thirty microlitres of eluate was obtained from the regenerated columns, 1 μL of which was used for qPCR. The data were processed as shown in Fig. 1C . ( C ) Comparison of DNA purification efficacy between the regenerated and fresh columns. A 50 μL Tbox 5 PCR reaction was purified with the regenerated or fresh columns, and the DNA concentrations were measured with a Nanophotometer (Thermo Scientific) and then subjected to a statistical analysis. The DNA quality was verified by agarose gel electrophoresis and imaged using a Bio-Rad ChemiDoc XRS + System. Data acquisition and settings are described as in the materials and methods section. The full-length image is presented in Supplementary Fig. S2 . The DNA concentration for each sample is shown beneath the gel picture. ( D ) The regenerated columns showed a similar capacity for purifying different sizes of DNA as the fresh columns. DNA from a 50 μL PCR reaction was purified and quantified as in C. Luc shRNA, Luciferase shRNA cDNA, 70 bp; Hand2, 654 bp, Tbox 5, 1557 bp; pLV-FLNB, 17360 bp. ( E ) Comparison of DNA purification efficacy between the regenerated and fresh columns from different PCR purification kits. DNA from a 50 μL LIF PCR reaction was purified using regenerated or fresh columns, and the data were processed and presented as in C. Each column in B and D represents the mean ± SD of three independent experiments. * p

Techniques Used: Polymerase Chain Reaction, Purification, DNA Purification, Real-time Polymerase Chain Reaction, Agarose Gel Electrophoresis, Concentration Assay, shRNA, Luciferase

6) Product Images from "Optimisation and comparison of orthogonal methods for separation and characterisation of extracellular vesicles to investigate how representative infant milk formula is of milk"

Article Title: Optimisation and comparison of orthogonal methods for separation and characterisation of extracellular vesicles to investigate how representative infant milk formula is of milk

Journal: bioRxiv

doi: 10.1101/2020.07.27.221622

Immunoblotting of EV specific markers Immunoblotting of skim milk (SM) and infant milk formula (IMF) EVs separated using gradient ultracentrifugation (GUC) and differential ultracentrifugation (DUC) and their densitometric analysis. Equal amount of protein (35 µg) were loaded for all the samples, electrophoresed until optimum separation was achieved and then transferred on to a PVDF membrane before staining with primary (overnight) and secondary (1 h) antibodies before imaging using hi-sensitivity chemiluminescence under Chemidoc XRS system. Representative blots for GUC samples are presented in (a) and DUC samples are presented in (c), overall densitometric analysis of GUC samples are presented in (b) and those of DUC samples in (d). ImageJ software was used to perform densitometric analysis. Each bar represents the mean of the densities of the signals obtained post immunoblotting (mean of n=3 biological repeats ± SEM).
Figure Legend Snippet: Immunoblotting of EV specific markers Immunoblotting of skim milk (SM) and infant milk formula (IMF) EVs separated using gradient ultracentrifugation (GUC) and differential ultracentrifugation (DUC) and their densitometric analysis. Equal amount of protein (35 µg) were loaded for all the samples, electrophoresed until optimum separation was achieved and then transferred on to a PVDF membrane before staining with primary (overnight) and secondary (1 h) antibodies before imaging using hi-sensitivity chemiluminescence under Chemidoc XRS system. Representative blots for GUC samples are presented in (a) and DUC samples are presented in (c), overall densitometric analysis of GUC samples are presented in (b) and those of DUC samples in (d). ImageJ software was used to perform densitometric analysis. Each bar represents the mean of the densities of the signals obtained post immunoblotting (mean of n=3 biological repeats ± SEM).

Techniques Used: Staining, Imaging, Software

7) Product Images from "Phenotype and Response to PAMPs of Human Monocyte-Derived Foam Cells Obtained by Long-Term Culture in the Presence of oxLDLs"

Article Title: Phenotype and Response to PAMPs of Human Monocyte-Derived Foam Cells Obtained by Long-Term Culture in the Presence of oxLDLs

