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    Millipore polyvinylidene fluoride pvdf membrane
    Detection and characterization of HcAPN3 expressed in H. cunea BBMV from different development larval stages and infected Sf9 cells. Protein from BBMV prepared from different developmental instars (lane 1–5), Sf9 cells containing control baculovirus alone (lane 6) and Sf9 cells infected with recombinant baculoviruse (lane 7) were separated by 10% <t>SDS-PAGE</t> and electrotransferred to <t>PVDF</t> membrane. ( A ) Western blot analysis of the expression of HcAPN3 with anti-HcAPN3 antibodies; ( B ) Binding detection of Cry1Ab35 toxin to HcAPN3 by ligand blot assay with anti-Cry1Ab35 antibodies. Lane M shows molecular weight markers and arrows indicate the position of the HcAPN3 protein in H. cunea BBMV.

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    1) Product Images from "Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin"

    Article Title: Identification and Characterization of Hyphantria cunea Aminopeptidase N as a Binding Protein of Bacillus thuringiensis Cry1Ab35 Toxin

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms18122575

    Detection and characterization of HcAPN3 expressed in H. cunea BBMV from different development larval stages and infected Sf9 cells. Protein from BBMV prepared from different developmental instars (lane 1–5), Sf9 cells containing control baculovirus alone (lane 6) and Sf9 cells infected with recombinant baculoviruse (lane 7) were separated by 10% SDS-PAGE and electrotransferred to PVDF membrane. ( A ) Western blot analysis of the expression of HcAPN3 with anti-HcAPN3 antibodies; ( B ) Binding detection of Cry1Ab35 toxin to HcAPN3 by ligand blot assay with anti-Cry1Ab35 antibodies. Lane M shows molecular weight markers and arrows indicate the position of the HcAPN3 protein in H. cunea BBMV.
    Figure Legend Snippet: Detection and characterization of HcAPN3 expressed in H. cunea BBMV from different development larval stages and infected Sf9 cells. Protein from BBMV prepared from different developmental instars (lane 1–5), Sf9 cells containing control baculovirus alone (lane 6) and Sf9 cells infected with recombinant baculoviruse (lane 7) were separated by 10% SDS-PAGE and electrotransferred to PVDF membrane. ( A ) Western blot analysis of the expression of HcAPN3 with anti-HcAPN3 antibodies; ( B ) Binding detection of Cry1Ab35 toxin to HcAPN3 by ligand blot assay with anti-Cry1Ab35 antibodies. Lane M shows molecular weight markers and arrows indicate the position of the HcAPN3 protein in H. cunea BBMV.

    Techniques Used: Infection, Recombinant, SDS Page, Western Blot, Expressing, Binding Assay, Molecular Weight

    HcAPN3G and HcAPN3E fragment peptides expressed in E.coli BL21 (DE3) cells. HcAPN3G (lane 1) and HcAPN3E (lane 2) peptides expressed in E. coli BL21 (DE3) cells were separated by 10% SDS-PAGE, and either stained with Coomassie Brilliant Blue R-250 ( A ) or transferred to a PVDF membrane and probed by Cry1Ab35 toxin in ligand blot assay ( B ) with anti-Cry1Ab35 antibodies. Lane 3 and 4 was HcAPN3G and HcAPN3E control without Cry1Ab35 toxin ligand respectivily. Lane M shows molecular weight markers and arrows indicate the 58 kDa HcAPN3G and 49 kDa HcAPN3E protein bands.
    Figure Legend Snippet: HcAPN3G and HcAPN3E fragment peptides expressed in E.coli BL21 (DE3) cells. HcAPN3G (lane 1) and HcAPN3E (lane 2) peptides expressed in E. coli BL21 (DE3) cells were separated by 10% SDS-PAGE, and either stained with Coomassie Brilliant Blue R-250 ( A ) or transferred to a PVDF membrane and probed by Cry1Ab35 toxin in ligand blot assay ( B ) with anti-Cry1Ab35 antibodies. Lane 3 and 4 was HcAPN3G and HcAPN3E control without Cry1Ab35 toxin ligand respectivily. Lane M shows molecular weight markers and arrows indicate the 58 kDa HcAPN3G and 49 kDa HcAPN3E protein bands.

    Techniques Used: SDS Page, Staining, Molecular Weight

    2) Product Images from "Chemical Characterization of N-Linked Oligosaccharide As the Antigen Epitope Recognized by an Anti-Sperm Auto-Monoclonal Antibody, Ts4"

    Article Title: Chemical Characterization of N-Linked Oligosaccharide As the Antigen Epitope Recognized by an Anti-Sperm Auto-Monoclonal Antibody, Ts4

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0133784

    Reactivity of lectins against proteins in the mouse testicular TS fraction co-immunoprecipitated with Ts4. The immunoprecipitated proteins from testicular TS fraction with either Ts4 or normal control IgM (n.c.) were separated by SDS-PAGE under reducing conditions. Control experiments were conducted under the same conditions except for the absence of the TS fraction (buf). The testicular TS fraction was used as a positive control (IP (-)). Proteins were electroblotted onto PVDF membranes and then probed with E-PHA (A), PSA (B), WGA (C), DSA (D), L-PHA (E), DBA (F), or SJA (G). Arrowheads indicate the lectin-reactive bands corresponding to TEX101. Mr, molecular mass.
    Figure Legend Snippet: Reactivity of lectins against proteins in the mouse testicular TS fraction co-immunoprecipitated with Ts4. The immunoprecipitated proteins from testicular TS fraction with either Ts4 or normal control IgM (n.c.) were separated by SDS-PAGE under reducing conditions. Control experiments were conducted under the same conditions except for the absence of the TS fraction (buf). The testicular TS fraction was used as a positive control (IP (-)). Proteins were electroblotted onto PVDF membranes and then probed with E-PHA (A), PSA (B), WGA (C), DSA (D), L-PHA (E), DBA (F), or SJA (G). Arrowheads indicate the lectin-reactive bands corresponding to TEX101. Mr, molecular mass.

    Techniques Used: Immunoprecipitation, SDS Page, Positive Control, Whole Genome Amplification

    Immunoreactivity of Ts4 against testicular proteins pretreated with periodic acid. The testicular TS fractions (each 5 μg protein) were loaded on a 10% gel, separated by SDS-PAGE under reducing conditions, and then blotted onto a PVDF membrane. The PVDF membrane was divided into individual lanes, which were treated with 0.075 M NaIO 4 and HIO 4 2H 2 O in PBS for various times. Specific bands were detected with Ts4 or 6035 (arrowheads). Mr, molecular mass.
    Figure Legend Snippet: Immunoreactivity of Ts4 against testicular proteins pretreated with periodic acid. The testicular TS fractions (each 5 μg protein) were loaded on a 10% gel, separated by SDS-PAGE under reducing conditions, and then blotted onto a PVDF membrane. The PVDF membrane was divided into individual lanes, which were treated with 0.075 M NaIO 4 and HIO 4 2H 2 O in PBS for various times. Specific bands were detected with Ts4 or 6035 (arrowheads). Mr, molecular mass.

    Techniques Used: SDS Page

    SDS-PAGE analyses of mouse testicular proteins immunoprecipitated with Ts4. Western blot analyses using Ts4 (A). Testicular TS proteins immunoprecipitated with either Ts4 or normal control mouse IgM (n.c.) were separated via SDS-PAGE on 10% gels under reducing conditions. Control experiments were conducted under the same conditions, but in the absence of the testicular extract (buf). Separated proteins were electroblotted onto PVDF membranes and then probed with Ts4. Arrowheads indicate molecular mass (Mr) of the specific immunoreactive bands. Visualized by CBB-staining (B). The same samples were applied to lanes of the 10% SDS-PAGE gel under reducing conditions, and then the gel was CBB-stained. Apparent positions of dominant bands obtained via immunoprecipitation with Ts4 are indicated with arrowheads.
    Figure Legend Snippet: SDS-PAGE analyses of mouse testicular proteins immunoprecipitated with Ts4. Western blot analyses using Ts4 (A). Testicular TS proteins immunoprecipitated with either Ts4 or normal control mouse IgM (n.c.) were separated via SDS-PAGE on 10% gels under reducing conditions. Control experiments were conducted under the same conditions, but in the absence of the testicular extract (buf). Separated proteins were electroblotted onto PVDF membranes and then probed with Ts4. Arrowheads indicate molecular mass (Mr) of the specific immunoreactive bands. Visualized by CBB-staining (B). The same samples were applied to lanes of the 10% SDS-PAGE gel under reducing conditions, and then the gel was CBB-stained. Apparent positions of dominant bands obtained via immunoprecipitation with Ts4 are indicated with arrowheads.

