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  • 99
    Thermo Fisher tris
    Characterization of the hybrid pore formation. a Typical current profile over time recorded through a 5.5 nm diameter SS pore at +100 mV. After injection of 0.1 nmol of portal protein, short current drops are detected, interpreted as portal collisions with the solid-state nanopore. b A representative current vs time trace recorded for a 5.4 nm SS nanopore at +80 mV, showing stable insertion of a portal protein. c Current as a function of the applied voltage for a 5.7 nm diameter SS pore recorded before (red markers) and after insertion of a portal protein (purple). d Current noise analysis of a 5.5 nm diameter solid-state nanopore before (red) and after insertion of a portal protein (purple). e Conductance of solid-state nanopore vs conductance of hybrid SS-portal pores formed after electrokinetic corking of the portal protein within the SS nanopore ( n = 32 for CD/N hybrids and n = 15 for CGG hybrids). Experiments were performed in 0.5 M <t>NaCl,</t> 20 mM <t>Tris,</t> pH 7.5
    Tris, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 11802 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris
    Transport characteristic and quantum capacitance of CVD graphene upon hydrogenation. a Illustration of the field effect transistor setup fabricated from CVD graphene. b Room temperature conductance ( G ) plots as a function of the gate voltage ( V g ) showing the p-doping effect upon hydrogenation from 0 to 30 s. The gray dashed line is a guide-to-the-eye, highlighting the sublinear behavior of the G ( V g ) curves. c The shifts of the charge neutrality point (CNP) upon hydrogenation. d The carrier mobility of graphene, µ , vs the hydrogenation time. e Quantum capacitance C q of graphene measured as a function of V ch for 0–30 s of hydrogenation. f Impurity density n imp vs hydrogenation time. The electrolyte solution is 0.1 M <t>KCl</t> with 10 mM <t>Tris</t> (pH 8). The error bars in d , f are the standard deviation of experimental values
    Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 30544 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad tris
    <t>2DE</t> gel (11 cm, pH 4–7, <t>Bis-Tris</t> 12%) showing all the protein spots detected in nacre WSM from Crassostrea gigas . Numbered spots represent proteins identified by mass spectrometry.
    Tris, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 3276 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris base a
    (Panel A ) Minocycline (20 µM) in the presence of 3 mM Ca 2+ induces an electrical current in BLM made from DPhPC. The experimental buffer was 10 mM <t>Tris,</t> 10 mM <t>MES,</t> 100 mM KCl, pH 8.5; the voltage was 30 mV. (Panels B, C ) Ion channel activity induced by minocycline (8 µM) in the presence of Ca 2+ (3 mM in panel B and 20 µM in panel C) at 50 mV in BLM made from DPhPC. The experimental buffer was 10 mM Tris, 10 mM MES, 1 M KCl, pH 9.0. (A current of 0.7 pA at 50 mV corresponds to a conductance of 14 pS)
    Tris Base A, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 81 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris acetate
    ( A ) ChIP experiment to determine the occupancy of hras -1, hras -2 and control sequence (870 bp downstream from TSS) by <t>hnRNP</t> A1. Histograms shows the relative occupancy of hras -1 and hras -2 by hnRNP A1, RNA Pol II (positive control) and IgG (negative control). Data have been normalized by IgG signal; ( B ) EMSA of 32 P-labelled hras -1 Y and hras -2 Y in 50 mM <t>Tris-acetate</t> pH 5.5, 50 mM KCl, incubated 40 min at room temperature with increasing amounts of recombinant hnRNP A1 (0–12 μg). Lane (Δ,A1) indicates the i M incubated 40 min at room temperature, with denatured hnRNPA1 in binding buffer (see Methods); ( C ) EMSA at pH 5.5 of hras -1 Y with BSA or denatured hnRNP A1 and EMSA of hras -1 Y (m) with hnRNP A1; ss = single-stranded oligonucleotide; 1:1 and 1:2 DNA-protein complexes.
    Tris Acetate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 383 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris borate
    Characterization of LMW-HA and its effects on EC proliferation. Panel A , to evaluate the molecular weight ( MW ) and purity of our LMW-HA preparation, a 4–20% <t>Tris</t> <t>borate-EDTA</t> ( TBE ) gel was run with HA molecular weight standards (Select-HA TM 75–150
    Tris Borate, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 62 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris hydrochloride tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris Hydrochloride Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 8927 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    tris  (Roche)
    99
    Roche tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 23329 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Applichem tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Applichem, used in various techniques. Bioz Stars score: 95/100, based on 170 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Merck KGaA tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 97/100, based on 542 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Avantor tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Avantor, used in various techniques. Bioz Stars score: 99/100, based on 299 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    SERVA Electrophoresis tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by SERVA Electrophoresis, used in various techniques. Bioz Stars score: 93/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Amresco tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Amresco, used in various techniques. Bioz Stars score: 94/100, based on 341 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    BioShop tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by BioShop, used in various techniques. Bioz Stars score: 93/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Carl Roth GmbH tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 97/100, based on 307 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Fisher Scientific tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 98/100, based on 726 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Sinopharm tris
    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: <t>Au/NAC/DPTA–Cu(II)–His</t> 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in <t>TRIS</t> buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).
    Tris, supplied by Sinopharm, used in various techniques. Bioz Stars score: 95/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris hcl
    Neu3 behaves as an integral membrane protein. ( a ) Soluble (S, first lane) and membrane (P, second lane) fractions of NEU3 -transfected cells were obtained as described in Fig. 1a . The latter fraction was then incubated for 40 min on ice with <t>Tris</t> buffer (control) or Na 2 CO 3 at pH 11.5 in order to extract peripheral membrane proteins. After treatment, membranes were collected by ultracentrifugation, and membrane-bound (P, fourth and sixth lanes) and solubilized (S, third and fifth lanes) proteins were analyzed by Western blotting using anti-Neu3 antibody. K-Ras and Cav-1 were used as markers of an extractable and a non-extractable membrane protein, respectively. Tub was used as a marker of a soluble protein. ( b ) Intact NEU3 -transfected cells were treated with (+) or without (−) 100 µg/ml proteinase K (PK) for 30 min at 37 °C. The remaining proteins were run on a SDS-PAGE gel and Western blotted with anti-c-Myc and anti-Neu3 antibodies. Transferrin Receptor (TfR) was used as a marker of a PK-accessible protein, whereas Cav-1 and sialyltransferase ST3Gal-II were used as markers of proteins not accessible to PK. The molecular masses in kDa of the standard proteins are shown on the left. ( c ) Antibody accessibility in permeabilized and non-permeabilized cells. The signal of the indicated antibodies were analyzed after fixation in cells treated with 0.1% saponin in <t>PBS/BSA</t> (permeabilized) or with PBS/BSA alone (non-permeabilized). Cav-1 was used as a marker of an inner membrane protein detected only after cell permeabilization, and GPI-YFP was used as a marker of an outer membrane protein accessible by antibody without permeabilization. Cells nuclei were stained blue with Hoechst dye. ( d ) Cell surface proteins exposed to the extracellular environment of NEU3 -transfected cells were biotinylated and isolated by streptavidin agarose pull-down. Biotinylated (B) and non-biotinylated (NB) fractions were analyzed by Western blotting. Endogenous marker Cav-1 was used as control of a membrane protein not exposed to the extracellular environment. Densitometric analysis indicating the percentage of Neu3 in each fraction is shown. ( e ) Kyte-Doolittle hydrophobicity plot for Neu3 sequence using a window size of 19. The red line corresponds to a hydrophobicity score of 1.6 and designates an empirical cutoff value for α-helix transmembrane segments of ~19 amino acids long.
    Tris Hcl, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2636 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher tris edta
    Effect of SAP on heat-induced GST aggregation in MES-Ca and <t>Tris-EDTA</t> buffers. ( a,c ) Time course of GST aggregation monitored by turbidity in the absence (black diamond) or presence of 1:10 (molar ratio of SAP to GST) (orange circle), 1:5 (red circle), or 1:2 (dark brown circle) SAP in MES-Ca buffer ( a ), or 1:10 (right green circle), 1:5 (green circle), or 1:2 (dark green circle) SAP in Tris-EDTA buffer ( c ) at 43 °C. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b,d ) Turbidity of each sample at 32 h in MES-Ca ( b ) and Tris-EDTA buffers ( d ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. **P
    Tris Edta, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 508 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore tris glycerol
    Effect of SAP on heat-induced GST aggregation in MES-Ca and <t>Tris-EDTA</t> buffers. ( a,c ) Time course of GST aggregation monitored by turbidity in the absence (black diamond) or presence of 1:10 (molar ratio of SAP to GST) (orange circle), 1:5 (red circle), or 1:2 (dark brown circle) SAP in MES-Ca buffer ( a ), or 1:10 (right green circle), 1:5 (green circle), or 1:2 (dark green circle) SAP in Tris-EDTA buffer ( c ) at 43 °C. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b,d ) Turbidity of each sample at 32 h in MES-Ca ( b ) and Tris-EDTA buffers ( d ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. **P
    Tris Glycerol, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore trimethylolpropane tris
    Effect of SAP on heat-induced GST aggregation in MES-Ca and <t>Tris-EDTA</t> buffers. ( a,c ) Time course of GST aggregation monitored by turbidity in the absence (black diamond) or presence of 1:10 (molar ratio of SAP to GST) (orange circle), 1:5 (red circle), or 1:2 (dark brown circle) SAP in MES-Ca buffer ( a ), or 1:10 (right green circle), 1:5 (green circle), or 1:2 (dark green circle) SAP in Tris-EDTA buffer ( c ) at 43 °C. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b,d ) Turbidity of each sample at 32 h in MES-Ca ( b ) and Tris-EDTA buffers ( d ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. **P
    Trimethylolpropane Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher bis tris
    Effect of SAP on heat-induced GST aggregation in MES-Ca and <t>Tris-EDTA</t> buffers. ( a,c ) Time course of GST aggregation monitored by turbidity in the absence (black diamond) or presence of 1:10 (molar ratio of SAP to GST) (orange circle), 1:5 (red circle), or 1:2 (dark brown circle) SAP in MES-Ca buffer ( a ), or 1:10 (right green circle), 1:5 (green circle), or 1:2 (dark green circle) SAP in Tris-EDTA buffer ( c ) at 43 °C. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b,d ) Turbidity of each sample at 32 h in MES-Ca ( b ) and Tris-EDTA buffers ( d ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. **P
    Bis Tris, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 2020 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher tris edta buffer
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    Image Search Results


