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  • 99
    Thermo Fisher ficoll 400
    Overview of the shRNA electroporation procedure for H. symbiolongicarpus embryos. One-cell stage embryos are collected in a petri dish and transferred in a small volume of Millipore-filtered seawater (MFSW—blue) into wells of a depression slide. MFSW in each well is removed and replaced by 100 μl of the electroporation solution, consisting of 15% <t>Ficoll-400</t> in MFSW containing the shRNAs (purple). The embryos in the electroporation solution are then transferred into an electroporation cuvette. The cuvette is placed inside the safety stand of the ECM 830 Square wave electroporation system (BTX) and electroporation of the embryos with the chosen parameters is carried out. Electroporated embryos are then carefully transferred to a petri dish with MFSW for their recovery and future phenotypic analyses. A detailed protocol can be found in Supplementary Info S1 .
    Ficoll 400, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 51 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore ficoll 400
    Comparing fluorescence recovery after photobleaching (FRAP), fluorescence correlation spectroscopy (FCS), and single-molecule tracking on BSA-AF647 in 10% Ficoll 400.  (A)  Single-molecule tracking: simplified schematic of the stages in tracking and the resulting fit with shaded regions indicating error bounds of one SD.  (B)  FRAP: schematic of technique, profile of bleached region in an immobilized sample, and example fluorescence intensity recovery trace.  (C)  FCS: schematic of the confocal volume, example section of intensity fluctuation trace, and correlation curve.
    Ficoll 400, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 16469 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ficoll 400/product/Millipore
    Average 99 stars, based on 16469 article reviews
    Price from $9.99 to $1999.99
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    95
    GE Healthcare ficoll 400
    Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% <t>Ficoll</t> 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.
    Ficoll 400, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 95/100, based on 180 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore ficoll pm 400
    Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% <t>Ficoll</t> 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.
    Ficoll Pm 400, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 265 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare 400 kda ficoll
    Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% <t>Ficoll</t> 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.
    400 Kda Ficoll, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Mediatech ficoll 400
    Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% <t>Ficoll</t> 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.
    Ficoll 400, supplied by Mediatech, used in various techniques. Bioz Stars score: 91/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ficoll 400/product/Mediatech
    Average 91 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    ficoll 400 - by Bioz Stars, 2020-09
    91/100 stars
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    91
    Dot Scientific ficoll 400
    Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% <t>Ficoll</t> 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.
    Ficoll 400, supplied by Dot Scientific, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ficoll 400/product/Dot Scientific
    Average 91 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    ficoll 400 - by Bioz Stars, 2020-09
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    91
    Spectrum Chemicals Inc ficoll 400
    In vitro transcription under macromolecular crowding conditions. ( a ) Effect of macromolecular crowding agents, Ficoll-70 (F-70), <t>Ficoll-400</t> (F-400) and PEG-8000 (PEG) on the Rluc mRNA synthesis from the pIVEX1.3-RL template. Transcriptions were incubated for 3 hr; ( b ) Northern blotting analysis of the Rluc mRNA synthesized by in vitro transcription; ( c ) Time course of in vitro transcription under macromolecular crowding conditions emulated by Ficoll-70. The initial velocity of transcription (409, 146 and 94 ng/µl/min for reactions with 20%, 40% and 0% (w/v) Ficoll-70, respectively) was calculated based on the synthesis of mRNA during the period of 0–10 min. In panel a and c , each data point is the mean of triplicate values; error bars indicate the standard deviation from the mean.
    Ficoll 400, supplied by Spectrum Chemicals Inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ficoll 400/product/Spectrum Chemicals Inc
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ficoll 400 - by Bioz Stars, 2020-09
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    Image Search Results


    Overview of the shRNA electroporation procedure for H. symbiolongicarpus embryos. One-cell stage embryos are collected in a petri dish and transferred in a small volume of Millipore-filtered seawater (MFSW—blue) into wells of a depression slide. MFSW in each well is removed and replaced by 100 μl of the electroporation solution, consisting of 15% Ficoll-400 in MFSW containing the shRNAs (purple). The embryos in the electroporation solution are then transferred into an electroporation cuvette. The cuvette is placed inside the safety stand of the ECM 830 Square wave electroporation system (BTX) and electroporation of the embryos with the chosen parameters is carried out. Electroporated embryos are then carefully transferred to a petri dish with MFSW for their recovery and future phenotypic analyses. A detailed protocol can be found in Supplementary Info S1 .

