m tris acetate  (Millipore)


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    Name:
    TRIS acetate
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    Catalog Number:
    93295
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    Millipore m tris acetate

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    Average 97 stars, based on 4 article reviews
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    Selection:

    Article Title: The phosphite oxidoreductase gene, ptxD as a bio-contained chloroplast marker and crop-protection tool for algal biotechnology using Chlamydomonas
    Article Snippet: .. Direct selection for ptxD transformants was on agar plates containing Tris-acetate medium supplemented with sodium phosphite (Na2 HPO3 ·5H2 O, 04283 Sigma-Aldrich) at a final concentration of 1 mM (referred to as TA-Phi medium: Table ). ..

    Concentration Assay:

    Article Title: The phosphite oxidoreductase gene, ptxD as a bio-contained chloroplast marker and crop-protection tool for algal biotechnology using Chlamydomonas
    Article Snippet: .. Direct selection for ptxD transformants was on agar plates containing Tris-acetate medium supplemented with sodium phosphite (Na2 HPO3 ·5H2 O, 04283 Sigma-Aldrich) at a final concentration of 1 mM (referred to as TA-Phi medium: Table ). ..

    Activation Assay:

    Article Title: Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites
    Article Snippet: .. The mixture was adsorbed to a TALON metal affinity resin (BD-Biosciences) in a final volume of 100 μl, equilibrated with activation buffer (60 mM NH4 Cl, 10 mM Mg-acetate, 6 mM β-mercaptoethanol, 10 mM Tris-acetate, pH 7.5.) and 20 µg of bovine serum albumin (Sigma). ..

    Incubation:

    Article Title: GC-elements controlling HRAS transcription form i-motif structures unfolded by heterogeneous ribonucleoprotein particle A1
    Article Snippet: .. Radiolabelled oligonucleotides (10 nM) were incubated for 30 min at 20 °C with increasing amounts of hnRNP A1 (0–12 μg) as specified in , in 50 mM Tris–acetate, pH 5.5, 50 mM KCl, 1 mM DTT, 8% glycerol, 1% Phosphatase Inhibitor Cocktail I (Sigma, Milan, Italy), 5 mM NaF, 1 mM Na3 VO4 , 2.5 ng/μl salmon sperm DNA (binding buffer). .. The energy transfer (E T ) was calculated from the fluorescence intensity of the donor D in the presence (I DA ) and absence (I D) of the acceptor as: I DA and I D were measured in same buffer under identical concentrations (I D was obtained by transforming the dual-labeled oligonucleotide into the corresponding duplex in which the fluorophores are at a distance for which FRET = 0).

    Article Title: IFN? regulates discordant mechanisms of uveitis versus joint and axial disease in a murine model resembling spondyloarthritis
    Article Snippet: .. For aggrecan staining, sections were washed in chondroitinase buffer (0.1 Tris/acetate buffer, Ph 7.4) for 5 minutes before 45 min incubation in chondroitinase-ABC (Sigma) at 37°C. .. The following primary antibodies were applied to sections overnight at 4°C: rat anti-NIMP (R14, Abcam), anti-CCR3 (Y3L; Abcam), anti-CD3 (RM0027-3B19; Abcam), anti-CD45R/B220 (BD Pharmingen), anti-GFAP (DAKO), rabbit anti-mouse aggrecan (anti-aggrecan “G1-neoepitope [NITEGE373 ] (ABR Affinity Bioreagents), rabbit polyclonal IgG (Abcam), and isotype control rat, IgG2a or IgG2b (eBioscience).

    Western Blot:

    Article Title: Cartilage boundary lubrication synergism is mediated by hyaluronan concentration and PRG4 concentration and structure
    Article Snippet: .. Purity of the PRG4 preparation was confirmed by 3–8 % Tris-Acetate SDS-PAGE followed by protein stain and Western blotting with anti-PRG4 antibody 5C11 (obtained from Millipore, Etobicoke, ON, Canada) [ ] with Invitrogen’s NuPAGE system. .. Concentration of the purified PRG4 was determined by bicinchoninic acid assay.

