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  • 95
    Millipore tris hcl buffer
    <t>OMV</t> display protease activity. (A) Ten micrograms of OMV proteins was loaded on 10% <t>Tris-glycine</t> gel with 0.1% gelatin as the substrate. Following separation at denaturing conditions, proteins were renatured and then incubated at 37°C for 2 days to allow substrate cleavage. Colloidal Coomassie brilliant blue G-250 was used to stain the gel. Clear bands marked by the arrows indicate the digestion of gelatin by proteases. (B) Peptidase activity of B. fragilis vesicles was tested using different p -nitroanilide-linked amino acids. Ten micrograms of purified OMV proteins was incubated with different substrates for 1 h at 37°C. Activities were determined by measuring the absorbance of the released p -nitroanilide at 405 nm. All activities are represented relative to the alanine-peptidase activity. All experiments were done in triplicates.
    Tris Hcl Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 3974 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    N/A
    For recreating Screening Suite conditions Kit contents 200 ml 1M Tris hydroxymethyl aminomethane HCl pH 8 5
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    99
    Amresco tris hcl
    <t>OMV</t> display protease activity. (A) Ten micrograms of OMV proteins was loaded on 10% <t>Tris-glycine</t> gel with 0.1% gelatin as the substrate. Following separation at denaturing conditions, proteins were renatured and then incubated at 37°C for 2 days to allow substrate cleavage. Colloidal Coomassie brilliant blue G-250 was used to stain the gel. Clear bands marked by the arrows indicate the digestion of gelatin by proteases. (B) Peptidase activity of B. fragilis vesicles was tested using different p -nitroanilide-linked amino acids. Ten micrograms of purified OMV proteins was incubated with different substrates for 1 h at 37°C. Activities were determined by measuring the absorbance of the released p -nitroanilide at 405 nm. All activities are represented relative to the alanine-peptidase activity. All experiments were done in triplicates.
    Tris Hcl, supplied by Amresco, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Applichem tris hcl
    <t>OMV</t> display protease activity. (A) Ten micrograms of OMV proteins was loaded on 10% <t>Tris-glycine</t> gel with 0.1% gelatin as the substrate. Following separation at denaturing conditions, proteins were renatured and then incubated at 37°C for 2 days to allow substrate cleavage. Colloidal Coomassie brilliant blue G-250 was used to stain the gel. Clear bands marked by the arrows indicate the digestion of gelatin by proteases. (B) Peptidase activity of B. fragilis vesicles was tested using different p -nitroanilide-linked amino acids. Ten micrograms of purified OMV proteins was incubated with different substrates for 1 h at 37°C. Activities were determined by measuring the absorbance of the released p -nitroanilide at 405 nm. All activities are represented relative to the alanine-peptidase activity. All experiments were done in triplicates.
    Tris Hcl, supplied by Applichem, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad tris hcl
    Recombinant N-His 6 -GpsA protein is an active G3P dehydrogenase in vitro. R. prowazekii gpsA was cloned into pET15b, heterologously expressed in E. coli BL21(DE3), and purified with N-His 6 -GpsA. (A) Purified protein was resolved on a 4 to 15% <t>Tris-HCl</t> <t>SDS-polyacrylamide</t> gel and visualized by Imperial protein staining and Western blot analysis using anti-His 6 monoclonal antibody (sizes [in kDa] are indicated on the left). The mass spectrometry analysis coverage map shows matched peptides in bold font (30% coverage). (B) N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P was verified by paper chromatography. [ 32 P]ATP, [ 32 P]DHAP, [ 32 P]G3P, and [ 32 P]orthophosphate were used as standards. The reaction mixtures were incubated for 60 min at room temperature prior to chromatographic analysis. Lane A, a negative-control reaction mixture containing 6 μM [ 32 P]DHAP and 100 μM NADPH only; lane B, a negative-control reaction mixture containing [ 32 P]DHAP and 2.5 μg ml −1 N-His 6 -GpsA protein only; lane C, the N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P absolutely required the presence of NADPH. The density of each compound on the chromatograph is expressed as a percentage of the total lane density (summarized in tabular form to the right of each spot on the chromatograph). (C) N-His 6 -GpsA-catalyzed conversion of DHAP to G3P was measured spectrophotometrically at OD 340 by following the oxidation of NADPH or NADH over time. Error bars represent standard deviations. The reaction mixtures contained 1.0 μg ml −1 N-His 6 -GpsA, 500 μM DHAP, and 100 μM NAD(P)H in modified buffer A; and the reactions were carried out at room temperature.