    Techniques Used: SDS Page, Immunoprecipitation, Western Blot, Staining

    3) Product Images from "5-Keto-d-Gluconate Production Is Catalyzed by a Quinoprotein Glycerol Dehydrogenase, Major Polyol Dehydrogenase, in Gluconobacter Species"

    Article Title: 5-Keto-d-Gluconate Production Is Catalyzed by a Quinoprotein Glycerol Dehydrogenase, Major Polyol Dehydrogenase, in Gluconobacter Species

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.69.4.1959-1966.2003

    Immunoblotting analysis of the membrane fractions of G. suboxydans IFO 3257 and 3255 strains and their SLDH disruptants and of the purified ARDH with anti-SLDH. Protein bands in the gel of SDS-PAGE were transferred electrophoretically onto PVDF membrane, and the enzyme band was visualized as described in Materials and Methods. Lane M: prestained marker proteins; lanes 1 to 4: membrane fractions (2 μg of protein each) of G. suboxydans strain 3255, 3255 sldA ::Km, 3275, and 3275 sldA ::Km, respectively; lane 5: ARDH (0.5 μg of protein) purified from G. suboxydans IFO 3257.
    Figure Legend Snippet: Immunoblotting analysis of the membrane fractions of G. suboxydans IFO 3257 and 3255 strains and their SLDH disruptants and of the purified ARDH with anti-SLDH. Protein bands in the gel of SDS-PAGE were transferred electrophoretically onto PVDF membrane, and the enzyme band was visualized as described in Materials and Methods. Lane M: prestained marker proteins; lanes 1 to 4: membrane fractions (2 μg of protein each) of G. suboxydans strain 3255, 3255 sldA ::Km, 3275, and 3275 sldA ::Km, respectively; lane 5: ARDH (0.5 μg of protein) purified from G. suboxydans IFO 3257.

    Techniques Used: Purification, SDS Page, Marker

    4) Product Images from "Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains"

    Article Title: Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkh346

    Identification of the low-weight crosslinking product. Western blot analysis was performed to identify the origin of the low molecular weight crosslinking product of RPA-ABCD. The reaction mixtures contained the photoreactive DNA-30 duplex structure with the ‘long’ FAP-dUMP photoreactive residue (1 µM) and RPA-ABCD (1 µM). Mixtures were preincubated for 20 min at 25°C and were either UV-irradiated (+) or not irradiated (–). Protein samples were then separated on 15% SDS–polyacrylamide gels and either silver stained (lanes 5 and 6 for non-irradiated and irradiated mixtures, respectively) or transferred to a PVDF membrane and visualized with antibodies. Lanes 1 and 3 contained non-irradiated probes, and lanes 2 and 4 contained irradiated probes preadsorbed with monoclonal antibodies specific to p32 and p14, respectively. The positions of protein markers are indicated in the left margin.
    Figure Legend Snippet: Identification of the low-weight crosslinking product. Western blot analysis was performed to identify the origin of the low molecular weight crosslinking product of RPA-ABCD. The reaction mixtures contained the photoreactive DNA-30 duplex structure with the ‘long’ FAP-dUMP photoreactive residue (1 µM) and RPA-ABCD (1 µM). Mixtures were preincubated for 20 min at 25°C and were either UV-irradiated (+) or not irradiated (–). Protein samples were then separated on 15% SDS–polyacrylamide gels and either silver stained (lanes 5 and 6 for non-irradiated and irradiated mixtures, respectively) or transferred to a PVDF membrane and visualized with antibodies. Lanes 1 and 3 contained non-irradiated probes, and lanes 2 and 4 contained irradiated probes preadsorbed with monoclonal antibodies specific to p32 and p14, respectively. The positions of protein markers are indicated in the left margin.

    Techniques Used: Western Blot, Molecular Weight, Recombinase Polymerase Amplification, Irradiation, Staining

    5) Product Images from "Sigma factor 1 in chloroplast gene transcription and photosynthetic light acclimation"

    Article Title: Sigma factor 1 in chloroplast gene transcription and photosynthetic light acclimation

    Journal: Journal of Experimental Botany

    doi: 10.1093/jxb/erz464

    T-DNA insertional mutagenesis decreases SIG1 transcript and protein levels. (A) SIG1 transcript abundance in sig1-1 and sig1-2 mutants as quantified by qRT-PCR. The log2 fold change after normalization with the wild type is shown. Error bars represent ±SE of the mean of four biological replicates. (B) SIG1 protein level as estimated by immunoblotting. Representative SIG1 and actin blots are shown with the corresponding stained PVDF membrane. Both SIG1 and actin are detected on the same membrane. Numbers below each lane denote the ratio of SIG1 to actin band intensity. The percentage decreases in SIG1 relative to the wild-type control are also given. The full uncropped versions of SIG1 and actin immunoblots are given in Supplementary Fig. S5 . (C) An immunoblot of SIG1 with serial dilutions of the wild-type sample. The corresponding stained membrane is also shown. Molecular weight markers are indicated on the left. The mature SIG1 protein has a predicted mol. wt of 54 kDa. The SIG1 protein, however, runs on an 11.5% (w/v) SDS–6 M urea–PAGE gel with an apparent mol. wt of ~49 kDa.
    Figure Legend Snippet: T-DNA insertional mutagenesis decreases SIG1 transcript and protein levels. (A) SIG1 transcript abundance in sig1-1 and sig1-2 mutants as quantified by qRT-PCR. The log2 fold change after normalization with the wild type is shown. Error bars represent ±SE of the mean of four biological replicates. (B) SIG1 protein level as estimated by immunoblotting. Representative SIG1 and actin blots are shown with the corresponding stained PVDF membrane. Both SIG1 and actin are detected on the same membrane. Numbers below each lane denote the ratio of SIG1 to actin band intensity. The percentage decreases in SIG1 relative to the wild-type control are also given. The full uncropped versions of SIG1 and actin immunoblots are given in Supplementary Fig. S5 . (C) An immunoblot of SIG1 with serial dilutions of the wild-type sample. The corresponding stained membrane is also shown. Molecular weight markers are indicated on the left. The mature SIG1 protein has a predicted mol. wt of 54 kDa. The SIG1 protein, however, runs on an 11.5% (w/v) SDS–6 M urea–PAGE gel with an apparent mol. wt of ~49 kDa.

    Techniques Used: Mutagenesis, Quantitative RT-PCR, Staining, Western Blot, Molecular Weight, Polyacrylamide Gel Electrophoresis

    6) Product Images from "Photoconductivity of acid exfoliated and flash-light-processed MoS2 films"

    Article Title: Photoconductivity of acid exfoliated and flash-light-processed MoS2 films

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-21688-0

    ( a ) Schematic drawing of experimental procedures. MoS 2 was first exfoliated in a pH 1.0 nitric acid solution and then collected on a PVDF membrane by filtration, followed by flash-light processing and polishing. Gold electrodes with a designed pattern were then deposited onto the film, and the photoresponse was measured under illumination. ( b ) TEM image of exfoliated MoS2 sheets. The insert is the electron diffraction pattern of the flake. ( c ) AFM image of MoS 2 sheets, ( d ) A photograph of exfoliated MoS 2 after two months of settling and the UV/Vis absorbance of exfoliated MoS 2 in water. Low ( e ) and high ( f ) magnification SEM images of MoS 2 film deposited onto a PVDF membrane after flash-light processing and polishing. ( g ) Cross-section SEM image of MoS 2 film.
    Figure Legend Snippet: ( a ) Schematic drawing of experimental procedures. MoS 2 was first exfoliated in a pH 1.0 nitric acid solution and then collected on a PVDF membrane by filtration, followed by flash-light processing and polishing. Gold electrodes with a designed pattern were then deposited onto the film, and the photoresponse was measured under illumination. ( b ) TEM image of exfoliated MoS2 sheets. The insert is the electron diffraction pattern of the flake. ( c ) AFM image of MoS 2 sheets, ( d ) A photograph of exfoliated MoS 2 after two months of settling and the UV/Vis absorbance of exfoliated MoS 2 in water. Low ( e ) and high ( f ) magnification SEM images of MoS 2 film deposited onto a PVDF membrane after flash-light processing and polishing. ( g ) Cross-section SEM image of MoS 2 film.