    Sonication:

    Article Title: Protein kinase A induces UCP1 expression in specific adipose depots to increase energy expenditure and improve metabolic health
    Article Snippet: .. Ground tissue samples of ∼50 mg were sonicated at 1 mg/10 μl in 240 mmol/l Tris-acetate, 1.0% SDS, 0.5% glycerol, 5 mmol/l dithiothreitol, protease inhibitors (Sigma-Aldrich, cat. no. P8340), phosphatase inhibitor (Santa Cruz Biotechnology, catalog no. sc-45044), 1 mmol/l Na3 VO4 , 10 mmol/l β-glycerophosphate; boiled for 10 min; and sonicated again. .. Lysates were resolved by gel electrophoresis and transferred to nitrocellulose.

    Binding Assay:

    Article Title: GC-elements controlling HRAS transcription form i-motif structures unfolded by heterogeneous ribonucleoprotein particle A1
    Article Snippet: .. Radiolabelled oligonucleotides (10 nM) were incubated for 30 min at 20 °C with increasing amounts of hnRNP A1 (0–12 μg) as specified in , in 50 mM Tris–acetate, pH 5.5, 50 mM KCl, 1 mM DTT, 8% glycerol, 1% Phosphatase Inhibitor Cocktail I (Sigma, Milan, Italy), 5 mM NaF, 1 mM Na3 VO4 , 2.5 ng/μl salmon sperm DNA (binding buffer). .. The energy transfer (E T ) was calculated from the fluorescence intensity of the donor D in the presence (I DA ) and absence (I D) of the acceptor as: I DA and I D were measured in same buffer under identical concentrations (I D was obtained by transforming the dual-labeled oligonucleotide into the corresponding duplex in which the fluorophores are at a distance for which FRET = 0).

    SDS Page:

    Article Title: Cartilage boundary lubrication synergism is mediated by hyaluronan concentration and PRG4 concentration and structure
    Article Snippet: .. Purity of the PRG4 preparation was confirmed by 3–8 % Tris-Acetate SDS-PAGE followed by protein stain and Western blotting with anti-PRG4 antibody 5C11 (obtained from Millipore, Etobicoke, ON, Canada) [ ] with Invitrogen’s NuPAGE system. .. Concentration of the purified PRG4 was determined by bicinchoninic acid assay.

    Staining:

    Article Title: Cartilage boundary lubrication synergism is mediated by hyaluronan concentration and PRG4 concentration and structure
    Article Snippet: .. Purity of the PRG4 preparation was confirmed by 3–8 % Tris-Acetate SDS-PAGE followed by protein stain and Western blotting with anti-PRG4 antibody 5C11 (obtained from Millipore, Etobicoke, ON, Canada) [ ] with Invitrogen’s NuPAGE system. .. Concentration of the purified PRG4 was determined by bicinchoninic acid assay.

    Article Title: IFN? regulates discordant mechanisms of uveitis versus joint and axial disease in a murine model resembling spondyloarthritis
    Article Snippet: .. For aggrecan staining, sections were washed in chondroitinase buffer (0.1 Tris/acetate buffer, Ph 7.4) for 5 minutes before 45 min incubation in chondroitinase-ABC (Sigma) at 37°C. .. The following primary antibodies were applied to sections overnight at 4°C: rat anti-NIMP (R14, Abcam), anti-CCR3 (Y3L; Abcam), anti-CD3 (RM0027-3B19; Abcam), anti-CD45R/B220 (BD Pharmingen), anti-GFAP (DAKO), rabbit anti-mouse aggrecan (anti-aggrecan “G1-neoepitope [NITEGE373 ] (ABR Affinity Bioreagents), rabbit polyclonal IgG (Abcam), and isotype control rat, IgG2a or IgG2b (eBioscience).