    Tris Hcl, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 426 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    BioShop tris hcl
    Recombinant N-His 6 -GpsA protein is an active G3P dehydrogenase in vitro. R. prowazekii gpsA was cloned into pET15b, heterologously expressed in E. coli BL21(DE3), and purified with N-His 6 -GpsA. (A) Purified protein was resolved on a 4 to 15% <t>Tris-HCl</t> <t>SDS-polyacrylamide</t> gel and visualized by Imperial protein staining and Western blot analysis using anti-His 6 monoclonal antibody (sizes [in kDa] are indicated on the left). The mass spectrometry analysis coverage map shows matched peptides in bold font (30% coverage). (B) N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P was verified by paper chromatography. [ 32 P]ATP, [ 32 P]DHAP, [ 32 P]G3P, and [ 32 P]orthophosphate were used as standards. The reaction mixtures were incubated for 60 min at room temperature prior to chromatographic analysis. Lane A, a negative-control reaction mixture containing 6 μM [ 32 P]DHAP and 100 μM NADPH only; lane B, a negative-control reaction mixture containing [ 32 P]DHAP and 2.5 μg ml −1 N-His 6 -GpsA protein only; lane C, the N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P absolutely required the presence of NADPH. The density of each compound on the chromatograph is expressed as a percentage of the total lane density (summarized in tabular form to the right of each spot on the chromatograph). (C) N-His 6 -GpsA-catalyzed conversion of DHAP to G3P was measured spectrophotometrically at OD 340 by following the oxidation of NADPH or NADH over time. Error bars represent standard deviations. The reaction mixtures contained 1.0 μg ml −1 N-His 6 -GpsA, 500 μM DHAP, and 100 μM NAD(P)H in modified buffer A; and the reactions were carried out at room temperature.
    Tris Hcl, supplied by BioShop, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Boehringer Ingelheim tris hcl
    Recombinant N-His 6 -GpsA protein is an active G3P dehydrogenase in vitro. R. prowazekii gpsA was cloned into pET15b, heterologously expressed in E. coli BL21(DE3), and purified with N-His 6 -GpsA. (A) Purified protein was resolved on a 4 to 15% <t>Tris-HCl</t> <t>SDS-polyacrylamide</t> gel and visualized by Imperial protein staining and Western blot analysis using anti-His 6 monoclonal antibody (sizes [in kDa] are indicated on the left). The mass spectrometry analysis coverage map shows matched peptides in bold font (30% coverage). (B) N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P was verified by paper chromatography. [ 32 P]ATP, [ 32 P]DHAP, [ 32 P]G3P, and [ 32 P]orthophosphate were used as standards. The reaction mixtures were incubated for 60 min at room temperature prior to chromatographic analysis. Lane A, a negative-control reaction mixture containing 6 μM [ 32 P]DHAP and 100 μM NADPH only; lane B, a negative-control reaction mixture containing [ 32 P]DHAP and 2.5 μg ml −1 N-His 6 -GpsA protein only; lane C, the N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P absolutely required the presence of NADPH. The density of each compound on the chromatograph is expressed as a percentage of the total lane density (summarized in tabular form to the right of each spot on the chromatograph). (C) N-His 6 -GpsA-catalyzed conversion of DHAP to G3P was measured spectrophotometrically at OD 340 by following the oxidation of NADPH or NADH over time. Error bars represent standard deviations. The reaction mixtures contained 1.0 μg ml −1 N-His 6 -GpsA, 500 μM DHAP, and 100 μM NAD(P)H in modified buffer A; and the reactions were carried out at room temperature.
    Tris Hcl, supplied by Boehringer Ingelheim, used in various techniques. Bioz Stars score: 96/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Carl Roth GmbH tris hcl
    Alternating the media 10 mM <t>Tris-HCl</t> and <t>1×</t> PBS buffer for three consecutive runs. ( A ) Shows the minimum shift when exchanging the media. ( B ) Illustrates the changes in amplitude and its phase at a frequency of 251 Hz, when exchanging the media. Comparing the signals, when plotted in the same graph, reveals that the read-out systems detected the media exchange simultaneously, without influencing each other ( C ).
    Tris Hcl, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 99/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    HiMedia Laboratories tris hcl