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2020.01592

Western blot analysis of CD11b, CD36, CD47, and CD81 in prolonged- hMDMs and hMDFCs. Whole-cell lysates (25 μg) from prolonged- hMDMs and hMDFCs were analyzed using immunoblotting. Enhanced chemiluminescence signal was detected with Bio-Rad ChemiDoc XRS+ system. β-actin level was determined as a loading control. (A) Images shown are representative of four independent experiments (donors). (B) Quantification of protein levels. The optical density was measured for the bands of interest and normalized to β-actin signal. To compare expression levels of receptors, the relative optical density was calculated (prolonged-hMDFCs vs. corresponding prolonged-hMDMs). Results represents the mean ± SD from four independent experiments. Due to semi-quantitative nature of measurements, statistical analysis was not performed.
Figure Legend Snippet: Western blot analysis of CD11b, CD36, CD47, and CD81 in prolonged- hMDMs and hMDFCs. Whole-cell lysates (25 μg) from prolonged- hMDMs and hMDFCs were analyzed using immunoblotting. Enhanced chemiluminescence signal was detected with Bio-Rad ChemiDoc XRS+ system. β-actin level was determined as a loading control. (A) Images shown are representative of four independent experiments (donors). (B) Quantification of protein levels. The optical density was measured for the bands of interest and normalized to β-actin signal. To compare expression levels of receptors, the relative optical density was calculated (prolonged-hMDFCs vs. corresponding prolonged-hMDMs). Results represents the mean ± SD from four independent experiments. Due to semi-quantitative nature of measurements, statistical analysis was not performed.

Techniques Used: Western Blot, Expressing

8) Product Images from "Abrogation of Neuraminidase Reduces Biofilm Formation, Capsule Biosynthesis, and Virulence of Porphyromonas gingivalis"

Article Title: Abrogation of Neuraminidase Reduces Biofilm Formation, Capsule Biosynthesis, and Virulence of Porphyromonas gingivalis

Journal: Infection and Immunity

doi: 10.1128/IAI.05773-11

PG0352 (Sia Pg ) exhibits neuraminidase activity. (A) Preparation of recombinant PG0352 protein (rSia Pg ). (B) Filter paper spot test of rSia Pg . The assay was conducted using 4-MUNANA as the substrate, and the images were processed using the ChemiDoc XRS
Figure Legend Snippet: PG0352 (Sia Pg ) exhibits neuraminidase activity. (A) Preparation of recombinant PG0352 protein (rSia Pg ). (B) Filter paper spot test of rSia Pg . The assay was conducted using 4-MUNANA as the substrate, and the images were processed using the ChemiDoc XRS

Techniques Used: Activity Assay, Recombinant, Spot Test

9) Product Images from "Development of viral nanoparticles for efficient intracellular delivery †"

Article Title: Development of viral nanoparticles for efficient intracellular delivery †

Journal: Nanoscale

doi: 10.1039/c2nr30366c

Characterization of CPMV labeling with the biotinylated R5 peptide. (A) Size exclusion chromatography of wild-type CPMV, CPMV–R5L and CPMV–R5Hat 280 nm. (B) ECL dot blot of purified CPMV particles. The number of biotin labels per particle was determined using standardized biotin concentrations and Chemidoc XRS software. (C) Native gel electrophoresis of intact CPMV particles (10 µg) using a 0.8% (w/v) agarose gel. Particles were visualized under UV light. Lane 1 = CPMV, 2 = CPMV–4FB, 3 = CPMV–R5H, 4 = CPMV–PFB, 5 = CPMV–R5L. (D) SDS–PAGE of CPMV particles (10 µg) using a 4–12% Bis-Tris gel and western blotting using streptavidin–alkaline phosphatase to detect the N-terminal biotin tag of the R5 peptide. (E) Zeta potential of CPMV wild type, CPMV–R5L and CPMV–R5H formulations.
Figure Legend Snippet: Characterization of CPMV labeling with the biotinylated R5 peptide. (A) Size exclusion chromatography of wild-type CPMV, CPMV–R5L and CPMV–R5Hat 280 nm. (B) ECL dot blot of purified CPMV particles. The number of biotin labels per particle was determined using standardized biotin concentrations and Chemidoc XRS software. (C) Native gel electrophoresis of intact CPMV particles (10 µg) using a 0.8% (w/v) agarose gel. Particles were visualized under UV light. Lane 1 = CPMV, 2 = CPMV–4FB, 3 = CPMV–R5H, 4 = CPMV–PFB, 5 = CPMV–R5L. (D) SDS–PAGE of CPMV particles (10 µg) using a 4–12% Bis-Tris gel and western blotting using streptavidin–alkaline phosphatase to detect the N-terminal biotin tag of the R5 peptide. (E) Zeta potential of CPMV wild type, CPMV–R5L and CPMV–R5H formulations.