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  • 86
    Millipore co immunoprecipitation lysis buffer
    PIWIL1 cooperates with UPF1 to negatively regulate PIWIL1-bound RNAs in a piRNA-independent manner. (A) A Coomassie blue staining protein gel of <t>PIWIL1-co-immunoprecipitation,</t> Mass spectrometry of this protein gel identifies PIWIL1 (blue arrow) as well as UPF1 (red arrow). (B) Western blotting showing reciprocal co-immunoprecipitated between PIWIL1 and UPF1 (total and phosphorylated form, p-UPF1) and between PIWIL1 and UPF2. (C) Western blotting shows that PIWIL1 co-immunoprecipitates with NMD complex core proteins UPF1, phosphorylated UPF1 (p-UPF1), UPF2, and SMG1. (D) Immunofluorescence staining of PIWIL1 (green) and DCP1A (red, a P body marker) in wildtype and PIWIL_KO SNU-1 cells. (E) Immunofluorescence staining of PIWIL1 (green), DCP1A (red), and UPF1 (fuchsia) in SNU-1 cells, which shows PIWIL1 co-localized with UPF1 in the P body. (F) Venn diagram of PIWIL1-bound RNAs, UPF1-bound RNAs, and PIWIL1-negatively regulated RNAs, with P
    Co Immunoprecipitation Lysis Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore tbp nhbp
    Schematic representation of oxSWNHs containing the <t>TBP–NHBP</t> peptide complex (oxSWNHs/TBP–NHBP) on the Ti surface. oxSWNHs were modified by artificial peptide aptamers against SWNH (NHBP-1) and Ti (minTBP-1). Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.
    Tbp Nhbp, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore rsb 150
    General translation is inhibited by hypoxia in HCT116 cells. A . Cytoplasmic extracts were loaded on a linear 15–40% sucrose gradient ultracentrifugation. After centrifugation, the polysome profile was plotted by A 254 values (upper), and RNA was extracted from each fraction for analysis. The purified RNA was resolved on a 1% formaldehyde/agarose gel, and rRNA was visualized by ethidium bromide staining (lower). The distribution of ribosomal subunits and polysomes are indicated. B . HCT116 cells were treated with hypoxia (1% O 2 ) for 0, 4, 8, 16, and 24 h. The polysomal distribution of β-actin mRNA was detected by polysome profiling and RT-PCR. Translational efficiency of β-actin mRNA was calculated and shown as a percentage at different time points. C . The phosphorylation status of eIF2α and 4E-BP1 was determined by immunoblot analysis in HCT116 cells exposed to hypoxia for the indicated period of time. The levels of phosphorylated (pi-) and total proteins were detected by specific antibodies against phospho-eIF2α (Ser51), eIF2α, phospho-4E-BP1 (Thr37/46), and 4E-BP1. Detection of β-actin protein served as a loading control. D . Immunoblot analysis of HIF-1α, GLUT1, VEGFA, and β-actin proteins in HCT116 cells exposed to hypoxia for 16 h. Detection of β-actin protein served as a loading control. E . HCT116 cells were grown under normoxia (21% O 2 ) or hypoxia (1% O 2 ) for 16 h. Cells were harvested and lysed in <t>RSB-150</t> buffer. Cytoplasmic extracts were loaded on a linear 15–40% sucrose gradient ultracentrifugation and collected into 11 fractions (1 ml/fraction). RNA isolated from each fraction was detected by RT-PCR and subjected to agarose gel electrophoresis. The polysomal region of the gradient includes fractions 7–11. Translational efficiency of β-actin, HIF-1α, and VEGFA mRNAs was calculated and shown as a percentage. 28S and 18S rRNAs were directly visualized by ethidium bromide staining. The distribution of ribosomal subunits and polysomes are indicated.
    Rsb 150, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Millipore tris tricin page gel
    The <t>TRIS-tricin-PAGE</t> of 18 positive bacteriocin factions of E. thailandicus E5 isolate showing molecular weight below 10 kDa. Corresponding bands of fractions 6–14 (a) , Corresponding bands of fractions 15–23 (b) , zymogram of fraction E5-F12 showing growth inhibition of the indicator strain, S. aureus as pointed by the arrow (c) .
    Tris Tricin Page Gel, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    PIWIL1 cooperates with UPF1 to negatively regulate PIWIL1-bound RNAs in a piRNA-independent manner. (A) A Coomassie blue staining protein gel of PIWIL1-co-immunoprecipitation, Mass spectrometry of this protein gel identifies PIWIL1 (blue arrow) as well as UPF1 (red arrow). (B) Western blotting showing reciprocal co-immunoprecipitated between PIWIL1 and UPF1 (total and phosphorylated form, p-UPF1) and between PIWIL1 and UPF2. (C) Western blotting shows that PIWIL1 co-immunoprecipitates with NMD complex core proteins UPF1, phosphorylated UPF1 (p-UPF1), UPF2, and SMG1. (D) Immunofluorescence staining of PIWIL1 (green) and DCP1A (red, a P body marker) in wildtype and PIWIL_KO SNU-1 cells. (E) Immunofluorescence staining of PIWIL1 (green), DCP1A (red), and UPF1 (fuchsia) in SNU-1 cells, which shows PIWIL1 co-localized with UPF1 in the P body. (F) Venn diagram of PIWIL1-bound RNAs, UPF1-bound RNAs, and PIWIL1-negatively regulated RNAs, with P

