trifluoroacetic acid Search Results


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  • 98
    Thermo Fisher trifluoroacetic acid
    Synthesis of AP, trimethyl-AP, P-matrix, and C-matrix. Conditions: ( a ) 2.0 equivalents of triphenylphosphine, 2.0 equivalents of diethylazodicarboxylate (DEAD), 2.0 equivalents of 2-propanol, tetrahydrofuran (THF). ( b ) 1.0 equivalent of 4-amino-2-chlorobenzoic acid or 5-chloro-1,3-phenylenediamine, 3.0 equivalents of diisopropylethylamine (DIEA), n -butanol, 90°C, 12 h. ( c ) 5.0 equivalents of ( R )-(−)2-amino-3-methyl-1-butanol, 5.0 equivalents of DIEA, n -butanol, 110°C, 18 h. ( d ) 1.05 equivalents of 1,3-diisopropylcarbodiimide (DIC), 1.05 equivalents of hydroxybenzotriazole, 2.0 equivalents of DIEA, 2.0 equivalents of 1- tert -butyloxycarbonyl-1,8-diamino-3,6-dioxaoctane ( 4 ), 0.05 equivalents of 4-dimethylaminopyridine, dimethylformamide (DMF)/CH 2 Cl 2 /1,4-dioxane, 1:1:1 (vol/vol). ( e ) <t>Trifluoroacetic</t> acid/CH 2 Cl 2 /H 2 O/(CH 3 ) 2 S, 45:45:1:1 (vol/vol), 12 h. ( f ) 17.3 equivalents of NaH, 10.7 equivalents of methyl iodide, DMF, 12 h. ( g ) 33.0 equivalents of ( R )-(−)2-amino-3-methyl-1-butanol, n -butanol, 140°C, 12 h. ( h ) 45.0 mM compound 5 or 6 , 1.5 ml of ReactiGel 6X (Pierce, product 20259), 0.1 M aqueous K 2 CO 3 , 12 h.
    Trifluoroacetic Acid, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 2901 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore trifluoroacetic acid
    Sephadex LH-20 chromatograms of a mixture of oligoferulic acids generated by radical coupling of ethyl ferulate. Chromatographic conditions were (A) 0.5 mM aqueous <t>trifluoroacetic</t> acid/methanol 95/5 (v/v), flow rate: 1.5 mL/min; (B) 0.5 mM aqueous trifluoroacetic acid/methanol 50/50 (v/v), flow rate: 1.0 mL/min; (C) 0.5 mM aqueous trifluoroacetic acid/methanol 40/60 (v/v), flow rate: 1.0 mL/min. Collected fractions contained: 1, unknown; 2, 8-8(cyclic)-dehydrodiferulic acid (DFA) and trimer 1 ; 3, 8-8(noncyclic)-DFA; 4, trimer 2 ; 5, 8-8(cyclic)/5-5-dehydrotriferulic acid (TriFA); 6, monoethyl ester of trimer 3 ; 7, unknown; 8, trimer 3 ; 9, 5-5-DFA and 8-5(noncyclic)/5-5-TriFA; 10, 5-5/8-O-4-TriFA.
    Trifluoroacetic Acid, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4222 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore trifluoroacetic acid d
    Sephadex LH-20 chromatograms of a mixture of oligoferulic acids generated by radical coupling of ethyl ferulate. Chromatographic conditions were (A) 0.5 mM aqueous <t>trifluoroacetic</t> acid/methanol 95/5 (v/v), flow rate: 1.5 mL/min; (B) 0.5 mM aqueous trifluoroacetic acid/methanol 50/50 (v/v), flow rate: 1.0 mL/min; (C) 0.5 mM aqueous trifluoroacetic acid/methanol 40/60 (v/v), flow rate: 1.0 mL/min. Collected fractions contained: 1, unknown; 2, 8-8(cyclic)-dehydrodiferulic acid (DFA) and trimer 1 ; 3, 8-8(noncyclic)-DFA; 4, trimer 2 ; 5, 8-8(cyclic)/5-5-dehydrotriferulic acid (TriFA); 6, monoethyl ester of trimer 3 ; 7, unknown; 8, trimer 3 ; 9, 5-5-DFA and 8-5(noncyclic)/5-5-TriFA; 10, 5-5/8-O-4-TriFA.
    Trifluoroacetic Acid D, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Millipore trifluoroacetic acid solution
    Sephadex LH-20 chromatograms of a mixture of oligoferulic acids generated by radical coupling of ethyl ferulate. Chromatographic conditions were (A) 0.5 mM aqueous <t>trifluoroacetic</t> acid/methanol 95/5 (v/v), flow rate: 1.5 mL/min; (B) 0.5 mM aqueous trifluoroacetic acid/methanol 50/50 (v/v), flow rate: 1.0 mL/min; (C) 0.5 mM aqueous trifluoroacetic acid/methanol 40/60 (v/v), flow rate: 1.0 mL/min. Collected fractions contained: 1, unknown; 2, 8-8(cyclic)-dehydrodiferulic acid (DFA) and trimer 1 ; 3, 8-8(noncyclic)-DFA; 4, trimer 2 ; 5, 8-8(cyclic)/5-5-dehydrotriferulic acid (TriFA); 6, monoethyl ester of trimer 3 ; 7, unknown; 8, trimer 3 ; 9, 5-5-DFA and 8-5(noncyclic)/5-5-TriFA; 10, 5-5/8-O-4-TriFA.
    Trifluoroacetic Acid Solution, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Thermo Fisher n trifluoroacetic acid
    Sephadex LH-20 chromatograms of a mixture of oligoferulic acids generated by radical coupling of ethyl ferulate. Chromatographic conditions were (A) 0.5 mM aqueous <t>trifluoroacetic</t> acid/methanol 95/5 (v/v), flow rate: 1.5 mL/min; (B) 0.5 mM aqueous trifluoroacetic acid/methanol 50/50 (v/v), flow rate: 1.0 mL/min; (C) 0.5 mM aqueous trifluoroacetic acid/methanol 40/60 (v/v), flow rate: 1.0 mL/min. Collected fractions contained: 1, unknown; 2, 8-8(cyclic)-dehydrodiferulic acid (DFA) and trimer 1 ; 3, 8-8(noncyclic)-DFA; 4, trimer 2 ; 5, 8-8(cyclic)/5-5-dehydrotriferulic acid (TriFA); 6, monoethyl ester of trimer 3 ; 7, unknown; 8, trimer 3 ; 9, 5-5-DFA and 8-5(noncyclic)/5-5-TriFA; 10, 5-5/8-O-4-TriFA.
    N Trifluoroacetic Acid, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Avantor trifluoroacetic acid
    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of <t>trifluoroacetic</t> acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