    Alternating the media 10 mM <t>Tris-HCl</t> and <t>1×</t> PBS buffer for three consecutive runs. ( A ) Shows the minimum shift when exchanging the media. ( B ) Illustrates the changes in amplitude and its phase at a frequency of 251 Hz, when exchanging the media. Comparing the signals, when plotted in the same graph, reveals that the read-out systems detected the media exchange simultaneously, without influencing each other ( C ).
    Tris Hcl, supplied by HiMedia Laboratories, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Merck & Co tris hcl
    Cleavage of SC pUC19 DNA (50 μ M) by platinum complex (100 μ M) in the presence of H 2 O 2 (100 μ M), in 10 mM <t>Tris-HCl/1</t> mM <t>EDTA</t> buffer (pH 8.0). lane 1: DNA Marker; lane 2: DNA control; lane 3: DNA + complex; lane 4: DNA + complex 1 + H 2 O 2 ; lane 5: DNA + complex + H 2 O 2 + DMSO (4 μ L); lane 6: DNA + complex 1 + H 2 O 2 + NaN 3 (100 μ M).
    Tris Hcl, supplied by Merck & Co, used in various techniques. Bioz Stars score: 99/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Merck KGaA tris hcl
    Cleavage of SC pUC19 DNA (50 μ M) by platinum complex (100 μ M) in the presence of H 2 O 2 (100 μ M), in 10 mM <t>Tris-HCl/1</t> mM <t>EDTA</t> buffer (pH 8.0). lane 1: DNA Marker; lane 2: DNA control; lane 3: DNA + complex; lane 4: DNA + complex 1 + H 2 O 2 ; lane 5: DNA + complex + H 2 O 2 + DMSO (4 μ L); lane 6: DNA + complex 1 + H 2 O 2 + NaN 3 (100 μ M).
    Tris Hcl, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore tris hcl
    Cleavage of SC pUC19 DNA (50 μ M) by platinum complex (100 μ M) in the presence of H 2 O 2 (100 μ M), in 10 mM <t>Tris-HCl/1</t> mM <t>EDTA</t> buffer (pH 8.0). lane 1: DNA Marker; lane 2: DNA control; lane 3: DNA + complex; lane 4: DNA + complex 1 + H 2 O 2 ; lane 5: DNA + complex + H 2 O 2 + DMSO (4 μ L); lane 6: DNA + complex 1 + H 2 O 2 + NaN 3 (100 μ M).
    Tris Hcl, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2638 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Shanghai BioScience tris hcl
    Cleavage of SC pUC19 DNA (50 μ M) by platinum complex (100 μ M) in the presence of H 2 O 2 (100 μ M), in 10 mM <t>Tris-HCl/1</t> mM <t>EDTA</t> buffer (pH 8.0). lane 1: DNA Marker; lane 2: DNA control; lane 3: DNA + complex; lane 4: DNA + complex 1 + H 2 O 2 ; lane 5: DNA + complex + H 2 O 2 + DMSO (4 μ L); lane 6: DNA + complex 1 + H 2 O 2 + NaN 3 (100 μ M).
    Tris Hcl, supplied by Shanghai BioScience, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1238 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Avantor tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by Avantor, used in various techniques. Bioz Stars score: 96/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Beyotime tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by Beyotime, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Fisher Scientific tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 99/100, based on 65 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 793 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Mediatech tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by Mediatech, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Nacalai tris hcl
    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) <t>Tris:TSB</t> treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM <t>BME.</t> The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .
    Tris Hcl, supplied by Nacalai, used in various techniques. Bioz Stars score: 99/100, based on 58 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
    Tris Hcl, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 2275 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    3M Co tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
    Tris Hcl, supplied by 3M Co, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Alere tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    FUJIFILM tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Teknova tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Applygen Technologies tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
    Tris Hcl, supplied by Applygen Technologies, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biomol GmbH tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Ciphergen tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Wisent Corporation tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Biosolve tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Duchefa tris hcl
    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM <t>Tris</t> pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to <t>SDS–PAGE.</t> Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.
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    Image Search Results