    Characterization of the hybrid pore formation. a Typical current profile over time recorded through a 5.5 nm diameter SS pore at +100 mV. After injection of 0.1 nmol of portal protein, short current drops are detected, interpreted as portal collisions with the solid-state nanopore. b A representative current vs time trace recorded for a 5.4 nm SS nanopore at +80 mV, showing stable insertion of a portal protein. c Current as a function of the applied voltage for a 5.7 nm diameter SS pore recorded before (red markers) and after insertion of a portal protein (purple). d Current noise analysis of a 5.5 nm diameter solid-state nanopore before (red) and after insertion of a portal protein (purple). e Conductance of solid-state nanopore vs conductance of hybrid SS-portal pores formed after electrokinetic corking of the portal protein within the SS nanopore ( n = 32 for CD/N hybrids and n = 15 for CGG hybrids). Experiments were performed in 0.5 M NaCl, 20 mM Tris, pH 7.5

    Journal: Nature Communications

    Article Title: Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors

    doi: 10.1038/s41467-018-07116-x

    Figure Lengend Snippet: Characterization of the hybrid pore formation. a Typical current profile over time recorded through a 5.5 nm diameter SS pore at +100 mV. After injection of 0.1 nmol of portal protein, short current drops are detected, interpreted as portal collisions with the solid-state nanopore. b A representative current vs time trace recorded for a 5.4 nm SS nanopore at +80 mV, showing stable insertion of a portal protein. c Current as a function of the applied voltage for a 5.7 nm diameter SS pore recorded before (red markers) and after insertion of a portal protein (purple). d Current noise analysis of a 5.5 nm diameter solid-state nanopore before (red) and after insertion of a portal protein (purple). e Conductance of solid-state nanopore vs conductance of hybrid SS-portal pores formed after electrokinetic corking of the portal protein within the SS nanopore ( n = 32 for CD/N hybrids and n = 15 for CGG hybrids). Experiments were performed in 0.5 M NaCl, 20 mM Tris, pH 7.5

    Article Snippet: Protein was exchanged into 20 mM Tris pH 7.5, 0.5 M NaCl buffer (Zeba Spin Columns, Thermofisher) for use in hybrid nanopore formation.

    Techniques: Injection

    Sensing different biopolymers using a hybrid nanopore. Current vs time trace recorded through the hybrid pore at +60 mV in the presence of a 36.0 μM insulin, b 7.7 μM DNA hairpin, c 10.3 μM TPX2 peptide and d 16.6 μM ssDNA. The data in a were filtered at 10 kHz (gray) or 0.5 kHz (green). e Scatter plot of Δ I vs dwell time for the DNA hairpin (red, n = 5883 events), the peptide (purple, n = 3368 events) and the ssDNA (orange, n = 18,812 events)). Experiments were performed in 0.5 M NaCl, 20 mM Tris, pH 7.5

    Journal: Nature Communications

    Article Title: Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors

    doi: 10.1038/s41467-018-07116-x

    Figure Lengend Snippet: Sensing different biopolymers using a hybrid nanopore. Current vs time trace recorded through the hybrid pore at +60 mV in the presence of a 36.0 μM insulin, b 7.7 μM DNA hairpin, c 10.3 μM TPX2 peptide and d 16.6 μM ssDNA. The data in a were filtered at 10 kHz (gray) or 0.5 kHz (green). e Scatter plot of Δ I vs dwell time for the DNA hairpin (red, n = 5883 events), the peptide (purple, n = 3368 events) and the ssDNA (orange, n = 18,812 events)). Experiments were performed in 0.5 M NaCl, 20 mM Tris, pH 7.5

    Article Snippet: Protein was exchanged into 20 mM Tris pH 7.5, 0.5 M NaCl buffer (Zeba Spin Columns, Thermofisher) for use in hybrid nanopore formation.