Techniques Used: Labeling, Size-exclusion Chromatography, Dot Blot, Purification, Software, Nucleic Acid Electrophoresis, Agarose Gel Electrophoresis, SDS Page, Western Blot

10) Product Images from "Identification of aminosulfonylarylisoxazole as microRNA-31 regulators"

Article Title: Identification of aminosulfonylarylisoxazole as microRNA-31 regulators

Journal: PLoS ONE

doi: 10.1371/journal.pone.0182331

Protein expression of miR-31 targets following compound treatment. A549 cells were treated with compounds 2, 3, and 4 and lysed with RIPA buffer. Total protein concentration was calculated using a BCA assay kit, and 20 μg of total protein was used for western blot analyses of PPP2R2A (A), E2F2 (B), and STK40 (C). The intensity of each blot was normalized against that of β-tubulin. Bands were detected using the ChemiDoc™ XRS+ System. (* represents non-specific band).
Figure Legend Snippet: Protein expression of miR-31 targets following compound treatment. A549 cells were treated with compounds 2, 3, and 4 and lysed with RIPA buffer. Total protein concentration was calculated using a BCA assay kit, and 20 μg of total protein was used for western blot analyses of PPP2R2A (A), E2F2 (B), and STK40 (C). The intensity of each blot was normalized against that of β-tubulin. Bands were detected using the ChemiDoc™ XRS+ System. (* represents non-specific band).

Techniques Used: Expressing, Protein Concentration, BIA-KA, Western Blot

11) Product Images from "Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage"

Article Title: Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage

Journal: PLoS Neglected Tropical Diseases

doi: 10.1371/journal.pntd.0003731

Western blot analysis of basement membrane components in skin homogenates. Groups of five mice were injected by intradermal route in the ventral abdominal region with either BaP1 (PI, 75 μg), BlatH1 (PII, 1.5 μg), CsH1 (PIII, 35 μg) SVMPs or PBS (lane C). After 15 min, mice were sacrificed, their skin was removed, and an area of 12 mm diameter was dissected out. Tissues of the same group were homogenized and centrifuged, and the supernatant collected. Then, 10–20 μL of each skin homogenate sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE gradient gels, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-collagen type IV, (B) anti-collagen type VI, (C) anti-laminin, and (D) anti-nidogen 1. The anti-GAPDH antibody was used as loading control. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).
Figure Legend Snippet: Western blot analysis of basement membrane components in skin homogenates. Groups of five mice were injected by intradermal route in the ventral abdominal region with either BaP1 (PI, 75 μg), BlatH1 (PII, 1.5 μg), CsH1 (PIII, 35 μg) SVMPs or PBS (lane C). After 15 min, mice were sacrificed, their skin was removed, and an area of 12 mm diameter was dissected out. Tissues of the same group were homogenized and centrifuged, and the supernatant collected. Then, 10–20 μL of each skin homogenate sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE gradient gels, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-collagen type IV, (B) anti-collagen type VI, (C) anti-laminin, and (D) anti-nidogen 1. The anti-GAPDH antibody was used as loading control. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

Techniques Used: Western Blot, Mouse Assay, Injection, SDS Page, Immunodetection

Western blot analysis of basement membrane components in exudates collected from the gastrocnemius. Groups of five mice were injected in the right gastrocnemius with either BaP1 (PI, 75 μg), BlatH1 (PII, 3 μg), or CsH1 (PIII, 50 μg) SVMPs. After 15 min, mice were sacrificed, a 5 mm incision was made in the skin overlying the injected muscle, and a heparinized capillary tube was introduced under the skin to collect the wound exudate fluid; exudate samples from a single treatment were then pooled. Afterwards, 100 μg of protein of each sample was separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-collagen type IV, (B) anti-collagen type VI, (C) anti-laminin, and (D) anti-nidogen 1. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).
Figure Legend Snippet: Western blot analysis of basement membrane components in exudates collected from the gastrocnemius. Groups of five mice were injected in the right gastrocnemius with either BaP1 (PI, 75 μg), BlatH1 (PII, 3 μg), or CsH1 (PIII, 50 μg) SVMPs. After 15 min, mice were sacrificed, a 5 mm incision was made in the skin overlying the injected muscle, and a heparinized capillary tube was introduced under the skin to collect the wound exudate fluid; exudate samples from a single treatment were then pooled. Afterwards, 100 μg of protein of each sample was separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-collagen type IV, (B) anti-collagen type VI, (C) anti-laminin, and (D) anti-nidogen 1. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

Techniques Used: Western Blot, Mouse Assay, Injection, SDS Page, Immunodetection

12) Product Images from "Conditional U1 Gene Silencing in Toxoplasma gondii"