    OMV display protease activity. (A) Ten micrograms of OMV proteins was loaded on 10% Tris-glycine gel with 0.1% gelatin as the substrate. Following separation at denaturing conditions, proteins were renatured and then incubated at 37°C for 2 days to allow substrate cleavage. Colloidal Coomassie brilliant blue G-250 was used to stain the gel. Clear bands marked by the arrows indicate the digestion of gelatin by proteases. (B) Peptidase activity of B. fragilis vesicles was tested using different p -nitroanilide-linked amino acids. Ten micrograms of purified OMV proteins was incubated with different substrates for 1 h at 37°C. Activities were determined by measuring the absorbance of the released p -nitroanilide at 405 nm. All activities are represented relative to the alanine-peptidase activity. All experiments were done in triplicates.

    Journal: mBio

    Article Title: Preferential Packing of Acidic Glycosidases and Proteases into Bacteroides Outer Membrane Vesicles

    doi: 10.1128/mBio.00909-14

    Figure Lengend Snippet: OMV display protease activity. (A) Ten micrograms of OMV proteins was loaded on 10% Tris-glycine gel with 0.1% gelatin as the substrate. Following separation at denaturing conditions, proteins were renatured and then incubated at 37°C for 2 days to allow substrate cleavage. Colloidal Coomassie brilliant blue G-250 was used to stain the gel. Clear bands marked by the arrows indicate the digestion of gelatin by proteases. (B) Peptidase activity of B. fragilis vesicles was tested using different p -nitroanilide-linked amino acids. Ten micrograms of purified OMV proteins was incubated with different substrates for 1 h at 37°C. Activities were determined by measuring the absorbance of the released p -nitroanilide at 405 nm. All activities are represented relative to the alanine-peptidase activity. All experiments were done in triplicates.

    Article Snippet: The peptidase enzyme activity was determined by incubation of 10 µg of the quantified OMV proteins in a 50 mM Tris-HCl buffer (pH 6.5), with 200 µl of 50 mM l -lysine-p -nitroanilide dihydrobromide, l -alanine-p -nitroanilide hydrochloride, l -leucine-p-nitroanilide, or pyroglutamic acid-p -nitroanilide (Sigma-Aldrich), for 1 h at 37°C.

    Techniques: Activity Assay, Incubation, Staining, Purification

    Recombinant N-His 6 -GpsA protein is an active G3P dehydrogenase in vitro. R. prowazekii gpsA was cloned into pET15b, heterologously expressed in E. coli BL21(DE3), and purified with N-His 6 -GpsA. (A) Purified protein was resolved on a 4 to 15% Tris-HCl SDS-polyacrylamide gel and visualized by Imperial protein staining and Western blot analysis using anti-His 6 monoclonal antibody (sizes [in kDa] are indicated on the left). The mass spectrometry analysis coverage map shows matched peptides in bold font (30% coverage). (B) N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P was verified by paper chromatography. [ 32 P]ATP, [ 32 P]DHAP, [ 32 P]G3P, and [ 32 P]orthophosphate were used as standards. The reaction mixtures were incubated for 60 min at room temperature prior to chromatographic analysis. Lane A, a negative-control reaction mixture containing 6 μM [ 32 P]DHAP and 100 μM NADPH only; lane B, a negative-control reaction mixture containing [ 32 P]DHAP and 2.5 μg ml −1 N-His 6 -GpsA protein only; lane C, the N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P absolutely required the presence of NADPH. The density of each compound on the chromatograph is expressed as a percentage of the total lane density (summarized in tabular form to the right of each spot on the chromatograph). (C) N-His 6 -GpsA-catalyzed conversion of DHAP to G3P was measured spectrophotometrically at OD 340 by following the oxidation of NADPH or NADH over time. Error bars represent standard deviations. The reaction mixtures contained 1.0 μg ml −1 N-His 6 -GpsA, 500 μM DHAP, and 100 μM NAD(P)H in modified buffer A; and the reactions were carried out at room temperature.

    Journal: Journal of Bacteriology

    Article Title: Rickettsia prowazekii Uses an sn-Glycerol-3-Phosphate Dehydrogenase and a Novel Dihydroxyacetone Phosphate Transport System To Supply Triose Phosphate for Phospholipid Biosynthesis ▿