    Techniques:

    Dynamics of TPX2 peptide transport. a Current vs time trace recorded through a hybrid pore at +30, +40 and +55 mV in the presence of 10.3 μM TPX2 peptide. b Semi-log plot of the event frequency as a function of the applied voltage. c Semi-log plot of the peptide dwell time as a function of the applied voltage. The lines in ( b , c ) are exponential fits to the data. Experiments were performed in 0.5 M NaCl, 20 mM Tris, pH 7.5. Data shown in semi-log plots are mean and s.d. of 23,516 events (total for all points) from one hybrid nanopore

    Journal: Nature Communications

    Article Title: Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors

    doi: 10.1038/s41467-018-07116-x

    Figure Lengend Snippet: Dynamics of TPX2 peptide transport. a Current vs time trace recorded through a hybrid pore at +30, +40 and +55 mV in the presence of 10.3 μM TPX2 peptide. b Semi-log plot of the event frequency as a function of the applied voltage. c Semi-log plot of the peptide dwell time as a function of the applied voltage. The lines in ( b , c ) are exponential fits to the data. Experiments were performed in 0.5 M NaCl, 20 mM Tris, pH 7.5. Data shown in semi-log plots are mean and s.d. of 23,516 events (total for all points) from one hybrid nanopore

    Article Snippet: Protein was exchanged into 20 mM Tris pH 7.5, 0.5 M NaCl buffer (Zeba Spin Columns, Thermofisher) for use in hybrid nanopore formation.

    Techniques:

    Design of a bio-inspired lipid-free hybrid nanopore. a Cartoon of the DNA packaging machine of a dsDNA virus. Viral genomic DNA (red) is translocated into the preformed virus capsid by the packaging ATPase (yellow) through the portal protein (aqua) embedded in viral capsid (gray). b Left, electrostatic properties of the tunnel in wild-type and mutant portal proteins. Slice through the middle of molecular surface colored according to charge from red (−1 kT e −1 ) to blue (+1 kT e −1 ). b Right (gray box), dimensions of the portal protein (teal, L) and the SS nanopore (pink, R). c Insertion of the purified portal protein into a nanopore fabricated in a thin solid-state (SS) membrane. Portal protein is applied to the trans chamber of a SS nanopore device containing an electrolyte solution of 20 mM Tris pH 7.5, 0.5 M NaCl. The protein electrokinetically inserts into the SS pore during application of a positive voltage. d Cartoon image of the hybrid pore, in which application of voltage results in ion current through the pore (blue arrows), as well as leakage current that is peripheral to the pore (red arrows)

    Journal: Nature Communications

    Article Title: Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors

    doi: 10.1038/s41467-018-07116-x

    Figure Lengend Snippet: Design of a bio-inspired lipid-free hybrid nanopore. a Cartoon of the DNA packaging machine of a dsDNA virus. Viral genomic DNA (red) is translocated into the preformed virus capsid by the packaging ATPase (yellow) through the portal protein (aqua) embedded in viral capsid (gray). b Left, electrostatic properties of the tunnel in wild-type and mutant portal proteins. Slice through the middle of molecular surface colored according to charge from red (−1 kT e −1 ) to blue (+1 kT e −1 ). b Right (gray box), dimensions of the portal protein (teal, L) and the SS nanopore (pink, R). c Insertion of the purified portal protein into a nanopore fabricated in a thin solid-state (SS) membrane. Portal protein is applied to the trans chamber of a SS nanopore device containing an electrolyte solution of 20 mM Tris pH 7.5, 0.5 M NaCl. The protein electrokinetically inserts into the SS pore during application of a positive voltage. d Cartoon image of the hybrid pore, in which application of voltage results in ion current through the pore (blue arrows), as well as leakage current that is peripheral to the pore (red arrows)

    Article Snippet: Protein was exchanged into 20 mM Tris pH 7.5, 0.5 M NaCl buffer (Zeba Spin Columns, Thermofisher) for use in hybrid nanopore formation.

    Techniques: Mutagenesis, Purification

    Transport characteristic and quantum capacitance of CVD graphene upon hydrogenation. a Illustration of the field effect transistor setup fabricated from CVD graphene. b Room temperature conductance ( G ) plots as a function of the gate voltage ( V g ) showing the p-doping effect upon hydrogenation from 0 to 30 s. The gray dashed line is a guide-to-the-eye, highlighting the sublinear behavior of the G ( V g ) curves. c The shifts of the charge neutrality point (CNP) upon hydrogenation. d The carrier mobility of graphene, µ , vs the hydrogenation time. e Quantum capacitance C q of graphene measured as a function of V ch for 0–30 s of hydrogenation. f Impurity density n imp vs hydrogenation time. The electrolyte solution is 0.1 M KCl with 10 mM Tris (pH 8). The error bars in d , f are the standard deviation of experimental values

    Journal: Nature Communications

    Article Title: Quantum and electrochemical interplays in hydrogenated graphene

    doi: 10.1038/s41467-018-03026-0

    Figure Lengend Snippet: Transport characteristic and quantum capacitance of CVD graphene upon hydrogenation. a Illustration of the field effect transistor setup fabricated from CVD graphene. b Room temperature conductance ( G ) plots as a function of the gate voltage ( V g ) showing the p-doping effect upon hydrogenation from 0 to 30 s. The gray dashed line is a guide-to-the-eye, highlighting the sublinear behavior of the G ( V g ) curves. c The shifts of the charge neutrality point (CNP) upon hydrogenation. d The carrier mobility of graphene, µ , vs the hydrogenation time. e Quantum capacitance C q of graphene measured as a function of V ch for 0–30 s of hydrogenation. f Impurity density n imp vs hydrogenation time. The electrolyte solution is 0.1 M KCl with 10 mM Tris (pH 8). The error bars in d , f are the standard deviation of experimental values

    Article Snippet: Electrolyte- or electrochemical-gated GFET measurements were carried out in 0.1 M KCl solution containing 10 mM Tris as the buffer (pH 8, both from Sigma Aldrich).

    Techniques: Standard Deviation

    Electrochemical behavior of CVD graphene upon hydrogenation. a Cyclic voltammograms (CVs) obtained on graphene after 0–30 s of hydrogenation at a scan rate of 100 mV s −1 . b Current density vs scan rate for untreated graphene shown in a . c The electron transfer rate k 0 vs hydrogenation time from 0 to 30 s. d The averaged total capacitance C ave− tot vs hydrogenation time from 0 to 30 s. e CV curves obtained on graphene after 0–13 s of Ar treatment at a scan rate of 100 mV s −1 . f \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$k^0_{{\mathrm{Ar}}}$$\end{document} k Ar 0 vs argon plasma treating time from 0 to 13 s. The aqueous electrolyte solution contains 0.1 M KCl supplemented with 10 mM Tris at pH 8. The redox probe employed is 1 mM hexaammineruthenium (II)/hexaammineruthenium (III) chloride. The error bars in c , d , f are the standard deviation of experimental values

    Journal: Nature Communications

    Article Title: Quantum and electrochemical interplays in hydrogenated graphene

    doi: 10.1038/s41467-018-03026-0

    Figure Lengend Snippet: Electrochemical behavior of CVD graphene upon hydrogenation. a Cyclic voltammograms (CVs) obtained on graphene after 0–30 s of hydrogenation at a scan rate of 100 mV s −1 . b Current density vs scan rate for untreated graphene shown in a . c The electron transfer rate k 0 vs hydrogenation time from 0 to 30 s. d The averaged total capacitance C ave− tot vs hydrogenation time from 0 to 30 s. e CV curves obtained on graphene after 0–13 s of Ar treatment at a scan rate of 100 mV s −1 . f \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$k^0_{{\mathrm{Ar}}}$$\end{document} k Ar 0 vs argon plasma treating time from 0 to 13 s. The aqueous electrolyte solution contains 0.1 M KCl supplemented with 10 mM Tris at pH 8. The redox probe employed is 1 mM hexaammineruthenium (II)/hexaammineruthenium (III) chloride. The error bars in c , d , f are the standard deviation of experimental values

    Article Snippet: Electrolyte- or electrochemical-gated GFET measurements were carried out in 0.1 M KCl solution containing 10 mM Tris as the buffer (pH 8, both from Sigma Aldrich).