    Techniques Used: Filtration, Transmission Electron Microscopy

    7) Product Images from "ADP-Ribosylation Factor 6 Expression and Activation Are Reduced in Myometrium in Complicated Pregnancies"

    Article Title: ADP-Ribosylation Factor 6 Expression and Activation Are Reduced in Myometrium in Complicated Pregnancies

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0037954

    Expression of ARF1, ARF6 and CYTH3 proteins in human myometrium. A. Immunoblot analysis of the expression of ARF6, ARF1, CYTH1-4 and tubulin proteins in human placenta and myometrium. Lanes 1, Placental lysate, and 2, NP myometrium lysate. Immunoblot analysis of ARF6 and ARF6 (B) and CYTH1-4. (C) protein expression in human myometrium of NP, NIL, SL, NP-SL and PT-NIL. The tissue lysate proteins (50 µg) were separated by SDS-PAGE, blotted onto PVDF membranes, and probed with the indicated antibody (i). The lysate of MDA-MB-231 cells was used as a positive control (+ve) where indicated. The intensity of the bands was quantified by densitometric scanning. The data were normalised to the amount of tubulin in each sample and shown as means ± SE of 4 samples in the bottom graph (ii).
    Figure Legend Snippet: Expression of ARF1, ARF6 and CYTH3 proteins in human myometrium. A. Immunoblot analysis of the expression of ARF6, ARF1, CYTH1-4 and tubulin proteins in human placenta and myometrium. Lanes 1, Placental lysate, and 2, NP myometrium lysate. Immunoblot analysis of ARF6 and ARF6 (B) and CYTH1-4. (C) protein expression in human myometrium of NP, NIL, SL, NP-SL and PT-NIL. The tissue lysate proteins (50 µg) were separated by SDS-PAGE, blotted onto PVDF membranes, and probed with the indicated antibody (i). The lysate of MDA-MB-231 cells was used as a positive control (+ve) where indicated. The intensity of the bands was quantified by densitometric scanning. The data were normalised to the amount of tubulin in each sample and shown as means ± SE of 4 samples in the bottom graph (ii).

    Techniques Used: Expressing, SDS Page, Multiple Displacement Amplification, Positive Control

    8) Product Images from "2,4-Dichlorophenoxyacetic acid promotes S-nitrosylation and oxidation of actin affecting cytoskeleton and peroxisomal dynamics"

    Article Title: 2,4-Dichlorophenoxyacetic acid promotes S-nitrosylation and oxidation of actin affecting cytoskeleton and peroxisomal dynamics

    Journal: Journal of Experimental Botany

    doi: 10.1093/jxb/eru237

    Analysis of post-translational modifications of actin by carbonylation and S -nitrosylation. (A) Detection of carbonylated actin. Proteins from leaf extracts (500 μg) were derivatized with DNPH and immunoprecipitated with anti-DNP-IPA as indicated in the Materials and methods. Oxidized-purified proteins (10 μl) were subjected to SDS–PAGE, transferred onto PVDF membranes, and analysed with an anti-actin antibody. The figure is representative of four independent experiments. (B) Detection of S -nitrosylated actin. S -Nitrosylated proteins were labelled with biotin and immunopurified with anti-biotin–IPA, separated by SDS–PAGE, and the actin was identify by western blot analysis using an anti-actin antibody. The figure is representative of three independent experiments.
    Figure Legend Snippet: Analysis of post-translational modifications of actin by carbonylation and S -nitrosylation. (A) Detection of carbonylated actin. Proteins from leaf extracts (500 μg) were derivatized with DNPH and immunoprecipitated with anti-DNP-IPA as indicated in the Materials and methods. Oxidized-purified proteins (10 μl) were subjected to SDS–PAGE, transferred onto PVDF membranes, and analysed with an anti-actin antibody. The figure is representative of four independent experiments. (B) Detection of S -nitrosylated actin. S -Nitrosylated proteins were labelled with biotin and immunopurified with anti-biotin–IPA, separated by SDS–PAGE, and the actin was identify by western blot analysis using an anti-actin antibody. The figure is representative of three independent experiments.

    Techniques Used: Immunoprecipitation, Indirect Immunoperoxidase Assay, Purification, SDS Page, Western Blot

    9) Product Images from "Scavenger receptor-C acts as a receptor for Bacillus thuringiensis vegetative insecticidal protein Vip3Aa and mediates the internalization of Vip3Aa via endocytosis"

    Article Title: Scavenger receptor-C acts as a receptor for Bacillus thuringiensis vegetative insecticidal protein Vip3Aa and mediates the internalization of Vip3Aa via endocytosis

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1007347

    Vip3Aa interacts with Sf-SR-C in vitr o. (A) Confocal microscopy images of Sf9 cells treated with RFP or Vip3Aa-RFP (10 μg/mL) for 3 h. Nuclei are stained with DAPI (blue) and cell membrane are stained with FITC-phalloidin (green). Scale bar, 10 μm. (B) Bio-Vip3Aa was incubated with the extracts of Sf9 cell membrane proteins, immunoprecipitated with Streptavidin Mag Sepharose, and detected by Coomassie brilliant blue staining. (a): Lane 1, biotin labeled Vip3Aa; lane 2, the immune complexes. (b): Image of the band of Vip3Aa that was excised from lane 2. (C) The purified GST-Sf-SR-N and GST protein. (D) Vip3Aa-Flag or Cry1Ac were mixed with purified GST-Sf-SR-N, and then the associated complex was pulled down using GST-Sepharose affinity beads followed by immunoblotting (IB) with an anti-Flag antibody or anti-Cry1Ac antibody. (E) MST assay to measure the binding between Vip3Aa and GST-SR-C-N. The labelled Vip3Aa was kept constant at 10 nM, and the GST-SR-C-N is titrated from 0.3 nM to 10 μM. Fitted binding curves and Kd values (mean ± SD) were derived from three independent experiments. (F) Sf9 cells were transiently transfected with the plasmid pIZT-SR-C and the empty vector pIZT/V5-His respectively. 48 h after transfection, cells were collected for immunoblotting with anti-V5 antibody. (G) Sf9-pIZT-SR-C cells lysate was incubated with Vip3Aa-Flag or Cry1Ac, Sf-SR-C in the cells lysate was immunoprecipitated (IP) with anti-V5 antibody, Vip3Aa-Flag and Cry1Ac in the elution was detected by immunoblotting with anti-Flag antibody and anti-Cry1Ac antibody respectively. (H) The lysate of Sf9-pIZT-SR-C cells were subjected to SDS-PAGE, and then transferred to PVDF membranes. The PVDF membranes were probed with Vip3Aa-flag or with Vip3Aa-flag plus unlabeled Vip3Aa without Flag-tag (200-fold), followed by immunoblotting with an anti-Flag antibody.
    Figure Legend Snippet: Vip3Aa interacts with Sf-SR-C in vitr o. (A) Confocal microscopy images of Sf9 cells treated with RFP or Vip3Aa-RFP (10 μg/mL) for 3 h. Nuclei are stained with DAPI (blue) and cell membrane are stained with FITC-phalloidin (green). Scale bar, 10 μm. (B) Bio-Vip3Aa was incubated with the extracts of Sf9 cell membrane proteins, immunoprecipitated with Streptavidin Mag Sepharose, and detected by Coomassie brilliant blue staining. (a): Lane 1, biotin labeled Vip3Aa; lane 2, the immune complexes. (b): Image of the band of Vip3Aa that was excised from lane 2. (C) The purified GST-Sf-SR-N and GST protein. (D) Vip3Aa-Flag or Cry1Ac were mixed with purified GST-Sf-SR-N, and then the associated complex was pulled down using GST-Sepharose affinity beads followed by immunoblotting (IB) with an anti-Flag antibody or anti-Cry1Ac antibody. (E) MST assay to measure the binding between Vip3Aa and GST-SR-C-N. The labelled Vip3Aa was kept constant at 10 nM, and the GST-SR-C-N is titrated from 0.3 nM to 10 μM. Fitted binding curves and Kd values (mean ± SD) were derived from three independent experiments. (F) Sf9 cells were transiently transfected with the plasmid pIZT-SR-C and the empty vector pIZT/V5-His respectively. 48 h after transfection, cells were collected for immunoblotting with anti-V5 antibody. (G) Sf9-pIZT-SR-C cells lysate was incubated with Vip3Aa-Flag or Cry1Ac, Sf-SR-C in the cells lysate was immunoprecipitated (IP) with anti-V5 antibody, Vip3Aa-Flag and Cry1Ac in the elution was detected by immunoblotting with anti-Flag antibody and anti-Cry1Ac antibody respectively. (H) The lysate of Sf9-pIZT-SR-C cells were subjected to SDS-PAGE, and then transferred to PVDF membranes. The PVDF membranes were probed with Vip3Aa-flag or with Vip3Aa-flag plus unlabeled Vip3Aa without Flag-tag (200-fold), followed by immunoblotting with an anti-Flag antibody.