    doi: 10.1128/JB.00443-10

    Figure Lengend Snippet: Recombinant N-His 6 -GpsA protein is an active G3P dehydrogenase in vitro. R. prowazekii gpsA was cloned into pET15b, heterologously expressed in E. coli BL21(DE3), and purified with N-His 6 -GpsA. (A) Purified protein was resolved on a 4 to 15% Tris-HCl SDS-polyacrylamide gel and visualized by Imperial protein staining and Western blot analysis using anti-His 6 monoclonal antibody (sizes [in kDa] are indicated on the left). The mass spectrometry analysis coverage map shows matched peptides in bold font (30% coverage). (B) N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P was verified by paper chromatography. [ 32 P]ATP, [ 32 P]DHAP, [ 32 P]G3P, and [ 32 P]orthophosphate were used as standards. The reaction mixtures were incubated for 60 min at room temperature prior to chromatographic analysis. Lane A, a negative-control reaction mixture containing 6 μM [ 32 P]DHAP and 100 μM NADPH only; lane B, a negative-control reaction mixture containing [ 32 P]DHAP and 2.5 μg ml −1 N-His 6 -GpsA protein only; lane C, the N-His 6 -GpsA-catalyzed conversion of [ 32 P]DHAP to [ 32 P]G3P absolutely required the presence of NADPH. The density of each compound on the chromatograph is expressed as a percentage of the total lane density (summarized in tabular form to the right of each spot on the chromatograph). (C) N-His 6 -GpsA-catalyzed conversion of DHAP to G3P was measured spectrophotometrically at OD 340 by following the oxidation of NADPH or NADH over time. Error bars represent standard deviations. The reaction mixtures contained 1.0 μg ml −1 N-His 6 -GpsA, 500 μM DHAP, and 100 μM NAD(P)H in modified buffer A; and the reactions were carried out at room temperature.

    Article Snippet: Protein purification was verified by electrophoresis using a 4 to 15% Tris-HCl, SDS-polyacrylamide gel (Bio-Rad) and visualized by staining with Imperial protein stain (Bio-Rad).

    Techniques: Recombinant, In Vitro, Clone Assay, Purification, Staining, Western Blot, Mass Spectrometry, Paper Chromatography, Incubation, Negative Control, Modification

    Alternating the media 10 mM Tris-HCl and 1× PBS buffer for three consecutive runs. ( A ) Shows the minimum shift when exchanging the media. ( B ) Illustrates the changes in amplitude and its phase at a frequency of 251 Hz, when exchanging the media. Comparing the signals, when plotted in the same graph, reveals that the read-out systems detected the media exchange simultaneously, without influencing each other ( C ).

    Journal: Sensors (Basel, Switzerland)

    Article Title: Combining Electrochemical Impedance Spectroscopy and Surface Plasmon Resonance into one Simultaneous Read-Out System for the Detection of Surface Interactions

    doi: 10.3390/s131114650

    Figure Lengend Snippet: Alternating the media 10 mM Tris-HCl and 1× PBS buffer for three consecutive runs. ( A ) Shows the minimum shift when exchanging the media. ( B ) Illustrates the changes in amplitude and its phase at a frequency of 251 Hz, when exchanging the media. Comparing the signals, when plotted in the same graph, reveals that the read-out systems detected the media exchange simultaneously, without influencing each other ( C ).

    Article Snippet: Proof of Principle To assess the working principle of the combined unit, the reaction chamber of the PDMS flow-cell was filled sequentially with 10 mM Tris-HCl (Carl Roth, Karlsruhe, Germany) and 1× PBS buffer (pH 7.4; GIBCO Life Technologies GmbH, Darmstadt, Germany).

    Techniques:

    Cleavage of SC pUC19 DNA (50 μ M) by platinum complex (100 μ M) in the presence of H 2 O 2 (100 μ M), in 10 mM Tris-HCl/1 mM EDTA buffer (pH 8.0). lane 1: DNA Marker; lane 2: DNA control; lane 3: DNA + complex; lane 4: DNA + complex 1 + H 2 O 2 ; lane 5: DNA + complex + H 2 O 2 + DMSO (4 μ L); lane 6: DNA + complex 1 + H 2 O 2 + NaN 3 (100 μ M).

    Journal: Bioinorganic Chemistry and Applications

    Article Title: DNA Interaction and DNA Cleavage Studies of a New Platinum(II) Complex Containing Aliphatic and Aromatic Dinitrogen Ligands

    doi: 10.1155/2011/525794

    Figure Lengend Snippet: Cleavage of SC pUC19 DNA (50 μ M) by platinum complex (100 μ M) in the presence of H 2 O 2 (100 μ M), in 10 mM Tris-HCl/1 mM EDTA buffer (pH 8.0). lane 1: DNA Marker; lane 2: DNA control; lane 3: DNA + complex; lane 4: DNA + complex 1 + H 2 O 2 ; lane 5: DNA + complex + H 2 O 2 + DMSO (4 μ L); lane 6: DNA + complex 1 + H 2 O 2 + NaN 3 (100 μ M).