    Techniques: Standard Deviation

    S100P is expressed in Jeg-3 and Bewo but not HTR8 EV trophoblast cell lines. HTR8, Bewo and Jeg-3 cells, along with HeLa A3 induced for S100P expression (or their non-expressing counterparts), were grown for 48 hours prior to collection for mRNA qPCR analysis ( A ) or 72 hours prior to collection for protein Western blotting ( B ). mRNAs were isolated using TRIS reagent followed by reverse transcription and quantitative PCR analysis using S100P and β-actin primers, as described in Methods. Data is presented as 2 ∆ CT mean values ± SD of 3 independent samples of a representative experiment compared to the non-induced HeLaA3 cells. **P

    Journal: Scientific Reports

    Article Title: S100P enhances the motility and invasion of human trophoblast cell lines

    doi: 10.1038/s41598-018-29852-2

    Figure Lengend Snippet: S100P is expressed in Jeg-3 and Bewo but not HTR8 EV trophoblast cell lines. HTR8, Bewo and Jeg-3 cells, along with HeLa A3 induced for S100P expression (or their non-expressing counterparts), were grown for 48 hours prior to collection for mRNA qPCR analysis ( A ) or 72 hours prior to collection for protein Western blotting ( B ). mRNAs were isolated using TRIS reagent followed by reverse transcription and quantitative PCR analysis using S100P and β-actin primers, as described in Methods. Data is presented as 2 ∆ CT mean values ± SD of 3 independent samples of a representative experiment compared to the non-induced HeLaA3 cells. **P

    Article Snippet: qPCR analysis Following the appropriate incubation, trophoblast cells were collected after trypsinisation and mRNA extraction was carried out using TRIS reagent (Sigma, UK) according to the manufacturer’s protocol. qPCR was performed using S100P (sequences F: 5′-TCAAGGTGCTGATGGAGAA-3′ and R: 5′-ACACGATGAACTCACTGAA-3′) and β-actin primers (F: 5′-ATGTACGTTGCTATCCAGGC-3′ and R: 5′-CTCCTTAATGTCACGCACGAT-3′) and SYBR green mix (Roche, UK) according to the manufacturer’s protocols.

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Western Blot, Isolation

    Specific knock-down of S100P in Jeg-3 and Bewo trophoblastic cell lines. Bewo and Jeg-3 cells were incubated in the presence of different S100P or control siRNAs for 48 hours prior to collection for mRNA qPCR analysis ( A , D ) or 72 hours prior to collection for protein Western blotting ( B , C , E , F ). mRNAs were isolated using TRIS reagent followed by reverse transcription and quantitative PCR analysis using primers for S100P and β-actin, as indicated in Methods. Data is presented as 2 ∆ CT mean values ± SD of 3 independent samples of a representative experiment compared to non-treated control samples. ***P

    Journal: Scientific Reports

    Article Title: S100P enhances the motility and invasion of human trophoblast cell lines

    doi: 10.1038/s41598-018-29852-2

    Figure Lengend Snippet: Specific knock-down of S100P in Jeg-3 and Bewo trophoblastic cell lines. Bewo and Jeg-3 cells were incubated in the presence of different S100P or control siRNAs for 48 hours prior to collection for mRNA qPCR analysis ( A , D ) or 72 hours prior to collection for protein Western blotting ( B , C , E , F ). mRNAs were isolated using TRIS reagent followed by reverse transcription and quantitative PCR analysis using primers for S100P and β-actin, as indicated in Methods. Data is presented as 2 ∆ CT mean values ± SD of 3 independent samples of a representative experiment compared to non-treated control samples. ***P

    Article Snippet: qPCR analysis Following the appropriate incubation, trophoblast cells were collected after trypsinisation and mRNA extraction was carried out using TRIS reagent (Sigma, UK) according to the manufacturer’s protocol. qPCR was performed using S100P (sequences F: 5′-TCAAGGTGCTGATGGAGAA-3′ and R: 5′-ACACGATGAACTCACTGAA-3′) and β-actin primers (F: 5′-ATGTACGTTGCTATCCAGGC-3′ and R: 5′-CTCCTTAATGTCACGCACGAT-3′) and SYBR green mix (Roche, UK) according to the manufacturer’s protocols.

    Techniques: Incubation, Real-time Polymerase Chain Reaction, Western Blot, Isolation

    2DE gel (11 cm, pH 4–7, Bis-Tris 12%) showing all the protein spots detected in nacre WSM from Crassostrea gigas . Numbered spots represent proteins identified by mass spectrometry.

    Journal: The Scientific World Journal

    Article Title: Identification of Proteins with Potential Osteogenic Activity Present in the Water-Soluble Matrix Proteins from Crassostrea gigas Nacre Using a Proteomic Approach

    doi: 10.1100/2012/765909

    Figure Lengend Snippet: 2DE gel (11 cm, pH 4–7, Bis-Tris 12%) showing all the protein spots detected in nacre WSM from Crassostrea gigas . Numbered spots represent proteins identified by mass spectrometry.

    Article Snippet: After the alkylation step, each strip was quickly washed with MOPS running buffer pH 7,7 (50 mM MOPS, 50 mM Tris, 0,1% (w/v), and 1 mM EDTA) and loaded on 13,3 × 8,7 cm Criterion XT gels (Bio-Rad) with the wells previously filled with an agarose solution for 2DE, composed of 0,5% (w/v) low melting point agarose, 25 mM Tris, 192 mM glycine, 0,1% (w/v) SDS, and vestigial quantities of bromophenol blue (Bio-Rad).

    Techniques: Two-Dimensional Gel Electrophoresis, Mass Spectrometry

    (Panel A ) Minocycline (20 µM) in the presence of 3 mM Ca 2+ induces an electrical current in BLM made from DPhPC. The experimental buffer was 10 mM Tris, 10 mM MES, 100 mM KCl, pH 8.5; the voltage was 30 mV. (Panels B, C ) Ion channel activity induced by minocycline (8 µM) in the presence of Ca 2+ (3 mM in panel B and 20 µM in panel C) at 50 mV in BLM made from DPhPC. The experimental buffer was 10 mM Tris, 10 mM MES, 1 M KCl, pH 9.0. (A current of 0.7 pA at 50 mV corresponds to a conductance of 14 pS)

    Journal: Journal of bioenergetics and biomembranes

    Article Title: Minocycline chelates Ca2+, binds to membranes, and depolarizes mitochondria by formation of Ca2+-dependent ion channels

    doi: 10.1007/s10863-010-9271-1

    Figure Lengend Snippet: (Panel A ) Minocycline (20 µM) in the presence of 3 mM Ca 2+ induces an electrical current in BLM made from DPhPC. The experimental buffer was 10 mM Tris, 10 mM MES, 100 mM KCl, pH 8.5; the voltage was 30 mV. (Panels B, C ) Ion channel activity induced by minocycline (8 µM) in the presence of Ca 2+ (3 mM in panel B and 20 µM in panel C) at 50 mV in BLM made from DPhPC. The experimental buffer was 10 mM Tris, 10 mM MES, 1 M KCl, pH 9.0. (A current of 0.7 pA at 50 mV corresponds to a conductance of 14 pS)

    Article Snippet: β-Alanine, micro Biuret protein assay kit, bovine serum albumin (fatty acid free grade Sigma A-6003), CaCl2 , EGTA, gramicidin A, Hepes (ultra grade), minocycline, KCl, KOH, KH2 PO4 , MES, Ruthenium 360 (Ru360), succinate, sucrose (ultra grade), PBS-Tween buffer, and Tris-base were obtained from Sigma (St. Louis, MO, USA).