    Journal: Scientific Reports

    Article Title: Gene knockdown via electroporation of short hairpin RNAs in embryos of the marine hydroid Hydractinia symbiolongicarpus

    doi: 10.1038/s41598-020-69489-8

    Figure Lengend Snippet: Overview of the shRNA electroporation procedure for H. symbiolongicarpus embryos. One-cell stage embryos are collected in a petri dish and transferred in a small volume of Millipore-filtered seawater (MFSW—blue) into wells of a depression slide. MFSW in each well is removed and replaced by 100 μl of the electroporation solution, consisting of 15% Ficoll-400 in MFSW containing the shRNAs (purple). The embryos in the electroporation solution are then transferred into an electroporation cuvette. The cuvette is placed inside the safety stand of the ECM 830 Square wave electroporation system (BTX) and electroporation of the embryos with the chosen parameters is carried out. Electroporated embryos are then carefully transferred to a petri dish with MFSW for their recovery and future phenotypic analyses. A detailed protocol can be found in Supplementary Info S1 .

    Article Snippet: For Supplementary Videos and , embryos were electroporated with Dextran (Alexa Fluor 555; Invitrogen) at 1 mg/ml in Ficoll-400 15% MFSW and fixed 3 days post-electroporation in 4%PFA in PTw for 1 h at RT.

    Techniques: shRNA, Electroporation

    Comparing fluorescence recovery after photobleaching (FRAP), fluorescence correlation spectroscopy (FCS), and single-molecule tracking on BSA-AF647 in 10% Ficoll 400.  (A)  Single-molecule tracking: simplified schematic of the stages in tracking and the resulting fit with shaded regions indicating error bounds of one SD.  (B)  FRAP: schematic of technique, profile of bleached region in an immobilized sample, and example fluorescence intensity recovery trace.  (C)  FCS: schematic of the confocal volume, example section of intensity fluctuation trace, and correlation curve.

    Journal: Frontiers in Immunology

    Article Title: High-Speed Single-Molecule Tracking of CXCL13 in the B-Follicle

    doi: 10.3389/fimmu.2018.01073

    Figure Lengend Snippet: Comparing fluorescence recovery after photobleaching (FRAP), fluorescence correlation spectroscopy (FCS), and single-molecule tracking on BSA-AF647 in 10% Ficoll 400. (A) Single-molecule tracking: simplified schematic of the stages in tracking and the resulting fit with shaded regions indicating error bounds of one SD. (B) FRAP: schematic of technique, profile of bleached region in an immobilized sample, and example fluorescence intensity recovery trace. (C) FCS: schematic of the confocal volume, example section of intensity fluctuation trace, and correlation curve.

    Article Snippet: BSA labeled with 3–6 AF647 was purchased from Thermo Fisher Scientific Inc. Ficoll 400 (Sigma-Aldrich) was diluted in PBS at 0.1 g mL−1 to create a 10% solution of viscosity 0.005 Pa s at room temperature ( ).

    Techniques: Fluorescence, Spectroscopy

    Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% Ficoll 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.

    Journal: The Journal of biological chemistry

    Article Title: Apg2 Is a Novel Protein Required for the Cytoplasm to Vacuole Targeting, Autophagy, and Pexophagy Pathways *

    doi: 10.1074/jbc.M102342200

    Figure Lengend Snippet: Analysis of the apg2 Δ strain indicates that Apg2 is required for the vesicle formation/completion step A , precursor Ape1 in the apg2Δ strain is protease-accessible. Spheroplasts isolated from apg2 Δ, apg7 Δ, and ypt7 Δ cells were osmotically lysed (T, total) and centrifuged at 13,000 × g to obtain low-speed supernatant (S) and pellet (P) fractions. The pellet fractions were subjected to protease treatment in the absence or presence of 0.2% Triton X-100 as described under “Experimental Procedures.” B , precursor Ape1 in the apg2 Δ strain accumulated in a membrane-associated float fraction. Spheroplasts from the apg2 Δ strain were osmotically lysed (T, total) and separated into supernatant (S) and pellet (P) fractions by centrifugation at 13,000 × g for 10 min. The pellet fraction was resuspended in 15% Ficoll 400 in the absence or presence of 0.2% Triton X-100, and overlaid with 13 and 2% Ficoll 400 in a step gradient. The gradients were centrifuged at 13,000 × g for 10 min at room temperature. Three fractions were collected including float (F), non-float (NF) and pellet (P2) fractions as described under “Experimental Procedures.” All samples were trichloroacetic acid precipitated, acetone washed twice, resolved by SDS-polyacrylamide gel electrophoresis, and probed by immunoblot with antiserum against Ape1.