Article Title: Conditional U1 Gene Silencing in Toxoplasma gondii

Journal: PLoS ONE

doi: 10.1371/journal.pone.0130356

The U1 mediated knockdown strategy is not functional in P . falciparum . (A) Schematic showing the strategy used to replace the endogenous pfsub1 3’ UTR with a floxed heterologous PbDT 3’ UTR with a downstream sequence comprising 10 U1 recognition sequences. The single cross-over homologous recombination event also results in the fusion of a HA3 epitope tag to PfSUB1. The predicted results of DiCre mediated recombination induced by treatment with rapamycin are shown. The positions of hybridization of PCR primers designed to specifically amplify sequences from the intact and excised locus are indicated with red and blue arrows. (B) IFA of mature schizonts of integrant clone D3, probed with mAb NIMP.M7 (anti PfSUB1) and mAb 3F10 (anti HA3). (C) Efficient DiCre-mediated recombination between the integrated loxP sites, as shown by diagnostic PCR analysis of parasite genomic DNA extracted 44 h following rapamycin treatment of two independent parasite clones D3 and B11. The blue and red arrows correspond to primer pairs marked in (A). (D) Upper panel: Western blot analysis with mAb 3F10 shows no down-regulation of PfSUB1 protein expression protein 44 h or 6 days after rapamycin treatment. Lower panel: loading controls, showing total protein SDS PAGE gels detected by UV fluorescence on the BioRad Chemidoc XRS system prior to Western transfer.
Figure Legend Snippet: The U1 mediated knockdown strategy is not functional in P . falciparum . (A) Schematic showing the strategy used to replace the endogenous pfsub1 3’ UTR with a floxed heterologous PbDT 3’ UTR with a downstream sequence comprising 10 U1 recognition sequences. The single cross-over homologous recombination event also results in the fusion of a HA3 epitope tag to PfSUB1. The predicted results of DiCre mediated recombination induced by treatment with rapamycin are shown. The positions of hybridization of PCR primers designed to specifically amplify sequences from the intact and excised locus are indicated with red and blue arrows. (B) IFA of mature schizonts of integrant clone D3, probed with mAb NIMP.M7 (anti PfSUB1) and mAb 3F10 (anti HA3). (C) Efficient DiCre-mediated recombination between the integrated loxP sites, as shown by diagnostic PCR analysis of parasite genomic DNA extracted 44 h following rapamycin treatment of two independent parasite clones D3 and B11. The blue and red arrows correspond to primer pairs marked in (A). (D) Upper panel: Western blot analysis with mAb 3F10 shows no down-regulation of PfSUB1 protein expression protein 44 h or 6 days after rapamycin treatment. Lower panel: loading controls, showing total protein SDS PAGE gels detected by UV fluorescence on the BioRad Chemidoc XRS system prior to Western transfer.

Techniques Used: Functional Assay, Sequencing, Homologous Recombination, Hybridization, Polymerase Chain Reaction, Immunofluorescence, Diagnostic Assay, Clone Assay, Western Blot, Expressing, SDS Page, Fluorescence

13) Product Images from "Conditional U1 Gene Silencing in Toxoplasma gondii"

Article Title: Conditional U1 Gene Silencing in Toxoplasma gondii

Journal: PLoS ONE

doi: 10.1371/journal.pone.0130356

The U1 mediated knockdown strategy is not functional in P . falciparum . (A) Schematic showing the strategy used to replace the endogenous pfsub1 3’ UTR with a floxed heterologous PbDT 3’ UTR with a downstream sequence comprising 10 U1 recognition sequences. The single cross-over homologous recombination event also results in the fusion of a HA3 epitope tag to PfSUB1. The predicted results of DiCre mediated recombination induced by treatment with rapamycin are shown. The positions of hybridization of PCR primers designed to specifically amplify sequences from the intact and excised locus are indicated with red and blue arrows. (B) IFA of mature schizonts of integrant clone D3, probed with mAb NIMP.M7 (anti PfSUB1) and mAb 3F10 (anti HA3). (C) Efficient DiCre-mediated recombination between the integrated loxP sites, as shown by diagnostic PCR analysis of parasite genomic DNA extracted 44 h following rapamycin treatment of two independent parasite clones D3 and B11. The blue and red arrows correspond to primer pairs marked in (A). (D) Upper panel: Western blot analysis with mAb 3F10 shows no down-regulation of PfSUB1 protein expression protein 44 h or 6 days after rapamycin treatment. Lower panel: loading controls, showing total protein SDS PAGE gels detected by UV fluorescence on the BioRad Chemidoc XRS system prior to Western transfer.
Figure Legend Snippet: The U1 mediated knockdown strategy is not functional in P . falciparum . (A) Schematic showing the strategy used to replace the endogenous pfsub1 3’ UTR with a floxed heterologous PbDT 3’ UTR with a downstream sequence comprising 10 U1 recognition sequences. The single cross-over homologous recombination event also results in the fusion of a HA3 epitope tag to PfSUB1. The predicted results of DiCre mediated recombination induced by treatment with rapamycin are shown. The positions of hybridization of PCR primers designed to specifically amplify sequences from the intact and excised locus are indicated with red and blue arrows. (B) IFA of mature schizonts of integrant clone D3, probed with mAb NIMP.M7 (anti PfSUB1) and mAb 3F10 (anti HA3). (C) Efficient DiCre-mediated recombination between the integrated loxP sites, as shown by diagnostic PCR analysis of parasite genomic DNA extracted 44 h following rapamycin treatment of two independent parasite clones D3 and B11. The blue and red arrows correspond to primer pairs marked in (A). (D) Upper panel: Western blot analysis with mAb 3F10 shows no down-regulation of PfSUB1 protein expression protein 44 h or 6 days after rapamycin treatment. Lower panel: loading controls, showing total protein SDS PAGE gels detected by UV fluorescence on the BioRad Chemidoc XRS system prior to Western transfer.