    Techniques: Activity Assay

    ( A ) ChIP experiment to determine the occupancy of hras -1, hras -2 and control sequence (870 bp downstream from TSS) by hnRNP A1. Histograms shows the relative occupancy of hras -1 and hras -2 by hnRNP A1, RNA Pol II (positive control) and IgG (negative control). Data have been normalized by IgG signal; ( B ) EMSA of 32 P-labelled hras -1 Y and hras -2 Y in 50 mM Tris-acetate pH 5.5, 50 mM KCl, incubated 40 min at room temperature with increasing amounts of recombinant hnRNP A1 (0–12 μg). Lane (Δ,A1) indicates the i M incubated 40 min at room temperature, with denatured hnRNPA1 in binding buffer (see Methods); ( C ) EMSA at pH 5.5 of hras -1 Y with BSA or denatured hnRNP A1 and EMSA of hras -1 Y (m) with hnRNP A1; ss = single-stranded oligonucleotide; 1:1 and 1:2 DNA-protein complexes.

    Journal: Scientific Reports

    Article Title: GC-elements controlling HRAS transcription form i-motif structures unfolded by heterogeneous ribonucleoprotein particle A1

    doi: 10.1038/srep18097

    Figure Lengend Snippet: ( A ) ChIP experiment to determine the occupancy of hras -1, hras -2 and control sequence (870 bp downstream from TSS) by hnRNP A1. Histograms shows the relative occupancy of hras -1 and hras -2 by hnRNP A1, RNA Pol II (positive control) and IgG (negative control). Data have been normalized by IgG signal; ( B ) EMSA of 32 P-labelled hras -1 Y and hras -2 Y in 50 mM Tris-acetate pH 5.5, 50 mM KCl, incubated 40 min at room temperature with increasing amounts of recombinant hnRNP A1 (0–12 μg). Lane (Δ,A1) indicates the i M incubated 40 min at room temperature, with denatured hnRNPA1 in binding buffer (see Methods); ( C ) EMSA at pH 5.5 of hras -1 Y with BSA or denatured hnRNP A1 and EMSA of hras -1 Y (m) with hnRNP A1; ss = single-stranded oligonucleotide; 1:1 and 1:2 DNA-protein complexes.

    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).

    Techniques: Chromatin Immunoprecipitation, Sequencing, Positive Control, Negative Control, Incubation, Recombinant, Binding Assay

    Circular dichroism analysis of 3 μM (0.5 cm pathlength cell) hras -1 Y and hras -2 Y at pH 5.5, 50 mM Tris-acetate, 50 mM KCl, after incubation with increasing amounts of hnRNP A1 (r = 0–4). Spectra of DNA-protein complex have been subtracted of protein spectrum.

    Journal: Scientific Reports

    Article Title: GC-elements controlling HRAS transcription form i-motif structures unfolded by heterogeneous ribonucleoprotein particle A1

    doi: 10.1038/srep18097

    Figure Lengend Snippet: Circular dichroism analysis of 3 μM (0.5 cm pathlength cell) hras -1 Y and hras -2 Y at pH 5.5, 50 mM Tris-acetate, 50 mM KCl, after incubation with increasing amounts of hnRNP A1 (r = 0–4). Spectra of DNA-protein complex have been subtracted of protein spectrum.

    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).

    Techniques: Incubation

    ( A ) Sequences of the GC-rich elements located in the HRAS promoter upstream of major TSS’s; ( B,C ) Circular dichroism titrations of hras -1 Y and hras -2 Y (3 μM, 1 cm pathlength cell) in 50 mM Tris-acetate, 50 mM KCl, 40% PEG-300 and pH from 4.5 to 8; ( D ) Ellipticity (287 nm) versus pH curves for hras -1 Y and hras -2 Y in the presence and absence of PEG-300; ( E ) Determination of number of protons picked up by hras -1 Y and hras -2 Y upon folding into the i M.

    Journal: Scientific Reports

    Article Title: GC-elements controlling HRAS transcription form i-motif structures unfolded by heterogeneous ribonucleoprotein particle A1

    doi: 10.1038/srep18097

    Figure Lengend Snippet: ( A ) Sequences of the GC-rich elements located in the HRAS promoter upstream of major TSS’s; ( B,C ) Circular dichroism titrations of hras -1 Y and hras -2 Y (3 μM, 1 cm pathlength cell) in 50 mM Tris-acetate, 50 mM KCl, 40% PEG-300 and pH from 4.5 to 8; ( D ) Ellipticity (287 nm) versus pH curves for hras -1 Y and hras -2 Y in the presence and absence of PEG-300; ( E ) Determination of number of protons picked up by hras -1 Y and hras -2 Y upon folding into the i M.

    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).

    Techniques:

    Characterization of LMW-HA and its effects on EC proliferation. Panel A , to evaluate the molecular weight ( MW ) and purity of our LMW-HA preparation, a 4–20% Tris borate-EDTA ( TBE ) gel was run with HA molecular weight standards (Select-HA TM 75–150

    Journal: The Journal of Biological Chemistry

    Article Title: Transactivation of the Receptor-tyrosine Kinase Ephrin Receptor A2 Is Required for the Low Molecular Weight Hyaluronan-mediated Angiogenesis That Is implicated in Tumor Progression *

    doi: 10.1074/jbc.M114.554766

    Figure Lengend Snippet: Characterization of LMW-HA and its effects on EC proliferation. Panel A , to evaluate the molecular weight ( MW ) and purity of our LMW-HA preparation, a 4–20% Tris borate-EDTA ( TBE ) gel was run with HA molecular weight standards (Select-HA TM 75–150

    Article Snippet: LMW-HA with HA standards (Sigma and Enzo Life Sciences) was run on 4–20% Tris borate-EDTA gels and stained with Stains-All (Sigma) to confirm LMW-HA purity and size.

    Techniques: Molecular Weight

    The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in TRIS buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).

    Journal: Sensors (Basel, Switzerland)

    Article Title: Oriented Immobilization of His-Tagged Protein on a Redox Active Thiol Derivative of DPTA-Cu(II) Layer Deposited on a Gold Electrode--The Base of Electrochemical Biosensors

    doi: 10.3390/s130911586

    Figure Lengend Snippet: The relationship of relative Cu(II) redox current decrease vs. concentration of: ( A ) Aβ 16–23′ measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE V natural domain (▴)-in TRSI buffer; Au/NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain (▪)-in TRIS buffer (n = 7); ( B ) Aβ 1–40 measured with electrodes: Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain (▴)-in TRIS buffer, (♦)-in the presence of diluted human plasma; Au/NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain (▪)-in TRIS buffer (n = 7).