    Trifluoroacetic Acid, supplied by Avantor, used in various techniques. Bioz Stars score: 93/100, based on 177 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Fisher Scientific trifluoroacetic acid
    Flow injection analysis of (a) 50 μM GGFL and (b) a blank at +700 mV following mixing with biuret reagent. Flow injection analysis was performed in a mobile phase composed of 3.0% 1-propanol and 0.10% <t>trifluoroacetic</t> acid with an injection volume of 1.0 μL and with a biuret reagent composition of 0.6 M sodium carbonate, 0.6 M sodium bicarbonate, 30 mM sodium tartrate, and 5.0 mM copper sulfate, pH 9.80.
    Trifluoroacetic Acid, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 93/100, based on 359 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Merck KGaA trifluoroacetic acid
    a Representative RP-HPLC chromatograms obtained from the analysis of a a blank cream matrix sample. b A calibration spiked cream sample containing 19.7 μg mL −1 aluminium and c a cream sample containing 17.0 μg mL −1 aluminium. Chromatographic conditions: RP-HPLC on an XTerraMS C18 analytical column; mobile phase: acetonitrile:water (15:85, v/v) containing 0.08 % <t>trifluoroacetic</t> acid; flow rate 0.30 mL min −1 and a UV detector at 415 nm
    Trifluoroacetic Acid, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 94/100, based on 315 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    FUJIFILM trifluoroacetic acid
    HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and <t>trifluoroacetic</t> acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.
    Trifluoroacetic Acid, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 94/100, based on 130 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Bruker Corporation trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 96/100, based on 461 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Carl Roth GmbH trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Carl Roth GmbH, used in various techniques. Bioz Stars score: 92/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Burdick & Jackson trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Burdick & Jackson, used in various techniques. Bioz Stars score: 92/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck & Co trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Merck & Co, used in various techniques. Bioz Stars score: 92/100, based on 132 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    RATHBURN CHEMICALS LIMITED trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by RATHBURN CHEMICALS LIMITED, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Interchim trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Interchim, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Yonghua Chemical trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Yonghua Chemical, used in various techniques. Bioz Stars score: 93/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Tokyo Chemical Industry trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
    Trifluoroacetic Acid, supplied by Tokyo Chemical Industry, used in various techniques. Bioz Stars score: 92/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Solvay Pharmaceuticals trifluoroacetic acid
    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% <t>trifluoroacetic</t> acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.
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    Thermo Fisher trifluoroacetic acid tfa
    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M <t>trifluoroacetic</t> acid <t>(TFA),</t> then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P
    Trifluoroacetic Acid Tfa, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1177 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Tedia trifluoroacetic acid
    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M <t>trifluoroacetic</t> acid <t>(TFA),</t> then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P
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    Oakwood Chemical trifluoroacetic acid
    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M <t>trifluoroacetic</t> acid <t>(TFA),</t> then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P
    Trifluoroacetic Acid, supplied by Oakwood Chemical, used in various techniques. Bioz Stars score: 92/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Biosolve trifluoroacetic acid
    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M <t>trifluoroacetic</t> acid <t>(TFA),</t> then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P
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    Iris Biotech trifluoroacetic acid
    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M <t>trifluoroacetic</t> acid <t>(TFA),</t> then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P
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    Supelco trifluoroacetic acid
    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M <t>trifluoroacetic</t> acid <t>(TFA),</t> then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P
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    Image Search Results