    Journal: bioRxiv

    Article Title: PIWIL1 Promotes Gastric Cancer via a piRNA-Independent Mechanism

    doi: 10.1101/2020.05.03.075390

    Figure Lengend Snippet: PIWIL1 cooperates with UPF1 to negatively regulate PIWIL1-bound RNAs in a piRNA-independent manner. (A) A Coomassie blue staining protein gel of PIWIL1-co-immunoprecipitation, Mass spectrometry of this protein gel identifies PIWIL1 (blue arrow) as well as UPF1 (red arrow). (B) Western blotting showing reciprocal co-immunoprecipitated between PIWIL1 and UPF1 (total and phosphorylated form, p-UPF1) and between PIWIL1 and UPF2. (C) Western blotting shows that PIWIL1 co-immunoprecipitates with NMD complex core proteins UPF1, phosphorylated UPF1 (p-UPF1), UPF2, and SMG1. (D) Immunofluorescence staining of PIWIL1 (green) and DCP1A (red, a P body marker) in wildtype and PIWIL_KO SNU-1 cells. (E) Immunofluorescence staining of PIWIL1 (green), DCP1A (red), and UPF1 (fuchsia) in SNU-1 cells, which shows PIWIL1 co-localized with UPF1 in the P body. (F) Venn diagram of PIWIL1-bound RNAs, UPF1-bound RNAs, and PIWIL1-negatively regulated RNAs, with P

    Article Snippet: Co-immunoprecipitation Cells were lysed in co-immunoprecipitation lysis buffer [20mM Tris-HCl pH7.4, 150mM NaCl, 1 % (v/v) IGEPAL® CA-630 (Millipore SIGMA, Cat# I8896), 1mM EDTA, 0.5 mM DTT, cOmplete™ EDTA-free Protease Inhibitor Cocktail Tablets (MERCK, Cat# 4693132001), and PhosStop Tablets (MERCK, 4906837001)], and spun at 14,000 rpm for 10 minutes to remove the debris.

    Techniques: Staining, Immunoprecipitation, Mass Spectrometry, Western Blot, Immunofluorescence, Marker

    Schematic representation of oxSWNHs containing the TBP–NHBP peptide complex (oxSWNHs/TBP–NHBP) on the Ti surface. oxSWNHs were modified by artificial peptide aptamers against SWNH (NHBP-1) and Ti (minTBP-1). Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: Schematic representation of oxSWNHs containing the TBP–NHBP peptide complex (oxSWNHs/TBP–NHBP) on the Ti surface. oxSWNHs were modified by artificial peptide aptamers against SWNH (NHBP-1) and Ti (minTBP-1). Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: Modification, Binding Assay

    In vitro release of DEX from DEX-oxSWNHs/TBP–NHBP on Ti. Time course of cumulative release of [ 3 H]-DEX from DEX-oxSWNHs/TBP–NHBP on Ti plates in PBS (blue line), RPMI medium/5% FBS (green line), and α-MEM/5% FBS (red line) at 37°C over 14 days. The inset shows cumulative release of DEX from DEX-oxSWNHs/TBP–NHBP on Ti plates in PBS (blue line), RPMI medium/5% FBS (green line), and α-MEM/5% FBS (red line) at 37°C for 24 hours. Error bars indicate standard deviation ( n =3). Abbreviations: DEX, dexamethasone; PBS, phosphate-buffered saline; RPMI, Roswell Park Memorial Institute; α-MEM, α-minimal essential medium; oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: In vitro release of DEX from DEX-oxSWNHs/TBP–NHBP on Ti. Time course of cumulative release of [ 3 H]-DEX from DEX-oxSWNHs/TBP–NHBP on Ti plates in PBS (blue line), RPMI medium/5% FBS (green line), and α-MEM/5% FBS (red line) at 37°C over 14 days. The inset shows cumulative release of DEX from DEX-oxSWNHs/TBP–NHBP on Ti plates in PBS (blue line), RPMI medium/5% FBS (green line), and α-MEM/5% FBS (red line) at 37°C for 24 hours. Error bars indicate standard deviation ( n =3). Abbreviations: DEX, dexamethasone; PBS, phosphate-buffered saline; RPMI, Roswell Park Memorial Institute; α-MEM, α-minimal essential medium; oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: In Vitro, Standard Deviation, Binding Assay