    Article Snippet: Materials and Chemicals N -Acetylcysteamine (NAC), TRIS-hydrochloride, copper (II) acetate, chloroform, potassium chloride, sodium chloride were obtained from Sigma-Aldrich (Poznań, Poland).

    Techniques: Concentration Assay

    The OSWV responses of: ( A ) Au-NAC/DPTA–Cu(II)–His 6 –RAGE V natural domain, ( B ) Au-NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain towards Aβ 16–23′ in the presence of 50 mM TRIS hydrochloride, 300 mM NaCl, pH 7.4. (a) 0.000, (b) 0.001, (c) 0.010, (d) 0.100, (e) 1.000 (μM).

    Journal: Sensors (Basel, Switzerland)

    Article Title: Oriented Immobilization of His-Tagged Protein on a Redox Active Thiol Derivative of DPTA-Cu(II) Layer Deposited on a Gold Electrode--The Base of Electrochemical Biosensors

    doi: 10.3390/s130911586

    Figure Lengend Snippet: The OSWV responses of: ( A ) Au-NAC/DPTA–Cu(II)–His 6 –RAGE V natural domain, ( B ) Au-NAC/DPTA–Cu(II)–His 6 –RAGE V mutated domain towards Aβ 16–23′ in the presence of 50 mM TRIS hydrochloride, 300 mM NaCl, pH 7.4. (a) 0.000, (b) 0.001, (c) 0.010, (d) 0.100, (e) 1.000 (μM).

    Article Snippet: Materials and Chemicals N -Acetylcysteamine (NAC), TRIS-hydrochloride, copper (II) acetate, chloroform, potassium chloride, sodium chloride were obtained from Sigma-Aldrich (Poznań, Poland).

    Techniques:

    The OSWV responses of: ( A) Au-NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain, ( B ) Au-NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain towards Aβ 1–40 in the presence of 50 mM TRIS hydrochloride, 300 mM NaCl, pH 7.4: (a) 0.000, (b) 0.001, (c) 0.010, (d) 0.100, (e) 1.000 [μM].

    Journal: Sensors (Basel, Switzerland)

    Article Title: Oriented Immobilization of His-Tagged Protein on a Redox Active Thiol Derivative of DPTA-Cu(II) Layer Deposited on a Gold Electrode--The Base of Electrochemical Biosensors

    doi: 10.3390/s130911586

    Figure Lengend Snippet: The OSWV responses of: ( A) Au-NAC/DPTA–Cu(II)–His 6 –RAGE VC1 natural domain, ( B ) Au-NAC/DPTA–Cu(II)–His 6 –RAGE VC1 mutated domain towards Aβ 1–40 in the presence of 50 mM TRIS hydrochloride, 300 mM NaCl, pH 7.4: (a) 0.000, (b) 0.001, (c) 0.010, (d) 0.100, (e) 1.000 [μM].

    Article Snippet: Materials and Chemicals N -Acetylcysteamine (NAC), TRIS-hydrochloride, copper (II) acetate, chloroform, potassium chloride, sodium chloride were obtained from Sigma-Aldrich (Poznań, Poland).

    Techniques:

    Neu3 behaves as an integral membrane protein. ( a ) Soluble (S, first lane) and membrane (P, second lane) fractions of NEU3 -transfected cells were obtained as described in Fig. 1a . The latter fraction was then incubated for 40 min on ice with Tris buffer (control) or Na 2 CO 3 at pH 11.5 in order to extract peripheral membrane proteins. After treatment, membranes were collected by ultracentrifugation, and membrane-bound (P, fourth and sixth lanes) and solubilized (S, third and fifth lanes) proteins were analyzed by Western blotting using anti-Neu3 antibody. K-Ras and Cav-1 were used as markers of an extractable and a non-extractable membrane protein, respectively. Tub was used as a marker of a soluble protein. ( b ) Intact NEU3 -transfected cells were treated with (+) or without (−) 100 µg/ml proteinase K (PK) for 30 min at 37 °C. The remaining proteins were run on a SDS-PAGE gel and Western blotted with anti-c-Myc and anti-Neu3 antibodies. Transferrin Receptor (TfR) was used as a marker of a PK-accessible protein, whereas Cav-1 and sialyltransferase ST3Gal-II were used as markers of proteins not accessible to PK. The molecular masses in kDa of the standard proteins are shown on the left. ( c ) Antibody accessibility in permeabilized and non-permeabilized cells. The signal of the indicated antibodies were analyzed after fixation in cells treated with 0.1% saponin in PBS/BSA (permeabilized) or with PBS/BSA alone (non-permeabilized). Cav-1 was used as a marker of an inner membrane protein detected only after cell permeabilization, and GPI-YFP was used as a marker of an outer membrane protein accessible by antibody without permeabilization. Cells nuclei were stained blue with Hoechst dye. ( d ) Cell surface proteins exposed to the extracellular environment of NEU3 -transfected cells were biotinylated and isolated by streptavidin agarose pull-down. Biotinylated (B) and non-biotinylated (NB) fractions were analyzed by Western blotting. Endogenous marker Cav-1 was used as control of a membrane protein not exposed to the extracellular environment. Densitometric analysis indicating the percentage of Neu3 in each fraction is shown. ( e ) Kyte-Doolittle hydrophobicity plot for Neu3 sequence using a window size of 19. The red line corresponds to a hydrophobicity score of 1.6 and designates an empirical cutoff value for α-helix transmembrane segments of ~19 amino acids long.

    Journal: Scientific Reports

    Article Title: Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein

    doi: 10.1038/s41598-017-04488-w

    Figure Lengend Snippet: Neu3 behaves as an integral membrane protein. ( a ) Soluble (S, first lane) and membrane (P, second lane) fractions of NEU3 -transfected cells were obtained as described in Fig. 1a . The latter fraction was then incubated for 40 min on ice with Tris buffer (control) or Na 2 CO 3 at pH 11.5 in order to extract peripheral membrane proteins. After treatment, membranes were collected by ultracentrifugation, and membrane-bound (P, fourth and sixth lanes) and solubilized (S, third and fifth lanes) proteins were analyzed by Western blotting using anti-Neu3 antibody. K-Ras and Cav-1 were used as markers of an extractable and a non-extractable membrane protein, respectively. Tub was used as a marker of a soluble protein. ( b ) Intact NEU3 -transfected cells were treated with (+) or without (−) 100 µg/ml proteinase K (PK) for 30 min at 37 °C. The remaining proteins were run on a SDS-PAGE gel and Western blotted with anti-c-Myc and anti-Neu3 antibodies. Transferrin Receptor (TfR) was used as a marker of a PK-accessible protein, whereas Cav-1 and sialyltransferase ST3Gal-II were used as markers of proteins not accessible to PK. The molecular masses in kDa of the standard proteins are shown on the left. ( c ) Antibody accessibility in permeabilized and non-permeabilized cells. The signal of the indicated antibodies were analyzed after fixation in cells treated with 0.1% saponin in PBS/BSA (permeabilized) or with PBS/BSA alone (non-permeabilized). Cav-1 was used as a marker of an inner membrane protein detected only after cell permeabilization, and GPI-YFP was used as a marker of an outer membrane protein accessible by antibody without permeabilization. Cells nuclei were stained blue with Hoechst dye. ( d ) Cell surface proteins exposed to the extracellular environment of NEU3 -transfected cells were biotinylated and isolated by streptavidin agarose pull-down. Biotinylated (B) and non-biotinylated (NB) fractions were analyzed by Western blotting. Endogenous marker Cav-1 was used as control of a membrane protein not exposed to the extracellular environment. Densitometric analysis indicating the percentage of Neu3 in each fraction is shown. ( e ) Kyte-Doolittle hydrophobicity plot for Neu3 sequence using a window size of 19. The red line corresponds to a hydrophobicity score of 1.6 and designates an empirical cutoff value for α-helix transmembrane segments of ~19 amino acids long.