    Synthesis of AP, trimethyl-AP, P-matrix, and C-matrix. Conditions: ( a ) 2.0 equivalents of triphenylphosphine, 2.0 equivalents of diethylazodicarboxylate (DEAD), 2.0 equivalents of 2-propanol, tetrahydrofuran (THF). ( b ) 1.0 equivalent of 4-amino-2-chlorobenzoic acid or 5-chloro-1,3-phenylenediamine, 3.0 equivalents of diisopropylethylamine (DIEA), n -butanol, 90°C, 12 h. ( c ) 5.0 equivalents of ( R )-(−)2-amino-3-methyl-1-butanol, 5.0 equivalents of DIEA, n -butanol, 110°C, 18 h. ( d ) 1.05 equivalents of 1,3-diisopropylcarbodiimide (DIC), 1.05 equivalents of hydroxybenzotriazole, 2.0 equivalents of DIEA, 2.0 equivalents of 1- tert -butyloxycarbonyl-1,8-diamino-3,6-dioxaoctane ( 4 ), 0.05 equivalents of 4-dimethylaminopyridine, dimethylformamide (DMF)/CH 2 Cl 2 /1,4-dioxane, 1:1:1 (vol/vol). ( e ) Trifluoroacetic acid/CH 2 Cl 2 /H 2 O/(CH 3 ) 2 S, 45:45:1:1 (vol/vol), 12 h. ( f ) 17.3 equivalents of NaH, 10.7 equivalents of methyl iodide, DMF, 12 h. ( g ) 33.0 equivalents of ( R )-(−)2-amino-3-methyl-1-butanol, n -butanol, 140°C, 12 h. ( h ) 45.0 mM compound 5 or 6 , 1.5 ml of ReactiGel 6X (Pierce, product 20259), 0.1 M aqueous K 2 CO 3 , 12 h.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: A cyclin-dependent kinase inhibitor inducing cancer cell differentiation: Biochemical identification using Xenopus egg extracts

    doi:

    Figure Lengend Snippet: Synthesis of AP, trimethyl-AP, P-matrix, and C-matrix. Conditions: ( a ) 2.0 equivalents of triphenylphosphine, 2.0 equivalents of diethylazodicarboxylate (DEAD), 2.0 equivalents of 2-propanol, tetrahydrofuran (THF). ( b ) 1.0 equivalent of 4-amino-2-chlorobenzoic acid or 5-chloro-1,3-phenylenediamine, 3.0 equivalents of diisopropylethylamine (DIEA), n -butanol, 90°C, 12 h. ( c ) 5.0 equivalents of ( R )-(−)2-amino-3-methyl-1-butanol, 5.0 equivalents of DIEA, n -butanol, 110°C, 18 h. ( d ) 1.05 equivalents of 1,3-diisopropylcarbodiimide (DIC), 1.05 equivalents of hydroxybenzotriazole, 2.0 equivalents of DIEA, 2.0 equivalents of 1- tert -butyloxycarbonyl-1,8-diamino-3,6-dioxaoctane ( 4 ), 0.05 equivalents of 4-dimethylaminopyridine, dimethylformamide (DMF)/CH 2 Cl 2 /1,4-dioxane, 1:1:1 (vol/vol). ( e ) Trifluoroacetic acid/CH 2 Cl 2 /H 2 O/(CH 3 ) 2 S, 45:45:1:1 (vol/vol), 12 h. ( f ) 17.3 equivalents of NaH, 10.7 equivalents of methyl iodide, DMF, 12 h. ( g ) 33.0 equivalents of ( R )-(−)2-amino-3-methyl-1-butanol, n -butanol, 140°C, 12 h. ( h ) 45.0 mM compound 5 or 6 , 1.5 ml of ReactiGel 6X (Pierce, product 20259), 0.1 M aqueous K 2 CO 3 , 12 h.

    Article Snippet: The Boc group was removed with trifluoroacetic acid and the resulting primary amino group was coupled to carbonylimidazole-activated agarose (Reacti-GelR Pierce, product 20259).

    Techniques:

    Sephadex LH-20 chromatograms of a mixture of oligoferulic acids generated by radical coupling of ethyl ferulate. Chromatographic conditions were (A) 0.5 mM aqueous trifluoroacetic acid/methanol 95/5 (v/v), flow rate: 1.5 mL/min; (B) 0.5 mM aqueous trifluoroacetic acid/methanol 50/50 (v/v), flow rate: 1.0 mL/min; (C) 0.5 mM aqueous trifluoroacetic acid/methanol 40/60 (v/v), flow rate: 1.0 mL/min. Collected fractions contained: 1, unknown; 2, 8-8(cyclic)-dehydrodiferulic acid (DFA) and trimer 1 ; 3, 8-8(noncyclic)-DFA; 4, trimer 2 ; 5, 8-8(cyclic)/5-5-dehydrotriferulic acid (TriFA); 6, monoethyl ester of trimer 3 ; 7, unknown; 8, trimer 3 ; 9, 5-5-DFA and 8-5(noncyclic)/5-5-TriFA; 10, 5-5/8-O-4-TriFA.

    Journal: Frontiers in Chemistry

    Article Title: A Multi-Step Chromatographic Approach to Purify Radically Generated Ferulate Oligomers Reveals Naturally Occurring 5-5/8-8(Cyclic)-, 8-8(Noncyclic)/8-O-4-, and 5-5/8-8(Noncyclic)-Coupled Dehydrotriferulic Acids