    Techniques Used: Confocal Microscopy, Staining, Incubation, Immunoprecipitation, Labeling, Purification, Microscale Thermophoresis, Binding Assay, Derivative Assay, Transfection, Plasmid Preparation, SDS Page, FLAG-tag

    10) Product Images from "Novel DNA Aptamers for Parkinson’s Disease Treatment Inhibit α-Synuclein Aggregation and Facilitate its Degradation"

    Article Title: Novel DNA Aptamers for Parkinson’s Disease Treatment Inhibit α-Synuclein Aggregation and Facilitate its Degradation

    Journal: Molecular Therapy. Nucleic Acids

    doi: 10.1016/j.omtn.2018.02.011

    The Aptamers of F5R1 and F5R2 Enhanced Lysosomal Degradation of α-syn and Rescued the Cell Defects (A) SK-N-SH cells pre-treated with F5R1, F5R2 or random DNA sequence were transfected the α-syn or vector control vectors and incubated for 24 hr. The extracts were separated by SDS-PAGE and blotted onto PVDF membrane. The membrane was blocked and probed with the α-syn specific polyclonal antibody. β-actin served as the loading control. (B) Quantitative analysis of the total protein level of α-syn from (A). (C) SK-N-SH cells were similarly treated as in (A) except for incubation time (48 hr). The cell extracts were immunoblotted with the α-syn polyclonal antibody. β-actin served as the loading control. (D) Quantitative analysis of the total protein level of α-syn from (C). Data are presented as the mean ± SD (one-way ANOVA) ***p
    Figure Legend Snippet: The Aptamers of F5R1 and F5R2 Enhanced Lysosomal Degradation of α-syn and Rescued the Cell Defects (A) SK-N-SH cells pre-treated with F5R1, F5R2 or random DNA sequence were transfected the α-syn or vector control vectors and incubated for 24 hr. The extracts were separated by SDS-PAGE and blotted onto PVDF membrane. The membrane was blocked and probed with the α-syn specific polyclonal antibody. β-actin served as the loading control. (B) Quantitative analysis of the total protein level of α-syn from (A). (C) SK-N-SH cells were similarly treated as in (A) except for incubation time (48 hr). The cell extracts were immunoblotted with the α-syn polyclonal antibody. β-actin served as the loading control. (D) Quantitative analysis of the total protein level of α-syn from (C). Data are presented as the mean ± SD (one-way ANOVA) ***p

    Techniques Used: Sequencing, Transfection, Plasmid Preparation, Incubation, SDS Page

    11) Product Images from "Salmonella enterotoxin (Stn) regulates membrane composition and integrity"

    Article Title: Salmonella enterotoxin (Stn) regulates membrane composition and integrity

    Journal: Disease Models & Mechanisms

    doi: 10.1242/dmm.009324

    Interaction between Stn and OmpA. OmpA (1 μg/reaction) was separated by SDS-PAGE and transferred to PVDF membranes, which were soaked in the presence of purified TF-tag (10 μg; A) or purified TF-Stn (10 μg; B), and also in the absence of probe (C) at 4°C for 16 hours. Interaction of TF-Stn and OmpA was detected with anti-TF antibody. Asterisks indicate the non-specific signals with anti-TF antibody and arrow is the specific signal that formed as a result of the OmpA-Stn complex. Panel C was performed as a control reaction for the verification of antibody quality. TF, trigger factor-tag used as a negative control.
    Figure Legend Snippet: Interaction between Stn and OmpA. OmpA (1 μg/reaction) was separated by SDS-PAGE and transferred to PVDF membranes, which were soaked in the presence of purified TF-tag (10 μg; A) or purified TF-Stn (10 μg; B), and also in the absence of probe (C) at 4°C for 16 hours. Interaction of TF-Stn and OmpA was detected with anti-TF antibody. Asterisks indicate the non-specific signals with anti-TF antibody and arrow is the specific signal that formed as a result of the OmpA-Stn complex. Panel C was performed as a control reaction for the verification of antibody quality. TF, trigger factor-tag used as a negative control.

    Techniques Used: SDS Page, Purification, Negative Control

    12) Product Images from "Scavenger receptor-C acts as a receptor for Bacillus thuringiensis vegetative insecticidal protein Vip3Aa and mediates the internalization of Vip3Aa via endocytosis"

    Article Title: Scavenger receptor-C acts as a receptor for Bacillus thuringiensis vegetative insecticidal protein Vip3Aa and mediates the internalization of Vip3Aa via endocytosis

    Journal: PLoS Pathogens

    doi: 10.1371/journal.ppat.1007347

    Vip3Aa interacts with Sf-SR-C in vitr o. (A) Confocal microscopy images of Sf9 cells treated with RFP or Vip3Aa-RFP (10 μg/mL) for 3 h. Nuclei are stained with DAPI (blue) and cell membrane are stained with FITC-phalloidin (green). Scale bar, 10 μm. (B) Bio-Vip3Aa was incubated with the extracts of Sf9 cell membrane proteins, immunoprecipitated with Streptavidin Mag Sepharose, and detected by Coomassie brilliant blue staining. (a): Lane 1, biotin labeled Vip3Aa; lane 2, the immune complexes. (b): Image of the band of Vip3Aa that was excised from lane 2. (C) The purified GST-Sf-SR-N and GST protein. (D) Vip3Aa-Flag or Cry1Ac were mixed with purified GST-Sf-SR-N, and then the associated complex was pulled down using GST-Sepharose affinity beads followed by immunoblotting (IB) with an anti-Flag antibody or anti-Cry1Ac antibody. (E) MST assay to measure the binding between Vip3Aa and GST-SR-C-N. The labelled Vip3Aa was kept constant at 10 nM, and the GST-SR-C-N is titrated from 0.3 nM to 10 μM. Fitted binding curves and Kd values (mean ± SD) were derived from three independent experiments. (F) Sf9 cells were transiently transfected with the plasmid pIZT-SR-C and the empty vector pIZT/V5-His respectively. 48 h after transfection, cells were collected for immunoblotting with anti-V5 antibody. (G) Sf9-pIZT-SR-C cells lysate was incubated with Vip3Aa-Flag or Cry1Ac, Sf-SR-C in the cells lysate was immunoprecipitated (IP) with anti-V5 antibody, Vip3Aa-Flag and Cry1Ac in the elution was detected by immunoblotting with anti-Flag antibody and anti-Cry1Ac antibody respectively. (H) The lysate of Sf9-pIZT-SR-C cells were subjected to SDS-PAGE, and then transferred to PVDF membranes. The PVDF membranes were probed with Vip3Aa-flag or with Vip3Aa-flag plus unlabeled Vip3Aa without Flag-tag (200-fold), followed by immunoblotting with an anti-Flag antibody.
    Figure Legend Snippet: Vip3Aa interacts with Sf-SR-C in vitr o. (A) Confocal microscopy images of Sf9 cells treated with RFP or Vip3Aa-RFP (10 μg/mL) for 3 h. Nuclei are stained with DAPI (blue) and cell membrane are stained with FITC-phalloidin (green). Scale bar, 10 μm. (B) Bio-Vip3Aa was incubated with the extracts of Sf9 cell membrane proteins, immunoprecipitated with Streptavidin Mag Sepharose, and detected by Coomassie brilliant blue staining. (a): Lane 1, biotin labeled Vip3Aa; lane 2, the immune complexes. (b): Image of the band of Vip3Aa that was excised from lane 2. (C) The purified GST-Sf-SR-N and GST protein. (D) Vip3Aa-Flag or Cry1Ac were mixed with purified GST-Sf-SR-N, and then the associated complex was pulled down using GST-Sepharose affinity beads followed by immunoblotting (IB) with an anti-Flag antibody or anti-Cry1Ac antibody. (E) MST assay to measure the binding between Vip3Aa and GST-SR-C-N. The labelled Vip3Aa was kept constant at 10 nM, and the GST-SR-C-N is titrated from 0.3 nM to 10 μM. Fitted binding curves and Kd values (mean ± SD) were derived from three independent experiments. (F) Sf9 cells were transiently transfected with the plasmid pIZT-SR-C and the empty vector pIZT/V5-His respectively. 48 h after transfection, cells were collected for immunoblotting with anti-V5 antibody. (G) Sf9-pIZT-SR-C cells lysate was incubated with Vip3Aa-Flag or Cry1Ac, Sf-SR-C in the cells lysate was immunoprecipitated (IP) with anti-V5 antibody, Vip3Aa-Flag and Cry1Ac in the elution was detected by immunoblotting with anti-Flag antibody and anti-Cry1Ac antibody respectively. (H) The lysate of Sf9-pIZT-SR-C cells were subjected to SDS-PAGE, and then transferred to PVDF membranes. The PVDF membranes were probed with Vip3Aa-flag or with Vip3Aa-flag plus unlabeled Vip3Aa without Flag-tag (200-fold), followed by immunoblotting with an anti-Flag antibody.