    Effects of DEX-oxSWNHs on GR transcriptional activity. ST2 cells were transfected with pBV2-MMTV-LUC and incubated with oxSWNHs/TBP–NHBP, DEX, or DEX-oxSWNHs/TBP–NHBP on Ti plates. Error bars indicate standard deviation ( n =5). ** P

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: Effects of DEX-oxSWNHs on GR transcriptional activity. ST2 cells were transfected with pBV2-MMTV-LUC and incubated with oxSWNHs/TBP–NHBP, DEX, or DEX-oxSWNHs/TBP–NHBP on Ti plates. Error bars indicate standard deviation ( n =5). ** P

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: Activity Assay, Transfection, Incubation, Standard Deviation

    Time-dependent changes in f and D determined using a QCM. ( A – F ) oxSWNHs/TBP–NHBP ( A ), oxSWNHs ( B ), TBP–NHBP ( C ), oxSWNHs/TBP–NHBP ( D ), TBP–NHBP ( E ), and TBP–NHBP and oxSWNHs/TBP–NHBP ( F ) deposited on a Ti-coated sensor. Values on the longitudinal axis represent negative Δ f and positive Δ D values. Changes associated with oxSWNHs/TBP–NHBP, oxSWNHs, and TBP–NHBP adsorption are indicated by green, gray, and purple lines, respectively. Green, gray, and purple arrowheads indicate the time points at which oxSWNHs/TBP–NHBP, oxSWNHs, and TBP–NHBP, respectively, were infused into the measurement chamber. Vs represent the time points at which the wash solution (10% DMF) was infused. Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide; DMF, dimethylformamide.

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: Time-dependent changes in f and D determined using a QCM. ( A – F ) oxSWNHs/TBP–NHBP ( A ), oxSWNHs ( B ), TBP–NHBP ( C ), oxSWNHs/TBP–NHBP ( D ), TBP–NHBP ( E ), and TBP–NHBP and oxSWNHs/TBP–NHBP ( F ) deposited on a Ti-coated sensor. Values on the longitudinal axis represent negative Δ f and positive Δ D values. Changes associated with oxSWNHs/TBP–NHBP, oxSWNHs, and TBP–NHBP adsorption are indicated by green, gray, and purple lines, respectively. Green, gray, and purple arrowheads indicate the time points at which oxSWNHs/TBP–NHBP, oxSWNHs, and TBP–NHBP, respectively, were infused into the measurement chamber. Vs represent the time points at which the wash solution (10% DMF) was infused. Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide; DMF, dimethylformamide.

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: Adsorption, Binding Assay

    Scanning electron micrographs of Ti plates functionalized with oxSWNHs/TBP–NHBP. ( A – E ) Ti plates were functionalized with oxSWNHs/TBP–NHBP ( A ), oxSWNHs ( B ), oxSWNHs/TBP(R-A)-NHBP ( C ), oxSWNHs/TBP ( D ), or oxSWNHs/NHBP ( E ). The inset shows magnified sections. Black scale: 20 µm; red scale: 2 µm. ( F ) Adsorption amounts measured using an electronic balance. Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: Scanning electron micrographs of Ti plates functionalized with oxSWNHs/TBP–NHBP. ( A – E ) Ti plates were functionalized with oxSWNHs/TBP–NHBP ( A ), oxSWNHs ( B ), oxSWNHs/TBP(R-A)-NHBP ( C ), oxSWNHs/TBP ( D ), or oxSWNHs/NHBP ( E ). The inset shows magnified sections. Black scale: 20 µm; red scale: 2 µm. ( F ) Adsorption amounts measured using an electronic balance. Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: Adsorption, Binding Assay

    Effects of DEX-oxSWNHs on ALP activity. MC3TS-E1 cells were cultured with oxSWNHs/TBP–NHBP, DEX, or DEX-oxSWNHs/TBP–NHBP on Ti plates for 5, 7, 10, and 14 days. Error bars indicate standard deviation ( n =5). ** P