    Article Snippet: Subcellular fractionation Cells were washed with cold PBS and harvested by scraping in 5 mM Tris/HCl pH 7.0 (buffer T) supplemented with protease inhibitor cocktail (PIC) (Sigma-Aldrich, St Louis, MO, USA).

    Techniques: Transfection, Incubation, Western Blot, Marker, SDS Page, Staining, Isolation, Sequencing

    Effect of SAP on heat-induced GST aggregation in MES-Ca and Tris-EDTA buffers. ( a,c ) Time course of GST aggregation monitored by turbidity in the absence (black diamond) or presence of 1:10 (molar ratio of SAP to GST) (orange circle), 1:5 (red circle), or 1:2 (dark brown circle) SAP in MES-Ca buffer ( a ), or 1:10 (right green circle), 1:5 (green circle), or 1:2 (dark green circle) SAP in Tris-EDTA buffer ( c ) at 43 °C. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b,d ) Turbidity of each sample at 32 h in MES-Ca ( b ) and Tris-EDTA buffers ( d ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. **P

    Journal: Scientific Reports

    Article Title: Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro

    doi: 10.1038/srep29077

    Figure Lengend Snippet: Effect of SAP on heat-induced GST aggregation in MES-Ca and Tris-EDTA buffers. ( a,c ) Time course of GST aggregation monitored by turbidity in the absence (black diamond) or presence of 1:10 (molar ratio of SAP to GST) (orange circle), 1:5 (red circle), or 1:2 (dark brown circle) SAP in MES-Ca buffer ( a ), or 1:10 (right green circle), 1:5 (green circle), or 1:2 (dark green circle) SAP in Tris-EDTA buffer ( c ) at 43 °C. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b,d ) Turbidity of each sample at 32 h in MES-Ca ( b ) and Tris-EDTA buffers ( d ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. **P

    Article Snippet: D76N β2-m amyloid fibril formation and ThT assay The reaction mixture (200 μL) that contained 30 μM D76N β2-m, 0–1.5 μM CRP, SAP, or AGP, Tris-EDTA (pH 7.5), Tris-Ca (pH 7.5), MES-Ca (pH 7.0), or MES-EDTA buffer (pH 7.0), and 5 μM ThT was incubated with shaking (800 rpm) at 37 °C in a 96-well plate (237105, Thermo Fisher Scientific, Nunc A/S, Roskilde, Denmark) sealed with sealing film.

    Techniques:

    Effects of CRP and SAP on Aβ(1-40) amyloid fibril formation in Ca 2+ -free Tris-EDTA buffer. ( a ) Time course of fibril formation monitored by ThT fluorescence in the absence (black diamond) or presence of 1:500 (molar ratio of CRP to Aβ(1-40)) (light blue square), 1:100 (blue square), or 1:20 (dark blue square) CRP, or 1:500 (orange circle), 1:100 (red circle), or 1:20 (dark brown circle) SAP. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b ) ThT fluorescence of each sample at 156 h in ( a ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. *P

    Journal: Scientific Reports

    Article Title: Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro

    doi: 10.1038/srep29077

    Figure Lengend Snippet: Effects of CRP and SAP on Aβ(1-40) amyloid fibril formation in Ca 2+ -free Tris-EDTA buffer. ( a ) Time course of fibril formation monitored by ThT fluorescence in the absence (black diamond) or presence of 1:500 (molar ratio of CRP to Aβ(1-40)) (light blue square), 1:100 (blue square), or 1:20 (dark blue square) CRP, or 1:500 (orange circle), 1:100 (red circle), or 1:20 (dark brown circle) SAP. Each point represents the average of three independent incubations. Representative data of three independent experiments are shown. ( b ) ThT fluorescence of each sample at 156 h in ( a ). The data are mean ± SD of three independent incubations. Statistical analysis was performed by unpaired Student’s t-test. *P

    Article Snippet: D76N β2-m amyloid fibril formation and ThT assay The reaction mixture (200 μL) that contained 30 μM D76N β2-m, 0–1.5 μM CRP, SAP, or AGP, Tris-EDTA (pH 7.5), Tris-Ca (pH 7.5), MES-Ca (pH 7.0), or MES-EDTA buffer (pH 7.0), and 5 μM ThT was incubated with shaking (800 rpm) at 37 °C in a 96-well plate (237105, Thermo Fisher Scientific, Nunc A/S, Roskilde, Denmark) sealed with sealing film.

    Techniques: Fluorescence

    Structure and assembly states of CRP and SAP. ( a,b ) Structures of pentameric CRP and SAP. These figures were prepared with the PDB files 1B09 for CRP ( a ) and 1SAC for SAP ( b ) using the software PyMOL. Pentamers were viewed along the 5-fold axis of symmetry from the A face (upper) and perpendicular to the 5-fold axis (lower). Yellow: calcium ions. ( c–f ) Analysis of molecular weight distribution of CRP and SAP by gel filtration chromatography. CRP ( c,d ) and SAP ( e,f ) at 1.5 μM were incubated in Tris-EDTA (pH 7.5) ( c,e ), Tris-Ca (pH 7.5) ( d ), or MES-Ca buffer (pH 7.0) ( f ) at 37 °C for 0 (black line) or 72 h (red line), then 300 μL aliquots were applied on a column equilibrated and eluted with the same buffer at 15 °C. Elution was monitored by absorbance at 280 nm. Arrows in each figure indicate the elution volumes of molecular weight markers (kDa).

    Journal: Scientific Reports

    Article Title: Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro

    doi: 10.1038/srep29077

    Figure Lengend Snippet: Structure and assembly states of CRP and SAP. ( a,b ) Structures of pentameric CRP and SAP. These figures were prepared with the PDB files 1B09 for CRP ( a ) and 1SAC for SAP ( b ) using the software PyMOL. Pentamers were viewed along the 5-fold axis of symmetry from the A face (upper) and perpendicular to the 5-fold axis (lower). Yellow: calcium ions. ( c–f ) Analysis of molecular weight distribution of CRP and SAP by gel filtration chromatography. CRP ( c,d ) and SAP ( e,f ) at 1.5 μM were incubated in Tris-EDTA (pH 7.5) ( c,e ), Tris-Ca (pH 7.5) ( d ), or MES-Ca buffer (pH 7.0) ( f ) at 37 °C for 0 (black line) or 72 h (red line), then 300 μL aliquots were applied on a column equilibrated and eluted with the same buffer at 15 °C. Elution was monitored by absorbance at 280 nm. Arrows in each figure indicate the elution volumes of molecular weight markers (kDa).