    Techniques Used: Confocal Microscopy, Staining, Incubation, Immunoprecipitation, Labeling, Purification, Microscale Thermophoresis, Binding Assay, Derivative Assay, Transfection, Plasmid Preparation, SDS Page, FLAG-tag

    13) Product Images from "Marburg virus-like particles by co-expression of glycoprotein and matrix protein in insect cells induces immune responses in mice"

    Article Title: Marburg virus-like particles by co-expression of glycoprotein and matrix protein in insect cells induces immune responses in mice

    Journal: Virology Journal

    doi: 10.1186/s12985-017-0869-3

    Western blot analysis of GP and VP40 protein expression in the MARV VLPs. 10 μg of MARV VLPs by co-expression of GP and VP40 were mixed with reducing (with β-mercaptoethanol) protein sample buffer, heated at 95 °C for 5 min, and then subjected to 10% SDS-PAGE with different gels. Two different gels were transferred onto a polyvinylidene fluoride (PVDF) membrane for the Western blot analysis, respectively. a GP was incubated with mouse anti-MARV GP polyclonal antibody (control, lane 1; MARV VLPs, lane 2) and the molecular weight were approximately 150KD. b VP40 proteins was incubated with mouse anti-MARV VP40 polyclonal antibody (MARV VLPs, lane 1; control, lane 2) and the molecular weight were approximately 38KD
    Figure Legend Snippet: Western blot analysis of GP and VP40 protein expression in the MARV VLPs. 10 μg of MARV VLPs by co-expression of GP and VP40 were mixed with reducing (with β-mercaptoethanol) protein sample buffer, heated at 95 °C for 5 min, and then subjected to 10% SDS-PAGE with different gels. Two different gels were transferred onto a polyvinylidene fluoride (PVDF) membrane for the Western blot analysis, respectively. a GP was incubated with mouse anti-MARV GP polyclonal antibody (control, lane 1; MARV VLPs, lane 2) and the molecular weight were approximately 150KD. b VP40 proteins was incubated with mouse anti-MARV VP40 polyclonal antibody (MARV VLPs, lane 1; control, lane 2) and the molecular weight were approximately 38KD

    Techniques Used: Western Blot, Expressing, SDS Page, Incubation, Molecular Weight

    Western blot analysis of GP and VP40 protein expression in the purified MARV VLPs. 10 μg of the purified MARV VLPs were mixed with reducing (with β-mercaptoethanol) protein sample buffer, heated at 95 °C for 5 min, and then subjected to 10% SDS-PAGE with different gels. Two different gels were transferred onto a polyvinylidene fluoride (PVDF) membrane for the Western blot analysis, respectively. a GP was incubated with mouse anti-MARV GP polyclonal antibody (purified MARV VLPs, lane 1; control, lane 2). b VP40 proteins was incubated with mouse anti-MARV VP40 polyclonal antibody (purified MARV VLPs, lane 1; control, lane 2)
    Figure Legend Snippet: Western blot analysis of GP and VP40 protein expression in the purified MARV VLPs. 10 μg of the purified MARV VLPs were mixed with reducing (with β-mercaptoethanol) protein sample buffer, heated at 95 °C for 5 min, and then subjected to 10% SDS-PAGE with different gels. Two different gels were transferred onto a polyvinylidene fluoride (PVDF) membrane for the Western blot analysis, respectively. a GP was incubated with mouse anti-MARV GP polyclonal antibody (purified MARV VLPs, lane 1; control, lane 2). b VP40 proteins was incubated with mouse anti-MARV VP40 polyclonal antibody (purified MARV VLPs, lane 1; control, lane 2)

    Techniques Used: Western Blot, Expressing, Purification, SDS Page, Incubation

    14) Product Images from "Novel DNA Aptamers for Parkinson’s Disease Treatment Inhibit α-Synuclein Aggregation and Facilitate its Degradation"

    Article Title: Novel DNA Aptamers for Parkinson’s Disease Treatment Inhibit α-Synuclein Aggregation and Facilitate its Degradation

    Journal: Molecular Therapy. Nucleic Acids

    doi: 10.1016/j.omtn.2018.02.011

    The Aptamers of F5R1 and F5R2 Enhanced Lysosomal Degradation of α-syn and Rescued the Cell Defects (A) SK-N-SH cells pre-treated with F5R1, F5R2 or random DNA sequence were transfected the α-syn or vector control vectors and incubated for 24 hr. The extracts were separated by SDS-PAGE and blotted onto PVDF membrane. The membrane was blocked and probed with the α-syn specific polyclonal antibody. β-actin served as the loading control. (B) Quantitative analysis of the total protein level of α-syn from (A). (C) SK-N-SH cells were similarly treated as in (A) except for incubation time (48 hr). The cell extracts were immunoblotted with the α-syn polyclonal antibody. β-actin served as the loading control. (D) Quantitative analysis of the total protein level of α-syn from (C). Data are presented as the mean ± SD (one-way ANOVA) ***p
    Figure Legend Snippet: The Aptamers of F5R1 and F5R2 Enhanced Lysosomal Degradation of α-syn and Rescued the Cell Defects (A) SK-N-SH cells pre-treated with F5R1, F5R2 or random DNA sequence were transfected the α-syn or vector control vectors and incubated for 24 hr. The extracts were separated by SDS-PAGE and blotted onto PVDF membrane. The membrane was blocked and probed with the α-syn specific polyclonal antibody. β-actin served as the loading control. (B) Quantitative analysis of the total protein level of α-syn from (A). (C) SK-N-SH cells were similarly treated as in (A) except for incubation time (48 hr). The cell extracts were immunoblotted with the α-syn polyclonal antibody. β-actin served as the loading control. (D) Quantitative analysis of the total protein level of α-syn from (C). Data are presented as the mean ± SD (one-way ANOVA) ***p

    Techniques Used: Sequencing, Transfection, Plasmid Preparation, Incubation, SDS Page

    15) Product Images from "Cell Membrane Expression of Cardiac Sodium Channel Nav1.5 Is Modulated by ?-Actinin-2 Interaction †"

    Article Title: Cell Membrane Expression of Cardiac Sodium Channel Nav1.5 Is Modulated by ?-Actinin-2 Interaction †

    Journal: Biochemistry

    doi: 10.1021/bi901086v

    α-Actinin-2 and Na v 1.5/LIII–IV interacted in vitro . (A) Blot overlay assay showing the in vitro interaction of α-actinin-2 with the His 6 -LIII–IV fusion protein. Increasing amounts (15, 25, and 45 µg) of cDNA encoding α-actinin-2 transiently expressed in tsA201 cells were separated by SDS–PAGE and transferred to PVDF membranes. The blots were used to detect the expression of α-actinin-2 proteins (whole cell extracts, bottom panel) or were incubated with either 1 µg/mL purified LIII–IV fusion protein (overlay assay, top panel) or 1 µg/mL BSA (negative control, middle panel) followed by anti-LIII–IV (top and middle panels) or anti-α-actinin-2 antibody (bottom panel). The LIII–IV fusion protein bound specifically to α-actinin-2 in a dose-dependent manner (top panel, lanes 1–3). No binding was detected in the control lane containing extracts from untransfected tsA201 cells (top panel, lane 4) or in the blot incubated with BSA (middle panel). (B) A His pulldown experiment was performed as described in Materials and Methods. tsA201 cell extracts transiently expressing α-actinin-2 were incubated with either His 6 -LIII–IV fusion protein prebound to Ni 2+ -NTA beads or Ni 2+ -NTA beads alone (negative control). After being extensively washed, bound proteins were eluted and separated via 10% SDS–PAGE which were then blotted with anti-α-actinin-2 antibody (top panel) or anti-LIII–IV antibody (bottom panel): lanes 1 and 2, extract starting material; lane 3, His 6 -LIII–IV fusion protein retained from extract; and lane 4, Ni 2+ -NTA beads alone (negative control). The asterisk indicates that the band detected in lane 3 may be a degradation product of the His 6 -LIII–IV fusion protein. These experiments were repeated four times with similar results.
    Figure Legend Snippet: α-Actinin-2 and Na v 1.5/LIII–IV interacted in vitro . (A) Blot overlay assay showing the in vitro interaction of α-actinin-2 with the His 6 -LIII–IV fusion protein. Increasing amounts (15, 25, and 45 µg) of cDNA encoding α-actinin-2 transiently expressed in tsA201 cells were separated by SDS–PAGE and transferred to PVDF membranes. The blots were used to detect the expression of α-actinin-2 proteins (whole cell extracts, bottom panel) or were incubated with either 1 µg/mL purified LIII–IV fusion protein (overlay assay, top panel) or 1 µg/mL BSA (negative control, middle panel) followed by anti-LIII–IV (top and middle panels) or anti-α-actinin-2 antibody (bottom panel). The LIII–IV fusion protein bound specifically to α-actinin-2 in a dose-dependent manner (top panel, lanes 1–3). No binding was detected in the control lane containing extracts from untransfected tsA201 cells (top panel, lane 4) or in the blot incubated with BSA (middle panel). (B) A His pulldown experiment was performed as described in Materials and Methods. tsA201 cell extracts transiently expressing α-actinin-2 were incubated with either His 6 -LIII–IV fusion protein prebound to Ni 2+ -NTA beads or Ni 2+ -NTA beads alone (negative control). After being extensively washed, bound proteins were eluted and separated via 10% SDS–PAGE which were then blotted with anti-α-actinin-2 antibody (top panel) or anti-LIII–IV antibody (bottom panel): lanes 1 and 2, extract starting material; lane 3, His 6 -LIII–IV fusion protein retained from extract; and lane 4, Ni 2+ -NTA beads alone (negative control). The asterisk indicates that the band detected in lane 3 may be a degradation product of the His 6 -LIII–IV fusion protein. These experiments were repeated four times with similar results.