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: Effects of DEX-oxSWNHs on ALP activity. MC3TS-E1 cells were cultured with oxSWNHs/TBP–NHBP, DEX, or DEX-oxSWNHs/TBP–NHBP on Ti plates for 5, 7, 10, and 14 days. Error bars indicate standard deviation ( n =5). ** P

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: ALP Assay, Activity Assay, Cell Culture, Standard Deviation

    Viability of MC3T3-E1 cells cultured for 2 days on oxSWNHs/TBP–NHBP on Ti. Viable cell counts were determined relative to cells grown on uncoated Ti (none). ( A ) Live (green, left panel) and dead (red, right panel) cells were stained with calcein-AM and propidium iodide, respectively. White scale: 100 µm. ( B ) Counts of live cells on uncoated Ti and oxSWNHs/TBP–NHBP-conjugated Ti. Error bars indicate standard deviation ( n =4). Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Journal: International Journal of Nanomedicine

    Article Title: Immobilization of a carbon nanomaterial-based localized drug-release system using a bispecific material-binding peptide

    doi: 10.2147/IJN.S155913

    Figure Lengend Snippet: Viability of MC3T3-E1 cells cultured for 2 days on oxSWNHs/TBP–NHBP on Ti. Viable cell counts were determined relative to cells grown on uncoated Ti (none). ( A ) Live (green, left panel) and dead (red, right panel) cells were stained with calcein-AM and propidium iodide, respectively. White scale: 100 µm. ( B ) Counts of live cells on uncoated Ti and oxSWNHs/TBP–NHBP-conjugated Ti. Error bars indicate standard deviation ( n =4). Abbreviations: oxSWNHs, oxidized single-walled carbon nanohorns; TBP, Ti-binding peptide; NHBP-1, SWNH-binding peptide.

    Article Snippet: DEX-oxSWNHs were mixed with TBP–NHBP and vortexed for 10 min. Ti plates (10×10×1 mm) in 24-well culture plates were incubated for 1 h at room temperature in 500 µL of the above mixture, washed three times with water filtered through a 0.22-µm membrane (Millex-GS; Millipore), and dried under vacuum for 8 h. The amount of DEX was quantified with [3 H]-DEX (1.48 TBq/mmol; Amersham Bioscience, Piscataway, NJ, USA) using an LS6500 scintillation counter (Beckman Coulter, Fullerton, CA, USA).

    Techniques: Cell Culture, Staining, Standard Deviation, Binding Assay

    General translation is inhibited by hypoxia in HCT116 cells. A . Cytoplasmic extracts were loaded on a linear 15–40% sucrose gradient ultracentrifugation. After centrifugation, the polysome profile was plotted by A 254 values (upper), and RNA was extracted from each fraction for analysis. The purified RNA was resolved on a 1% formaldehyde/agarose gel, and rRNA was visualized by ethidium bromide staining (lower). The distribution of ribosomal subunits and polysomes are indicated. B . HCT116 cells were treated with hypoxia (1% O 2 ) for 0, 4, 8, 16, and 24 h. The polysomal distribution of β-actin mRNA was detected by polysome profiling and RT-PCR. Translational efficiency of β-actin mRNA was calculated and shown as a percentage at different time points. C . The phosphorylation status of eIF2α and 4E-BP1 was determined by immunoblot analysis in HCT116 cells exposed to hypoxia for the indicated period of time. The levels of phosphorylated (pi-) and total proteins were detected by specific antibodies against phospho-eIF2α (Ser51), eIF2α, phospho-4E-BP1 (Thr37/46), and 4E-BP1. Detection of β-actin protein served as a loading control. D . Immunoblot analysis of HIF-1α, GLUT1, VEGFA, and β-actin proteins in HCT116 cells exposed to hypoxia for 16 h. Detection of β-actin protein served as a loading control. E . HCT116 cells were grown under normoxia (21% O 2 ) or hypoxia (1% O 2 ) for 16 h. Cells were harvested and lysed in RSB-150 buffer. Cytoplasmic extracts were loaded on a linear 15–40% sucrose gradient ultracentrifugation and collected into 11 fractions (1 ml/fraction). RNA isolated from each fraction was detected by RT-PCR and subjected to agarose gel electrophoresis. The polysomal region of the gradient includes fractions 7–11. Translational efficiency of β-actin, HIF-1α, and VEGFA mRNAs was calculated and shown as a percentage. 28S and 18S rRNAs were directly visualized by ethidium bromide staining. The distribution of ribosomal subunits and polysomes are indicated.