    Article Snippet: D76N β2-m amyloid fibril formation and ThT assay The reaction mixture (200 μL) that contained 30 μM D76N β2-m, 0–1.5 μM CRP, SAP, or AGP, Tris-EDTA (pH 7.5), Tris-Ca (pH 7.5), MES-Ca (pH 7.0), or MES-EDTA buffer (pH 7.0), and 5 μM ThT was incubated with shaking (800 rpm) at 37 °C in a 96-well plate (237105, Thermo Fisher Scientific, Nunc A/S, Roskilde, Denmark) sealed with sealing film.

    Techniques: Software, Molecular Weight, Filtration, Chromatography, Incubation

    Interactions of CRP and SAP with fresh and aggregated Aβ(1-40) and D76N β2-m. ( a–f ) Binding of Aβ(1-40) ( a–c ) and D76N β2-m ( d–f ) to immobilized CRP and SAP. CRP and SAP were immobilized on an ELISA plate and incubated with fresh ( f ) and aggregated (ag) Aβ(1-40) and D76N β2-m in Tris-EDTA ( a,d ), Tris-Ca ( b,e ), or MES-Ca buffer ( c,f ). The data are mean ± SD of three independent incubations. Representative data of three independent experiments are shown. ( g,h ) Crosslinking experiments. At 0 h (fresh mixture, f) and at the beginning of the growth phase (aggregated mixture, ag), the reaction mixture containing Aβ(1-40) or D76N β2-m was spiked with 1:20 CRP and SAP, and incubated for 30 min at 37 °C. After BS 3 was added to the mixture, SDS-PAGE (top) and western blotting analysis (bottom) were performed. In western blotting analysis, bound Aβ(1-40) and D76N β2-m were detected with anti-human Aβ(1-40) and β2-m antibodies, respectively.

    Journal: Scientific Reports

    Article Title: Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro

    doi: 10.1038/srep29077

    Figure Lengend Snippet: Interactions of CRP and SAP with fresh and aggregated Aβ(1-40) and D76N β2-m. ( a–f ) Binding of Aβ(1-40) ( a–c ) and D76N β2-m ( d–f ) to immobilized CRP and SAP. CRP and SAP were immobilized on an ELISA plate and incubated with fresh ( f ) and aggregated (ag) Aβ(1-40) and D76N β2-m in Tris-EDTA ( a,d ), Tris-Ca ( b,e ), or MES-Ca buffer ( c,f ). The data are mean ± SD of three independent incubations. Representative data of three independent experiments are shown. ( g,h ) Crosslinking experiments. At 0 h (fresh mixture, f) and at the beginning of the growth phase (aggregated mixture, ag), the reaction mixture containing Aβ(1-40) or D76N β2-m was spiked with 1:20 CRP and SAP, and incubated for 30 min at 37 °C. After BS 3 was added to the mixture, SDS-PAGE (top) and western blotting analysis (bottom) were performed. In western blotting analysis, bound Aβ(1-40) and D76N β2-m were detected with anti-human Aβ(1-40) and β2-m antibodies, respectively.

    Article Snippet: D76N β2-m amyloid fibril formation and ThT assay The reaction mixture (200 μL) that contained 30 μM D76N β2-m, 0–1.5 μM CRP, SAP, or AGP, Tris-EDTA (pH 7.5), Tris-Ca (pH 7.5), MES-Ca (pH 7.0), or MES-EDTA buffer (pH 7.0), and 5 μM ThT was incubated with shaking (800 rpm) at 37 °C in a 96-well plate (237105, Thermo Fisher Scientific, Nunc A/S, Roskilde, Denmark) sealed with sealing film.

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Incubation, SDS Page, Western Blot

    Hysteresis in DNA overstretching transition: ( a ) the extension-time graph of the DNA during a reversible overstretching transition. This experiment is done on 1× Tris-EDTA (TE) buffer with 150 mM NaCl at room temperature. Looking left to right, the extensional and contractile phases are symmetrical; ( b ) the extension-time graph of the DNA during a hysteretic overstretching transition. This experiment is done on 1× TE buffer in the absence of salt at room temperature. Looking left to right, the asymmetry between the extensional and contractile responses is clear visible. Bead-magnet distance are adjusted at a speed of 10 μm/s in ( a , b ).

    Journal: Micromachines

    Article Title: A Horizontal Magnetic Tweezers and Its Use for Studying Single DNA Molecules

    doi: 10.3390/mi9040188

    Figure Lengend Snippet: Hysteresis in DNA overstretching transition: ( a ) the extension-time graph of the DNA during a reversible overstretching transition. This experiment is done on 1× Tris-EDTA (TE) buffer with 150 mM NaCl at room temperature. Looking left to right, the extensional and contractile phases are symmetrical; ( b ) the extension-time graph of the DNA during a hysteretic overstretching transition. This experiment is done on 1× TE buffer in the absence of salt at room temperature. Looking left to right, the asymmetry between the extensional and contractile responses is clear visible. Bead-magnet distance are adjusted at a speed of 10 μm/s in ( a , b ).

    Article Snippet: The fourth step is to incubate in 1× Tris-EDTA (TE), 150 mM NaCl buffer (henceforth referred to as the “buffer”) at room temperature for about 10 min 5 µL end-functionalized DNA with 30 µL pre-washed 2.8 µm diameter superparamagnetic beads (11205D, Thermo Fisher Scientific, Waltham, MA, USA).

    Techniques:

    Methyl mercury exposure results in cortical accumulation of insoluble Tdp-43. Cortical tissue from mice exposed, by ingestion, to 0 ppm (no treatment, N  = 4) and 5 ppm methyl mercuric (II) chloride (MeHg, N  = 7) was fractionated by solubility. The sarkosyl insoluble (A) and total lysate (B) (TE: Tris-EDTA) fractions were immunoblotted and probed for endogenous Tdp-43. Upon systemic MeHg exposure, sarkosyl insoluble Tdp-43 (C) and high molecular weight (HMW) Tdp-43 (D) is significantly increased. Mean ±SEM; unpaired two-tailed t test, * p  

    Journal: Toxicological Sciences

    Article Title: Heavy Metal Neurotoxicants Induce ALS-Linked TDP-43 Pathology

    doi: 10.1093/toxsci/kfy267

    Figure Lengend Snippet: Methyl mercury exposure results in cortical accumulation of insoluble Tdp-43. Cortical tissue from mice exposed, by ingestion, to 0 ppm (no treatment, N  = 4) and 5 ppm methyl mercuric (II) chloride (MeHg, N  = 7) was fractionated by solubility. The sarkosyl insoluble (A) and total lysate (B) (TE: Tris-EDTA) fractions were immunoblotted and probed for endogenous Tdp-43. Upon systemic MeHg exposure, sarkosyl insoluble Tdp-43 (C) and high molecular weight (HMW) Tdp-43 (D) is significantly increased. Mean ±SEM; unpaired two-tailed t test, * p  

    Article Snippet: A total of ∼100 mg of frozen cortical tissue was lysed by bead mill (Thermo) homogenization in Tris-EDTA buffer (10 mM Tris pH8; 1 mM EDTA; 1 mM PMSF; 1× HALT PIC, and PhosSTOP [Roche]).

    Techniques: Mouse Assay, Solubility, Molecular Weight, Two Tailed Test