    Techniques Used: In Vitro, Overlay Assay, SDS Page, Expressing, Incubation, Purification, Negative Control, Binding Assay

    16) Product Images from "Photoconductivity of acid exfoliated and flash-light-processed MoS2 films"

    Article Title: Photoconductivity of acid exfoliated and flash-light-processed MoS2 films

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-21688-0

    ( a ) Schematic drawing of experimental procedures. MoS 2 was first exfoliated in a pH 1.0 nitric acid solution and then collected on a PVDF membrane by filtration, followed by flash-light processing and polishing. Gold electrodes with a designed pattern were then deposited onto the film, and the photoresponse was measured under illumination. ( b ) TEM image of exfoliated MoS2 sheets. The insert is the electron diffraction pattern of the flake. ( c ) AFM image of MoS 2 sheets, ( d ) A photograph of exfoliated MoS 2 after two months of settling and the UV/Vis absorbance of exfoliated MoS 2 in water. Low ( e ) and high ( f ) magnification SEM images of MoS 2 film deposited onto a PVDF membrane after flash-light processing and polishing. ( g ) Cross-section SEM image of MoS 2 film.
    Figure Legend Snippet: ( a ) Schematic drawing of experimental procedures. MoS 2 was first exfoliated in a pH 1.0 nitric acid solution and then collected on a PVDF membrane by filtration, followed by flash-light processing and polishing. Gold electrodes with a designed pattern were then deposited onto the film, and the photoresponse was measured under illumination. ( b ) TEM image of exfoliated MoS2 sheets. The insert is the electron diffraction pattern of the flake. ( c ) AFM image of MoS 2 sheets, ( d ) A photograph of exfoliated MoS 2 after two months of settling and the UV/Vis absorbance of exfoliated MoS 2 in water. Low ( e ) and high ( f ) magnification SEM images of MoS 2 film deposited onto a PVDF membrane after flash-light processing and polishing. ( g ) Cross-section SEM image of MoS 2 film.

    Techniques Used: Filtration, Transmission Electron Microscopy

    17) Product Images from "Investigation of Copper Cysteamine Nanoparticles as a New Type of Radiosensitiers for Colorectal Carcinoma Treatment"

    Article Title: Investigation of Copper Cysteamine Nanoparticles as a New Type of Radiosensitiers for Colorectal Carcinoma Treatment

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-09375-y

    The protein expression levels of Bax, Bcl-2, LC3B, and P62 was detected by western blot analysis. SW620 cells were seeded into a 6-well plate at a density of 5 × 10 5 cells per well, cultured overnight and treated with or without Cu-Cy-PDT. The cells were lysed for 30 minutes in 1 × RIPA buffer that contained protease and phosphatase inhibitors. Samples containing equal amounts of protein (25 μg) were resolved on SDS-PAGE in a 10–15% gel and then transferred to a polyvinylidene fluoride (PVDF) membrane (Millipore, Billerica, MA, USA). The membrane was then blocked in 5% non-fat milk for 2 h at room temperature, incubated with primary antibody Bax, Bcl-2, ATG7, LC3B, and Actin antibody (Cell Signaling, Danvers, MA, USA) overnight at 4 °C, washed with TBST, and incubated with a secondary antibody for 2 h at room temperature. The immunoblots of the incubated membranes were visualized with an enhanced chemiluminescence (ECL) Kit (CW Bio).
    Figure Legend Snippet: The protein expression levels of Bax, Bcl-2, LC3B, and P62 was detected by western blot analysis. SW620 cells were seeded into a 6-well plate at a density of 5 × 10 5 cells per well, cultured overnight and treated with or without Cu-Cy-PDT. The cells were lysed for 30 minutes in 1 × RIPA buffer that contained protease and phosphatase inhibitors. Samples containing equal amounts of protein (25 μg) were resolved on SDS-PAGE in a 10–15% gel and then transferred to a polyvinylidene fluoride (PVDF) membrane (Millipore, Billerica, MA, USA). The membrane was then blocked in 5% non-fat milk for 2 h at room temperature, incubated with primary antibody Bax, Bcl-2, ATG7, LC3B, and Actin antibody (Cell Signaling, Danvers, MA, USA) overnight at 4 °C, washed with TBST, and incubated with a secondary antibody for 2 h at room temperature. The immunoblots of the incubated membranes were visualized with an enhanced chemiluminescence (ECL) Kit (CW Bio).

    Techniques Used: Expressing, Western Blot, Cell Culture, SDS Page, Incubation

    18) Product Images from "Hepatitis B spliced protein (HBSP) promotes the carcinogenic effects of benzo [alpha] pyrene by interacting with microsomal epoxide hydrolase and enhancing its hydrolysis activity"

    Article Title: Hepatitis B spliced protein (HBSP) promotes the carcinogenic effects of benzo [alpha] pyrene by interacting with microsomal epoxide hydrolase and enhancing its hydrolysis activity

    Journal: BMC Cancer

    doi: 10.1186/1471-2407-14-282

    Effects of HBSP on the proliferation of B [alpha] P- treated Huh- 7 hepatoma cells. (A) HBSP expression in Huh-7/HBSP/B[alpha]P, Huh-7/GFP/B[alpha]P or Huh-7/HBSP. 30 μg of cellular proteins were subjected to 12% SDS-PAGE, transfered to a PVDF membrane, and probed with anti-mEH. β-actin served as a loading control. (B) Detection of BPDE-DNA in Huh-7/HBSP/B[alpha]P, Huh-7/GFP/B[alpha]P or Huh-7/HBSP cells. Cells on sterilized glass coverslips were detected for BPDE-DNA by immunocytochemistry assay. Images were taken at × 400 magnification. (C) Cell proliferation of Huh-7/HBSP/B[alpha]P, Huh-7/GFP/B[alpha]P, Huh-7/HBSP or Huh-7/GFP cells. Cells were seeded in 96-well plates at 2 × 10 3 /well, cell proliferation was determined daily in triplicate for 9 days by BrdU assay. The optical density (OD) was measured at 450 nm using a microplate reader. The analyses were repeated three times, and the results were expressed as mean ± SD.
    Figure Legend Snippet: Effects of HBSP on the proliferation of B [alpha] P- treated Huh- 7 hepatoma cells. (A) HBSP expression in Huh-7/HBSP/B[alpha]P, Huh-7/GFP/B[alpha]P or Huh-7/HBSP. 30 μg of cellular proteins were subjected to 12% SDS-PAGE, transfered to a PVDF membrane, and probed with anti-mEH. β-actin served as a loading control. (B) Detection of BPDE-DNA in Huh-7/HBSP/B[alpha]P, Huh-7/GFP/B[alpha]P or Huh-7/HBSP cells. Cells on sterilized glass coverslips were detected for BPDE-DNA by immunocytochemistry assay. Images were taken at × 400 magnification. (C) Cell proliferation of Huh-7/HBSP/B[alpha]P, Huh-7/GFP/B[alpha]P, Huh-7/HBSP or Huh-7/GFP cells. Cells were seeded in 96-well plates at 2 × 10 3 /well, cell proliferation was determined daily in triplicate for 9 days by BrdU assay. The optical density (OD) was measured at 450 nm using a microplate reader. The analyses were repeated three times, and the results were expressed as mean ± SD.

    Techniques Used: Expressing, SDS Page, Immunocytochemistry, BrdU Staining

    19) Product Images from "The Involvement of Wheat F-Box Protein Gene TaFBA1 in the Oxidative Stress Tolerance of Plants"

    Article Title: The Involvement of Wheat F-Box Protein Gene TaFBA1 in the Oxidative Stress Tolerance of Plants

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0122117

    Expression of TaFBA1 in wheat under MV-induced oxidative stress. Wheat seedlings with one leaf were subjected to 10-μM MV treatments. Seedlings treated with sterile water were chosen as controls. Seedlings were harvested at different time points for analysis. (A) Expression of TaFBA1 at the mRNA transcript level in shoots, as shown by qPCR; tubulin cDNA was used as a control reference; (B) Expression of TaFBA1 at the protein level in shoots as shown by western blot. After 12.5% SDS-PAGE, protein samples were electro-transferred onto a PVDF membrane and probed with the TaFBA1 antibody produced in our laboratory. The Rubisco large subunit was used as a loading control.
    Figure Legend Snippet: Expression of TaFBA1 in wheat under MV-induced oxidative stress. Wheat seedlings with one leaf were subjected to 10-μM MV treatments. Seedlings treated with sterile water were chosen as controls. Seedlings were harvested at different time points for analysis. (A) Expression of TaFBA1 at the mRNA transcript level in shoots, as shown by qPCR; tubulin cDNA was used as a control reference; (B) Expression of TaFBA1 at the protein level in shoots as shown by western blot. After 12.5% SDS-PAGE, protein samples were electro-transferred onto a PVDF membrane and probed with the TaFBA1 antibody produced in our laboratory. The Rubisco large subunit was used as a loading control.