    Journal: PLoS ONE

    Article Title: Hypoxia Induces Autophagy through Translational Up-Regulation of Lysosomal Proteins in Human Colon Cancer Cells

    doi: 10.1371/journal.pone.0153627

    Figure Lengend Snippet: General translation is inhibited by hypoxia in HCT116 cells. A . Cytoplasmic extracts were loaded on a linear 15–40% sucrose gradient ultracentrifugation. After centrifugation, the polysome profile was plotted by A 254 values (upper), and RNA was extracted from each fraction for analysis. The purified RNA was resolved on a 1% formaldehyde/agarose gel, and rRNA was visualized by ethidium bromide staining (lower). The distribution of ribosomal subunits and polysomes are indicated. B . HCT116 cells were treated with hypoxia (1% O 2 ) for 0, 4, 8, 16, and 24 h. The polysomal distribution of β-actin mRNA was detected by polysome profiling and RT-PCR. Translational efficiency of β-actin mRNA was calculated and shown as a percentage at different time points. C . The phosphorylation status of eIF2α and 4E-BP1 was determined by immunoblot analysis in HCT116 cells exposed to hypoxia for the indicated period of time. The levels of phosphorylated (pi-) and total proteins were detected by specific antibodies against phospho-eIF2α (Ser51), eIF2α, phospho-4E-BP1 (Thr37/46), and 4E-BP1. Detection of β-actin protein served as a loading control. D . Immunoblot analysis of HIF-1α, GLUT1, VEGFA, and β-actin proteins in HCT116 cells exposed to hypoxia for 16 h. Detection of β-actin protein served as a loading control. E . HCT116 cells were grown under normoxia (21% O 2 ) or hypoxia (1% O 2 ) for 16 h. Cells were harvested and lysed in RSB-150 buffer. Cytoplasmic extracts were loaded on a linear 15–40% sucrose gradient ultracentrifugation and collected into 11 fractions (1 ml/fraction). RNA isolated from each fraction was detected by RT-PCR and subjected to agarose gel electrophoresis. The polysomal region of the gradient includes fractions 7–11. Translational efficiency of β-actin, HIF-1α, and VEGFA mRNAs was calculated and shown as a percentage. 28S and 18S rRNAs were directly visualized by ethidium bromide staining. The distribution of ribosomal subunits and polysomes are indicated.

    Article Snippet: Cell pellets were resuspended in RSB-150 (10 mM Tris-HCl (pH 7.4), 3 mM MgCl2 , and 150 mM NaCl) containing 100 μg/ml cycloheximide, 40 μg/ml digitonin (Calbiochem), 20 U/ml RNasin (Promega), and 1X protease inhibitor cocktail (Thermo Fisher Scientific).

    Techniques: Centrifugation, Purification, Agarose Gel Electrophoresis, Staining, Reverse Transcription Polymerase Chain Reaction, Isolation

    The TRIS-tricin-PAGE of 18 positive bacteriocin factions of E. thailandicus E5 isolate showing molecular weight below 10 kDa. Corresponding bands of fractions 6–14 (a) , Corresponding bands of fractions 15–23 (b) , zymogram of fraction E5-F12 showing growth inhibition of the indicator strain, S. aureus as pointed by the arrow (c) .

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Purification, Characterization, Identification, and Anticancer Activity of a Circular Bacteriocin From Enterococcus thailandicus

    doi: 10.3389/fbioe.2020.00450

    Figure Lengend Snippet: The TRIS-tricin-PAGE of 18 positive bacteriocin factions of E. thailandicus E5 isolate showing molecular weight below 10 kDa. Corresponding bands of fractions 6–14 (a) , Corresponding bands of fractions 15–23 (b) , zymogram of fraction E5-F12 showing growth inhibition of the indicator strain, S. aureus as pointed by the arrow (c) .

    Article Snippet: The molecular size of the purified bacteriocin factions was determined by TRIS-tricin- PAGE gel using 15% resolving gel as described by Laemmli ( ).

    Techniques: Polyacrylamide Gel Electrophoresis, Molecular Weight, Inhibition