Techniques Used: Functional Assay, Sequencing, Homologous Recombination, Hybridization, Polymerase Chain Reaction, Immunofluorescence, Diagnostic Assay, Clone Assay, Western Blot, Expressing, SDS Page, Fluorescence

14) Product Images from "A novel bi-domain plant defensin MtDef5 with potent broad-spectrum antifungal activity binds to multiple phospholipids and forms oligomers"

Article Title: A novel bi-domain plant defensin MtDef5 with potent broad-spectrum antifungal activity binds to multiple phospholipids and forms oligomers

Journal: Scientific Reports

doi: 10.1038/s41598-017-16508-w

MtDef5 forms oligomers only in presence of PIP. ( A ) MtDef5 forms higher order oligomers in presence of PI3P, PI4P and PI5P as revealed by a protein cross-linking with BS 3 followed by SDS-PAGE and visualized using a Bio-Rad ChemiDoc XRS + system. ( B ) MtDef5 also forms oligomers in presence of PA and PI. The full length gel is presented in Supplementary Figure S5 .
Figure Legend Snippet: MtDef5 forms oligomers only in presence of PIP. ( A ) MtDef5 forms higher order oligomers in presence of PI3P, PI4P and PI5P as revealed by a protein cross-linking with BS 3 followed by SDS-PAGE and visualized using a Bio-Rad ChemiDoc XRS + system. ( B ) MtDef5 also forms oligomers in presence of PA and PI. The full length gel is presented in Supplementary Figure S5 .

Techniques Used: SDS Page

15) Product Images from "Giardia duodenalis Cathepsin B Proteases Degrade Intestinal Epithelial Interleukin-8 and Attenuate Interleukin-8-Induced Neutrophil Chemotaxis"

Article Title: Giardia duodenalis Cathepsin B Proteases Degrade Intestinal Epithelial Interleukin-8 and Attenuate Interleukin-8-Induced Neutrophil Chemotaxis

Journal: Infection and Immunity

doi: 10.1128/IAI.01771-14

Giardia duodenalis trophozoites secrete cysteine proteases that are inhibited by E-64d and Ca-074Me. Caco-2 monolayers were pretreated with 1 μM E-64d (A) or increasing concentrations of Ca-074Me (1, 10, or 50 μM) (B to E) and subsequently coincubated with G. duodenalis NF trophozoites (MOI, 10:1) for 6 h. Supernatan ts were incubated with the cathepsin B and L fluorogenic substrate ZFR-AMC (A and B) or the catB fluorogenic substrate ZRR-AMC (C) (200 μM, 5 min, 37°C, and pH 7.2). Proteolytic activity was determined by graphing the change in reflective light units over time. Caco-2 monolayers not containing G. duodenalis trophozoites were used as controls. Supernatants were collected, and the log total of supernatant trophozoites (D) and the ratio of motile to nonmotile trophozoites (E) were determined via enumeration on a hemocytometer. (F) Giardia duodenalis NF and GS/M trophozoite sonicates were run through an SDS-PAGE gel copolymerized with Z-Phe-Arg-AMC under nondenaturing conditions and visualized with a ChemiDoc XRS system. All data are representative of at least two independent experiments ( n = 2 or 3/group) and represented as means ± SEM. n.s., not significant. *, P
Figure Legend Snippet: Giardia duodenalis trophozoites secrete cysteine proteases that are inhibited by E-64d and Ca-074Me. Caco-2 monolayers were pretreated with 1 μM E-64d (A) or increasing concentrations of Ca-074Me (1, 10, or 50 μM) (B to E) and subsequently coincubated with G. duodenalis NF trophozoites (MOI, 10:1) for 6 h. Supernatan ts were incubated with the cathepsin B and L fluorogenic substrate ZFR-AMC (A and B) or the catB fluorogenic substrate ZRR-AMC (C) (200 μM, 5 min, 37°C, and pH 7.2). Proteolytic activity was determined by graphing the change in reflective light units over time. Caco-2 monolayers not containing G. duodenalis trophozoites were used as controls. Supernatants were collected, and the log total of supernatant trophozoites (D) and the ratio of motile to nonmotile trophozoites (E) were determined via enumeration on a hemocytometer. (F) Giardia duodenalis NF and GS/M trophozoite sonicates were run through an SDS-PAGE gel copolymerized with Z-Phe-Arg-AMC under nondenaturing conditions and visualized with a ChemiDoc XRS system. All data are representative of at least two independent experiments ( n = 2 or 3/group) and represented as means ± SEM. n.s., not significant. *, P