    Article Snippet: Ficoll 400 was from Amersham Pharmacia Biotech (Piscataway, NJ).

    Techniques: Isolation, Centrifugation, Polyacrylamide Gel Electrophoresis

    Effect of Ficoll PM 400 on percent cell adherence (A) , percent cells transfected (B), and percent dead cells (D). Plated C3H/10T1/2 cells were incubated with lipoplex (0 or 1 µg plasmid/well) for 6 h. The inclusion of 16.7% (w/w) Ficoll in the W 1 phase of the LLE can increase the percent of cells transfected (D) . LLE emulsion with or without Ficoll was exposed to ultrasound in a separate plate, with the releasate being added to plated cells. * p

    Journal: Advanced healthcare materials

    Article Title: In Situ Transfection by Controlled Release of Lipoplexes using Acoustic Droplet Vaporization

    doi: 10.1002/adhm.201600008

    Figure Lengend Snippet: Effect of Ficoll PM 400 on percent cell adherence (A) , percent cells transfected (B), and percent dead cells (D). Plated C3H/10T1/2 cells were incubated with lipoplex (0 or 1 µg plasmid/well) for 6 h. The inclusion of 16.7% (w/w) Ficoll in the W 1 phase of the LLE can increase the percent of cells transfected (D) . LLE emulsion with or without Ficoll was exposed to ultrasound in a separate plate, with the releasate being added to plated cells. * p

    Article Snippet: The cells were incubated with lipoplex (1 µg pDNA/well) diluted in DMEM containing 0–2% (w/v) Ficoll PM 400 (GE Healthcare, Waukesha, WI, USA) for 6 h. The overlying media was removed and the cells were stained/imaged the following day as stated previously.

    Techniques: Transfection, Incubation, Plasmid Preparation

    In vitro transcription under macromolecular crowding conditions. ( a ) Effect of macromolecular crowding agents, Ficoll-70 (F-70), Ficoll-400 (F-400) and PEG-8000 (PEG) on the Rluc mRNA synthesis from the pIVEX1.3-RL template. Transcriptions were incubated for 3 hr; ( b ) Northern blotting analysis of the Rluc mRNA synthesized by in vitro transcription; ( c ) Time course of in vitro transcription under macromolecular crowding conditions emulated by Ficoll-70. The initial velocity of transcription (409, 146 and 94 ng/µl/min for reactions with 20%, 40% and 0% (w/v) Ficoll-70, respectively) was calculated based on the synthesis of mRNA during the period of 0–10 min. In panel a and c , each data point is the mean of triplicate values; error bars indicate the standard deviation from the mean.

    Journal: PLoS ONE

    Article Title: Cell-Free Protein Expression under Macromolecular Crowding Conditions

    doi: 10.1371/journal.pone.0028707

    Figure Lengend Snippet: In vitro transcription under macromolecular crowding conditions. ( a ) Effect of macromolecular crowding agents, Ficoll-70 (F-70), Ficoll-400 (F-400) and PEG-8000 (PEG) on the Rluc mRNA synthesis from the pIVEX1.3-RL template. Transcriptions were incubated for 3 hr; ( b ) Northern blotting analysis of the Rluc mRNA synthesized by in vitro transcription; ( c ) Time course of in vitro transcription under macromolecular crowding conditions emulated by Ficoll-70. The initial velocity of transcription (409, 146 and 94 ng/µl/min for reactions with 20%, 40% and 0% (w/v) Ficoll-70, respectively) was calculated based on the synthesis of mRNA during the period of 0–10 min. In panel a and c , each data point is the mean of triplicate values; error bars indicate the standard deviation from the mean.

    Article Snippet: Ficoll-70 and Ficoll-400 (molecular weight: ∼70 kDa and ∼400 kDa, respectively) were purchased from Spectrum Chemicals & Laboratory Products (Gardena, CA).

    Techniques: In Vitro, Incubation, Northern Blot, Synthesized, Standard Deviation