    Article Snippet: Materials 4,7-diphenyl-1,10-phenanthroline (DIP), N,N -dimethyltrimethylenediamine, hydrazine dihydrochloride, potassium Chloride, nitric acid, Tris-acetate-EDTA (TAE) buffer, hydrogen peroxide, NaN3 , and Tris-HCl were purchased from Merck.

    Techniques: Marker

    Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) Tris:TSB treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM BME. The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .

    Journal: Metallomics : integrated biometal science

    Article Title: Human Calprotectin Affects the Redox Speciation of Iron

    doi: 10.1039/c7mt00044h

    Figure Lengend Snippet: Iron depletion by CP-Ser, ΔHis 3 Asp and ΔHis 4 under aerobic conditions. (A) Cartoon schematic of the metal-depletion assay. Bacterial growth medium was treated with 10.5 μM CP (250 μg/mL) and incubated at 30 ºC, 150 rpm. At a given time point, an aliquot of medium was transferred to a spin filter. Following centrifugation to remove CP, and the CP-treated medium was analyzed by ICP-MS. (B–D) Tris:TSB treated CP-Ser, ΔHis 3 Asp, or ΔHis 4 in the absence (black) or presence (red) of ≈3 mM BME. The metal content in the CP-treated medium was analyzed by ICP-MS at t = 0, 1, 2, 4, 8, 24, and 48 h. The mean and SDM are reported ( n .

    Article Snippet: Tris buffer (50 mL) containing 20 mM Tris, 100 mM NaCl, 2 mM CaCl2 , pH 7.5 in the absence and presence of 5 mM BME (Alfa Aesar) was prepared by diluting stock solutions of 1.0 M Tris-HCl (molecular biology grade, Alfa Aesar), 1.0 M NaCl (molecular biology grade, Sigma), and 1.0 M CaCl2 .

    Techniques: Depletion Assay, Incubation, Centrifugation, Mass Spectrometry

    Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM Tris pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to SDS–PAGE. Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.

    Journal: The EMBO Journal

    Article Title: Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors

    doi: 10.1093/emboj/19.20.5450

    Figure Lengend Snippet: Fig. 4. Cross-linking of N- and C-termini by DTSSP. ( A ) Co-transfected microsomes were subjected to trypsin digestion (lanes 2, 3 and 5–9) or mock digested (lanes 1 and 4) and pelleted. Microsomes in lane 3 and lanes 6–9 were then treated with 0.5 mM DTSSP for 30 min and the reaction was terminated by the addition of 20 mM Tris pH 7.5 as described in Materials and methods. All samples were then solubilized by the addition of 1% Zwittergent, immunoprecipitated with CT1 and subjected to SDS–PAGE. Lanes 1–3 were probed with an anti-Myc antibody and the same immunoblot was stripped and re-probed with a FLAG antibody (lanes 4–6). Cross-linked N-terminal peptides co-precipitating with CT1 are designated by a closed (type I) or open (type III) circle. No DTSSP-specific bands in trypsin treated samples were observed when the same immunoblot was probed with antibodies raised against amino acids 401–414 (KEEK, lane 7) and 1883–1902 (ABR, lane 8) of the type I receptor. Similarly, no immunoreactive bands were observed when the immunoblot was probed with an antibody to the type III C-terminus (CT3, lane 9). ( B ) Samples were treated as in (A), except that increasing concentrations (0.5–5.0 mM) of cross-linker were used in lanes 2–6 and lanes 8–12. Increasing the DTSSP concentration was accompanied by a shift in mobility of the 42 kDa N-terminal fragment in a dose-dependent manner (indicated by arrows, see text for details). As in (A), when the blot in (B) was stripped and reprobed with KEEK, ABR or CT3 antibodies, no immunoreactive reactive bands were observed in trypsin-treated samples (data not shown). *IgG band.

    Article Snippet: Pellets were either quenched with SDS–PAGE sample buffer directly or resuspended in 150 mM NaCl, 50 mM Tris–HCl pH 7.8, 1 mM EDTA, 1% Triton X-100, 0.5 mM PMSF and 1× complete protease inhibitor cocktail (Roche Molecular Biochemicals) for immunoprecipitation assays.

    Techniques: Transfection, Immunoprecipitation, SDS Page, Concentration Assay