    Techniques Used: Expressing, Real-time Polymerase Chain Reaction, Western Blot, SDS Page, Produced

    20) Product Images from "Phosphorylation of bamboo mosaic virus satellite RNA (satBaMV)-encoded protein P20 downregulates the formation of satBaMV-P20 ribonucleoprotein complex"

    Article Title: Phosphorylation of bamboo mosaic virus satellite RNA (satBaMV)-encoded protein P20 downregulates the formation of satBaMV-P20 ribonucleoprotein complex

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkr705

    Protein interactions of wild-type and mutant rP20. ( A ) Overlay assay. Purified WT, S11A or S11D rP20 was dot-blotted onto a PVDF membrane. After blocking with 1% BSA (w/v) in 140 mM NaCl, 10 mM Tris–HCl, pH 7.4, 2 mM EDTA, 0.1% Tween 20 (v/v) and 2 mM DTT at room temperature, the membrane was overlayed at 4°C with 35 [S]-Met-labeled WT, S11A or S11D translated in vitro. After washing the membrane in Tris-buffered saline buffer containing 0.05% Tween 20 (v/v), protein interactions were detected by autoradiography. Bovine serum albumin was used as a control. ( B ) Glutaraldehyde cross-linking assay. Total protein extracted from N. benthamiana leaves co-infected with BaMV and WT, S11A or S11D satBaMV was cross-linked with 0.025% glutaraldehyde (v/v) for indicated times at 30°C, resolved on 12.5% SDS–PAGE and immunodetected with anti-P20 serum.
    Figure Legend Snippet: Protein interactions of wild-type and mutant rP20. ( A ) Overlay assay. Purified WT, S11A or S11D rP20 was dot-blotted onto a PVDF membrane. After blocking with 1% BSA (w/v) in 140 mM NaCl, 10 mM Tris–HCl, pH 7.4, 2 mM EDTA, 0.1% Tween 20 (v/v) and 2 mM DTT at room temperature, the membrane was overlayed at 4°C with 35 [S]-Met-labeled WT, S11A or S11D translated in vitro. After washing the membrane in Tris-buffered saline buffer containing 0.05% Tween 20 (v/v), protein interactions were detected by autoradiography. Bovine serum albumin was used as a control. ( B ) Glutaraldehyde cross-linking assay. Total protein extracted from N. benthamiana leaves co-infected with BaMV and WT, S11A or S11D satBaMV was cross-linked with 0.025% glutaraldehyde (v/v) for indicated times at 30°C, resolved on 12.5% SDS–PAGE and immunodetected with anti-P20 serum.

    Techniques Used: Mutagenesis, Overlay Assay, Purification, Blocking Assay, Labeling, In Vitro, Autoradiography, Infection, SDS Page

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    Article Title: Role for Arf3p in Development of Polarity, but Not Endocytosis, in Saccharomyces cerevisiae D⃞
    Article Snippet: .. Proteins separated by SDS-PAGE, were transferred electrophoretically to Immobilon-P membranes (Millipore Corp., Bedford, MA), which were then incubated with antibodies in Tris-buffered saline (pH 7.4) containing 0.1% Tween 20 and 5% nonfat dry milk at room temperature for 60 min. ..

    Article Title: VEGF (Vascular Endothelial Growth Factor) Induces NRP1 (Neuropilin-1) Cleavage via ADAMs (a Disintegrin and Metalloproteinase) 9 and 10 to Generate Novel Carboxy-Terminal NRP1 Fragments That Regulate Angiogenic Signaling
    Article Snippet: .. The immunoprecipitated complex was resolved on a 4% to 12% SDS-PAGE gel, transferred as described above and the PVDF membrane was stained with Ponceau S (Sigma). .. All positively stained bands < 25 kDa were sent for automated N-terminal sequencing by Edman degradation to Alta Biosciences, University of Birmingham.

    Article Title: Lipid rafts both in cellular membrane and viral envelope are critical for PRRSV efficient infection
    Article Snippet: .. Western blot analysis Similar amount of volume from each sample was resolved by SDS-PAGE and transferred to polyvinylidene difluoride (PVDF) membranes (Millipore). .. Membranes were blocked with 5% nonfat milk in phosphate-buffered saline with 0.05% Tween 20 (PBST) and incubated for 2 h at room temperature with the primary antibodies at a suitable dilution (anti-Gp3 and –Gp4 at 1:200, anti-CD71 at 1:500, anti-caveolin at 1:1000, anti-N protein at 1:2000, anti-Nsp9 at 1:3000, and anti-Gp5 and –CD163 at 1:5000).

    Article Title: Phosphorylation of Human Immunodeficiency Virus Type 1 Vpr Regulates Cell Cycle Arrest
    Article Snippet: .. To determine the phosphorylated residue(s), the 32 P-labeled Vpr was immunoprecipitated from pcDNA-VPR-transfected HEK293 cells, separated by SDS-PAGE, and transferred to an Immobilon-P membrane to perform PAA. ..

    Article Title: N-terminal entrance loop of yeast Yps1 and O-glycosylation of substrates are determinant factors controlling the shedding activity of this GPI-anchored endopeptidase
    Article Snippet: .. Edman degradation Purified forms of ssYps1-DL or Yps1-DL were fractionated on SDS-PAGE and then transferred to PVDF membranes in 10 mM N -cyclohexyl-3-aminopropanesulfonic acid (CAPS) buffer pH 11 (Sigma). .. The membranes were then stained with 0.1% PhastGel Blue R (GE Healthcare), 40% methanol and 10% acetic acid and destained in 50% methanol.

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  • 99
    Millipore immobilon p membrane
    PAA of Vpr. The 32 P-labeled Vpr was immunoprecipitated from pcDNA-VPR-transfected HEK293 cells, separated by SDS-PAGE, and transferred to an <t>Immobilon-P</t> membrane. The Vpr band was excised and hydrolyzed. The hydrolysate was dried, dissolved in 10 μl of H 2 O containing 0.5 μg each of phosphoserine (p-Ser), phosphothreonine (p-Thr), and phosphotyrosine (p-Tyr), and then spotted onto a cellulose plate to perform PAA. The three phosphoamino acid locations are shown by ovals; the 32 P-phosphoamino acids were revealed by exposure of the plate to a phosphorimager screen.
    Immobilon P Membrane, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 377 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/immobilon p membrane/product/Millipore
    Average 99 stars, based on 377 article reviews
    Price from $9.99 to $1999.99
    immobilon p membrane - by Bioz Stars, 2020-11
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    90
    Millipore membranes flat sheet hydrophilic hpi pvdf mf membranes
    ATR-FTIR absorbance spectra for the top-side of <t>HPI</t> <t>PVDF</t> membranes after dead-end filtration and subsequent hydraulic cleaning. Lines (bottom to top) represent a clean, slightly fouled (2‒1 mg-O 3 mg-C −1 ), and moderately fouled (0 mg-O 3 mg-C −1 ) membranes. The extent of fouling was determined based on the restoration of membrane permeability after hydraulic cleaning. Spectra were normalized to the highest peak at a wavenumber of 875 cm −1 .
    Membranes Flat Sheet Hydrophilic Hpi Pvdf Mf Membranes, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Millipore elispot plates
    Number of brain MNCs and their CNS antigen-specific autoreactive phenotype 14 d after MCAo. A , Number of MNCs infiltrating ipsilateral and contralateral hemisphere of the brain in vehicle and SNS/HPA blockade group (three individual experiments; vehicle, N = 15; SNS/HPA block, N = 20). B–D , <t>Elispot</t> experiments. B , Higher number of total brain MNCs responded to pMOG 35–55 stimulation with IFN-γ production (Th1 cells) per equal number of brain MNCs in SNS/HPA block group compared with the vehicle group. C , A similar effect was observed in ipsilateral hemisphere MNCs when only the SNS axis of SIDS was blocked with propranolol (two experiments; vehicle group, N = 5–8; SNS block, N = 6 or 7). D , Number of splenocytes reacting to pMOG 35–55 stimulation with IFN-γ, IL-4, or IL-17 secretion did not differ between the groups. E , F , ELISA experiments. TGF-β1, IL-10, IL-4, IL-17, and IFN-γ secretion (pg/ml) by pMOG 35–55 -stimulated brain MNCs, ipsilateral hemisphere ( E ) and by pMOG 35–55 -stimulated splenocytes ( F ).
    Elispot Plates, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 468 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    PAA of Vpr. The 32 P-labeled Vpr was immunoprecipitated from pcDNA-VPR-transfected HEK293 cells, separated by SDS-PAGE, and transferred to an Immobilon-P membrane. The Vpr band was excised and hydrolyzed. The hydrolysate was dried, dissolved in 10 μl of H 2 O containing 0.5 μg each of phosphoserine (p-Ser), phosphothreonine (p-Thr), and phosphotyrosine (p-Tyr), and then spotted onto a cellulose plate to perform PAA. The three phosphoamino acid locations are shown by ovals; the 32 P-phosphoamino acids were revealed by exposure of the plate to a phosphorimager screen.