Techniques Used: Incubation, Activity Assay, SDS Page

16) Product Images from "Neuritin Activates Insulin Receptor Pathway to Up-regulate Kv4.2-mediated Transient Outward K+ Current in Rat Cerebellar Granule Neurons *"

Article Title: Neuritin Activates Insulin Receptor Pathway to Up-regulate Kv4.2-mediated Transient Outward K+ Current in Rat Cerebellar Granule Neurons *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M112.390260

Neuritin-induced I A densities and the increased expression of Kv4.2 α-subunit were dependent the Akt/mTOR signaling pathway. A , Western blot showing the levels of activated Akt (pAkt) and activated mTOR (p-mTOR) in CGNs incubated with 150 ng/ml neuritin for 15 min to 24 h. Chemiluminescent signals were detected with the ChemiDoc XRS System. B , effect of mTOR inhibitor, rapamycin, and Akt inhibitor LY294002 on neuritin-induced up-regulation of I A densities. C and D , effect of rapamycin and LY294002 on neuritin-induced up-regulation of Kv4.2 protein level. E , effect of rapamycin on neuritin-induced up-regulation of Kv4.2 mRNA expression measured by quantitative RT-PCR experiments. Data are shown as means ± S.E. ( error bars ). *, p
Figure Legend Snippet: Neuritin-induced I A densities and the increased expression of Kv4.2 α-subunit were dependent the Akt/mTOR signaling pathway. A , Western blot showing the levels of activated Akt (pAkt) and activated mTOR (p-mTOR) in CGNs incubated with 150 ng/ml neuritin for 15 min to 24 h. Chemiluminescent signals were detected with the ChemiDoc XRS System. B , effect of mTOR inhibitor, rapamycin, and Akt inhibitor LY294002 on neuritin-induced up-regulation of I A densities. C and D , effect of rapamycin and LY294002 on neuritin-induced up-regulation of Kv4.2 protein level. E , effect of rapamycin on neuritin-induced up-regulation of Kv4.2 mRNA expression measured by quantitative RT-PCR experiments. Data are shown as means ± S.E. ( error bars ). *, p

Techniques Used: Expressing, Western Blot, Incubation, Quantitative RT-PCR

Neuritin increased the expression levels of Kv4.2 α-subunit rather than Kv4.3 or Kv1.1 in CGNs. A , Western blot showing effect of 150 ng/ml neuritin on different Kv channels expression levels in CGNs with different DIC. Left , representative Western blots. Right , statistical analysis. B , Western blot results of Kv4.2 α-subunit protein expression levels in CGNs, showing the effect of incubating with 150 ng/ml neuritin for 12–36 h. Chemiluminescent signals were detected using the ChemiDoc XRS System. *, p
Figure Legend Snippet: Neuritin increased the expression levels of Kv4.2 α-subunit rather than Kv4.3 or Kv1.1 in CGNs. A , Western blot showing effect of 150 ng/ml neuritin on different Kv channels expression levels in CGNs with different DIC. Left , representative Western blots. Right , statistical analysis. B , Western blot results of Kv4.2 α-subunit protein expression levels in CGNs, showing the effect of incubating with 150 ng/ml neuritin for 12–36 h. Chemiluminescent signals were detected using the ChemiDoc XRS System. *, p

Techniques Used: Expressing, Western Blot

17) Product Images from "Reprogramming of Yersinia from Virulent to Persistent Mode Revealed by Complex In Vivo RNA-seq Analysis"

Article Title: Reprogramming of Yersinia from Virulent to Persistent Mode Revealed by Complex In Vivo RNA-seq Analysis