    Journal: Journal of Virology

    Article Title: Phosphorylation of Human Immunodeficiency Virus Type 1 Vpr Regulates Cell Cycle Arrest

    doi:

    Figure Lengend Snippet: PAA of Vpr. The 32 P-labeled Vpr was immunoprecipitated from pcDNA-VPR-transfected HEK293 cells, separated by SDS-PAGE, and transferred to an Immobilon-P membrane. The Vpr band was excised and hydrolyzed. The hydrolysate was dried, dissolved in 10 μl of H 2 O containing 0.5 μg each of phosphoserine (p-Ser), phosphothreonine (p-Thr), and phosphotyrosine (p-Tyr), and then spotted onto a cellulose plate to perform PAA. The three phosphoamino acid locations are shown by ovals; the 32 P-phosphoamino acids were revealed by exposure of the plate to a phosphorimager screen.

    Article Snippet: To determine the phosphorylated residue(s), the 32 P-labeled Vpr was immunoprecipitated from pcDNA-VPR-transfected HEK293 cells, separated by SDS-PAGE, and transferred to an Immobilon-P membrane to perform PAA.

    Techniques: Labeling, Immunoprecipitation, Transfection, SDS Page

    Trk is rapidly activated in response to neurotrophin stimulation. A , Selective neurotrophin stimulation of DRG neurites results in pTrk immunostaining in neurites and cell bodies of DRG neurons. After a 20 min neurotrophin ( +NT ) or vehicle control (− NT ) (0.1 ng/ml BSA) stimulation at the neurites, DRG neurons were fixed in 4% paraformaldehyde and immunostained using the anti-pTrk antibody in conjunction with a Cy3-conjugated secondary antibody. B , Trk phosphorylation is detected in the cell body as early as 5 min after selective neurotrophin ( +NT ) or vehicle control (− NT ) (0.1 ng/ml BSA) stimulation at the neurites. DRG neuron lysates from the neurites and from the cell bodies were pooled from nine compartmented cultures, separated on 10% SDS-PAGE gel, transferred to Immobilon-P membrane, and immunoblotted with anti-pTrk. C , Time course of Trk phosphorylation at the cell body in response to neurite stimulation. Intensity of the pTrk band was quantitated with the Molecular Dynamics Storm 860 imaging system using Image Quant (version 2.0; Molecular Dynamics) and normalized for protein loading. The time course of pTrk induction (calculated as the ratio between pTrk in neurotrophin- and control-stimulated cultures) was calculated from several experiments ( n = 3–10 for each time point; * p

    Journal: The Journal of Neuroscience

    Article Title: Rapid Nuclear Responses to Target-Derived Neurotrophins Require Retrograde Transport of Ligand–Receptor Complex

    doi: 10.1523/JNEUROSCI.19-18-07889.1999

    Figure Lengend Snippet: Trk is rapidly activated in response to neurotrophin stimulation. A , Selective neurotrophin stimulation of DRG neurites results in pTrk immunostaining in neurites and cell bodies of DRG neurons. After a 20 min neurotrophin ( +NT ) or vehicle control (− NT ) (0.1 ng/ml BSA) stimulation at the neurites, DRG neurons were fixed in 4% paraformaldehyde and immunostained using the anti-pTrk antibody in conjunction with a Cy3-conjugated secondary antibody. B , Trk phosphorylation is detected in the cell body as early as 5 min after selective neurotrophin ( +NT ) or vehicle control (− NT ) (0.1 ng/ml BSA) stimulation at the neurites. DRG neuron lysates from the neurites and from the cell bodies were pooled from nine compartmented cultures, separated on 10% SDS-PAGE gel, transferred to Immobilon-P membrane, and immunoblotted with anti-pTrk. C , Time course of Trk phosphorylation at the cell body in response to neurite stimulation. Intensity of the pTrk band was quantitated with the Molecular Dynamics Storm 860 imaging system using Image Quant (version 2.0; Molecular Dynamics) and normalized for protein loading. The time course of pTrk induction (calculated as the ratio between pTrk in neurotrophin- and control-stimulated cultures) was calculated from several experiments ( n = 3–10 for each time point; * p

    Article Snippet: The protein lysates were size-fractionated through a 10% SDS-acrylamide gel and transferred to Immobilon-P membrane (Millipore, Bedford, MA).

    Techniques: Immunostaining, SDS Page, Imaging

    ATR-FTIR absorbance spectra for the top-side of HPI PVDF membranes after dead-end filtration and subsequent hydraulic cleaning. Lines (bottom to top) represent a clean, slightly fouled (2‒1 mg-O 3 mg-C −1 ), and moderately fouled (0 mg-O 3 mg-C −1 ) membranes. The extent of fouling was determined based on the restoration of membrane permeability after hydraulic cleaning. Spectra were normalized to the highest peak at a wavenumber of 875 cm −1 .

    Journal: Water research

    Article Title: Treatment of reverse osmosis concentrate using an algal-based MBR combined with ozone pretreatment

    doi: 10.1016/j.watres.2019.05.003

    Figure Lengend Snippet: ATR-FTIR absorbance spectra for the top-side of HPI PVDF membranes after dead-end filtration and subsequent hydraulic cleaning. Lines (bottom to top) represent a clean, slightly fouled (2‒1 mg-O 3 mg-C −1 ), and moderately fouled (0 mg-O 3 mg-C −1 ) membranes. The extent of fouling was determined based on the restoration of membrane permeability after hydraulic cleaning. Spectra were normalized to the highest peak at a wavenumber of 875 cm −1 .

    Article Snippet: Membranes Flat-sheet hydrophilic (HPI) PVDF MF membranes (GVWP04700, Durapore, MilliporeSigma, USA) were used for all dead-end filtration tests.

    Techniques: Filtration, Permeability

    Number of brain MNCs and their CNS antigen-specific autoreactive phenotype 14 d after MCAo. A , Number of MNCs infiltrating ipsilateral and contralateral hemisphere of the brain in vehicle and SNS/HPA blockade group (three individual experiments; vehicle, N = 15; SNS/HPA block, N = 20). B–D , Elispot experiments. B , Higher number of total brain MNCs responded to pMOG 35–55 stimulation with IFN-γ production (Th1 cells) per equal number of brain MNCs in SNS/HPA block group compared with the vehicle group. C , A similar effect was observed in ipsilateral hemisphere MNCs when only the SNS axis of SIDS was blocked with propranolol (two experiments; vehicle group, N = 5–8; SNS block, N = 6 or 7). D , Number of splenocytes reacting to pMOG 35–55 stimulation with IFN-γ, IL-4, or IL-17 secretion did not differ between the groups. E , F , ELISA experiments. TGF-β1, IL-10, IL-4, IL-17, and IFN-γ secretion (pg/ml) by pMOG 35–55 -stimulated brain MNCs, ipsilateral hemisphere ( E ) and by pMOG 35–55 -stimulated splenocytes ( F ).

    Journal: The Journal of Neuroscience

    Article Title: Blocking Stroke-Induced Immunodeficiency Increases CNS Antigen-Specific Autoreactivity But Does Not Worsen Functional Outcome after Experimental Stroke

    doi: 10.1523/JNEUROSCI.1532-14.2015

    Figure Lengend Snippet: Number of brain MNCs and their CNS antigen-specific autoreactive phenotype 14 d after MCAo. A , Number of MNCs infiltrating ipsilateral and contralateral hemisphere of the brain in vehicle and SNS/HPA blockade group (three individual experiments; vehicle, N = 15; SNS/HPA block, N = 20). B–D , Elispot experiments. B , Higher number of total brain MNCs responded to pMOG 35–55 stimulation with IFN-γ production (Th1 cells) per equal number of brain MNCs in SNS/HPA block group compared with the vehicle group. C , A similar effect was observed in ipsilateral hemisphere MNCs when only the SNS axis of SIDS was blocked with propranolol (two experiments; vehicle group, N = 5–8; SNS block, N = 6 or 7). D , Number of splenocytes reacting to pMOG 35–55 stimulation with IFN-γ, IL-4, or IL-17 secretion did not differ between the groups. E , F , ELISA experiments. TGF-β1, IL-10, IL-4, IL-17, and IFN-γ secretion (pg/ml) by pMOG 35–55 -stimulated brain MNCs, ipsilateral hemisphere ( E ) and by pMOG 35–55 -stimulated splenocytes ( F ).

    Article Snippet: For this, Elispot plates (96-well plates with hydrophobic PVDF membrane, 0.45 μm pore size; EMD Millipore) were coated overnight with 5 μg/ml of the following: (1) IFN-γ (for Th1 cells; eBioscience, catalog #14-7313-85; RRID:AB_468472); (2) IL-4 (for Th2 cells; BD Biosciences, catalog #551878; RRID:AB_2336921); or (3) IL-17 (for Th17 cells; eBioscience, catalog #16-7175-85; RRID:AB_763573) specific capture antibody in sterile PBS.

    Techniques: Blocking Assay, Enzyme-linked Immunospot, Enzyme-linked Immunosorbent Assay