Journal: PLoS Pathogens

doi: 10.1371/journal.ppat.1004600

Establishment of persistent infection requires arcA, fnr, frdA , and wrbA . (A) Infection profile 42 dpi for FVB/N mice infected orally with10 7 CFUs of wt Y. pseudotuberculosis (n = 20) and indicated mutant strains (each group n = 16). The infections were monitored by IVIS at certain intervals up to 42 dpi. (B) Heatmap showing differences in clearance (by p -value) between wt and indicated mutant strains at different time points during the 42 day infection period. Heatmap color scale, from green to yellow, was adjusted according to p -values from 1 to 0. p -values were calculated with 2×2 contingency table by Fisher’s Exact Test, see also S6 Table . (C) Motility profile of wt Y. pseudotuberculosis and indicated mutant strains under anaerobic conditions at 26°C. Images were captured by the ChemiDoc XRS System (Bio-Rad), showing the bioluminescent signal produced by Y. pseudotuberculosis YPIII/pIBX.
Figure Legend Snippet: Establishment of persistent infection requires arcA, fnr, frdA , and wrbA . (A) Infection profile 42 dpi for FVB/N mice infected orally with10 7 CFUs of wt Y. pseudotuberculosis (n = 20) and indicated mutant strains (each group n = 16). The infections were monitored by IVIS at certain intervals up to 42 dpi. (B) Heatmap showing differences in clearance (by p -value) between wt and indicated mutant strains at different time points during the 42 day infection period. Heatmap color scale, from green to yellow, was adjusted according to p -values from 1 to 0. p -values were calculated with 2×2 contingency table by Fisher’s Exact Test, see also S6 Table . (C) Motility profile of wt Y. pseudotuberculosis and indicated mutant strains under anaerobic conditions at 26°C. Images were captured by the ChemiDoc XRS System (Bio-Rad), showing the bioluminescent signal produced by Y. pseudotuberculosis YPIII/pIBX.

Techniques Used: Infection, Mouse Assay, Mutagenesis, Produced

18) Product Images from "A novel bi-domain plant defensin MtDef5 with potent broad-spectrum antifungal activity binds to multiple phospholipids and forms oligomers"

Article Title: A novel bi-domain plant defensin MtDef5 with potent broad-spectrum antifungal activity binds to multiple phospholipids and forms oligomers

Journal: Scientific Reports

doi: 10.1038/s41598-017-16508-w

MtDef5 forms oligomers only in presence of PIP. ( A ) MtDef5 forms higher order oligomers in presence of PI3P, PI4P and PI5P as revealed by a protein cross-linking with BS 3 followed by SDS-PAGE and visualized using a Bio-Rad ChemiDoc XRS + system. ( B ) MtDef5 also forms oligomers in presence of PA and PI. The full length gel is presented in Supplementary Figure S5 .
Figure Legend Snippet: MtDef5 forms oligomers only in presence of PIP. ( A ) MtDef5 forms higher order oligomers in presence of PI3P, PI4P and PI5P as revealed by a protein cross-linking with BS 3 followed by SDS-PAGE and visualized using a Bio-Rad ChemiDoc XRS + system. ( B ) MtDef5 also forms oligomers in presence of PA and PI. The full length gel is presented in Supplementary Figure S5 .

Techniques Used: SDS Page

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Irradiation:

Article Title: Two Rapid Catalyst-Free Click Reactions for In Vivo Protein Labeling of Genetically Encoded Strained Alkene/Alkyne Functionalities
Article Snippet: .. The fluorescence was detected in a Bio-Rad ChemiDoc XRS+ system under UV irradiation. .. Live Cell Labeling and Imaging BL21(DE3) cells were transformed to carry plasmids pEVOL-PylT-Y306A/N346A/C348A/Y384F and pETDuet-OmpXTAG that contained a gene coding E. coli membrane protein OmpX with an amber mutation.

Agarose Gel Electrophoresis:

Article Title: Rapid Regeneration and Reuse of Silica Columns from PCR Purification and Gel Extraction Kits
Article Snippet: .. Data acquisition and settings Agarose gel electrophoresis was performed at 90 V for 20 min, after which the gel was imaged using a Bio-Rad ChemiDoc XRS + System with following a nucleic acid ethidium bromide staining protocol. .. The exposure time was set for 0.5 sec; the image colour was set grey and inverted presentation.

Fluorescence:

Article Title: Abrogation of Neuraminidase Reduces Biofilm Formation, Capsule Biosynthesis, and Virulence of Porphyromonas gingivalis
Article Snippet: .. Fluorescence was detected using the ChemiDoc XRS System (Bio-Rad) with an excitation wavelength of 302 nm and an emission wavelength of 548 nm. ..

Article Title: Two Rapid Catalyst-Free Click Reactions for In Vivo Protein Labeling of Genetically Encoded Strained Alkene/Alkyne Functionalities
Article Snippet: .. The fluorescence was detected in a Bio-Rad ChemiDoc XRS+ system under UV irradiation. .. Live Cell Labeling and Imaging BL21(DE3) cells were transformed to carry plasmids pEVOL-PylT-Y306A/N346A/C348A/Y384F and pETDuet-OmpXTAG that contained a gene coding E. coli membrane protein OmpX with an amber mutation.

Western Blot:

Article Title: Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level
Article Snippet: .. All Western blots were visualized and analyzed using a Chemidoc XRS+ system with Image Lab image capture software (BioRad). .. TheImage Lab software was used to quantify intensities of bands using low sensitivity setting.

Staining:

Article Title: Optimisation and comparison of orthogonal methods for separation and characterisation of extracellular vesicles to investigate how representative infant milk formula is of milk
Article Snippet: .. For this, 15 µg of protein samples were loaded on a 10% polyacrylamide gel, run at 120 volts, stained with coomassie blue (Sigma Aldrich, Ireland) and visualised using a Chemidoc XRS system (Bio-Rad). .. 2.5 Protein quantificationA bicinchoninic acid (BCA) reagent kit (Fisher Scientific, Cat. #10249133), with a bovine serum albumin (BSA) standard (0–800 μg/mL) (Sigma Aldrich, Ireland) curve, was used to determine total protein in samples.

Article Title: Rapid Regeneration and Reuse of Silica Columns from PCR Purification and Gel Extraction Kits
Article Snippet: .. Data acquisition and settings Agarose gel electrophoresis was performed at 90 V for 20 min, after which the gel was imaged using a Bio-Rad ChemiDoc XRS + System with following a nucleic acid ethidium bromide staining protocol. .. The exposure time was set for 0.5 sec; the image colour was set grey and inverted presentation.

Software:

Article Title: Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level
Article Snippet: .. All Western blots were visualized and analyzed using a Chemidoc XRS+ system with Image Lab image capture software (BioRad). .. TheImage Lab software was used to quantify intensities of bands using low sensitivity setting.

Article Title: Muscle Tissue Damage Induced by the Venom of Bothrops asper: Identification of Early and Late Pathological Events through Proteomic Analysis
Article Snippet: .. Images were captured with the ChemiDoc XRS+ System (BioRad) and the analysis was performed with the ImageLab software (BioRad). .. Quantification of proteolytic activity of wound exudates

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    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.
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    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

    Pseudotyped particle protein density analysis. Quantification of intensities of HA, NA and VSV M protein by Western Blot ( A ). The HA 1 ( B ) and NA ( C ) band intensities were directly detected by Chemidoc XRS+ imager and normalized to corresponding M band intensity to obtain the relative HA and NA expression levels on different VSV pseudotyped particles. Each error bar represents the mean ± SD of three independent experiments. NA protein was also detected except for HA only particles.

    Journal: Scientific Reports

    Article Title: Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level

    doi: 10.1038/srep35537

    Figure Lengend Snippet: Pseudotyped particle protein density analysis. Quantification of intensities of HA, NA and VSV M protein by Western Blot ( A ). The HA 1 ( B ) and NA ( C ) band intensities were directly detected by Chemidoc XRS+ imager and normalized to corresponding M band intensity to obtain the relative HA and NA expression levels on different VSV pseudotyped particles. Each error bar represents the mean ± SD of three independent experiments. NA protein was also detected except for HA only particles.

    Article Snippet: All Western blots were visualized and analyzed using a Chemidoc XRS+ system with Image Lab image capture software (BioRad).

    Techniques: Western Blot, Expressing

    Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.

    Journal: Scientific Reports

    Article Title: Bacterial periplasmic nitrate and trimethylamine-N-oxide respiration coupled to menaquinol-cytochrome c reductase (Qcr): Implications for electrogenic reduction of alternative electron acceptors

    doi: 10.1038/s41598-018-33857-2

    Figure Lengend Snippet: Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.

    Article Snippet: Images were obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min.

    Techniques: Mutagenesis, Reverse Transcription Polymerase Chain Reaction, Expressing, SDS Page, Staining, Activity Assay

    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Muscle Tissue Damage Induced by the Venom of Bothrops asper: Identification of Early and Late Pathological Events through Proteomic Analysis

    doi: 10.1371/journal.pntd.0004599

    Figure Lengend Snippet: Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

    Article Snippet: Images were captured with the ChemiDoc XRS+ System (BioRad) and the analysis was performed with the ImageLab software (BioRad).

    Techniques: Western Blot, Mouse Assay, Injection, SDS Page, Immunodetection