    doi: 10.3389/fchem.2018.00190

    Figure Lengend Snippet: Sephadex LH-20 chromatograms of a mixture of oligoferulic acids generated by radical coupling of ethyl ferulate. Chromatographic conditions were (A) 0.5 mM aqueous trifluoroacetic acid/methanol 95/5 (v/v), flow rate: 1.5 mL/min; (B) 0.5 mM aqueous trifluoroacetic acid/methanol 50/50 (v/v), flow rate: 1.0 mL/min; (C) 0.5 mM aqueous trifluoroacetic acid/methanol 40/60 (v/v), flow rate: 1.0 mL/min. Collected fractions contained: 1, unknown; 2, 8-8(cyclic)-dehydrodiferulic acid (DFA) and trimer 1 ; 3, 8-8(noncyclic)-DFA; 4, trimer 2 ; 5, 8-8(cyclic)/5-5-dehydrotriferulic acid (TriFA); 6, monoethyl ester of trimer 3 ; 7, unknown; 8, trimer 3 ; 9, 5-5-DFA and 8-5(noncyclic)/5-5-TriFA; 10, 5-5/8-O-4-TriFA.

    Article Snippet: Research chemicals were obtained from the following suppliers: Cu(I)Cl, copper(II)-tetramethylethylenediamine (TMEDA), HCl (37%), NaOH, ammonium chloride, ethyl acetate, and ethanol from Carl Roth GmbH (Karlsruhe, Germany); acetonitrile, diethyl ether, methanol, acetone, petroleum ether, tetrahydrofuran, and Na2 SO4 from VWR International (Radnor, PA, USA); acetone- d 6 , ferulic acid, [1-13 C]triethyl phosphonoacetate, and trifluoroacetic acid from Sigma-Aldrich (St. Louis, MO, USA); D2 O from deutero GmbH (Kastellaun, Germany); acetyl chloride and vanillin from Fluka (Buchs, Switzerland); formic acid from Merck KGaA (Darmstadt, Germany); NaHCO3 from Riedel-de Haën AG (Seelze, Germany); carbogen (5% CO2 ) from Air Liquide S.A. (Düsseldorf, Germany), and NaH (60% dispersion in oil) from Alfa Aesar (Karlsruhe, Germany).

    Techniques: Generated, Flow Cytometry, Direct Fluorescent Antibody Test

    Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.

    Journal: Toxins

    Article Title: Revealing the Function and the Structural Model of Ts4: Insights into the “Non-Toxic” Toxin from Tityus serrulatus Venom

    doi: 10.3390/toxins7072534

    Figure Lengend Snippet: Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.

    Article Snippet: RP-FPLC of the fraction VIIIB was performed in an Äkta Purifier UPC-10 system (GE Healthcare, Uppsala, Sweden), using a 4.6 mm × 250.0 mm C18 column (Shimadzu Corp., Kyoto, Kansai, Japan) equilibrated with 0.1% (v /v ) trifluoroacetic acid (TFA, Avantor Performance Materials Inc., Center Valley, PA, USA) at a flow rate of 0.8 mL/min.

    Techniques: Fast Protein Liquid Chromatography, Fractionation, Reversed-phase Chromatography, Concentration Assay, Flow Cytometry

    Flow injection analysis of (a) 50 μM GGFL and (b) a blank at +700 mV following mixing with biuret reagent. Flow injection analysis was performed in a mobile phase composed of 3.0% 1-propanol and 0.10% trifluoroacetic acid with an injection volume of 1.0 μL and with a biuret reagent composition of 0.6 M sodium carbonate, 0.6 M sodium bicarbonate, 30 mM sodium tartrate, and 5.0 mM copper sulfate, pH 9.80.

    Journal: Analytical chemistry

    Article Title: Fabrication of Microchannel Structures in Fluorinated Ethylene Propylene

    doi: 10.1021/ac025622c

    Figure Lengend Snippet: Flow injection analysis of (a) 50 μM GGFL and (b) a blank at +700 mV following mixing with biuret reagent. Flow injection analysis was performed in a mobile phase composed of 3.0% 1-propanol and 0.10% trifluoroacetic acid with an injection volume of 1.0 μL and with a biuret reagent composition of 0.6 M sodium carbonate, 0.6 M sodium bicarbonate, 30 mM sodium tartrate, and 5.0 mM copper sulfate, pH 9.80.

    Article Snippet: Trifluoroacetic acid was obtained from Fisher Scientific (Pittsburgh, PA).

    Techniques: Flow Cytometry, Injection

    a Representative RP-HPLC chromatograms obtained from the analysis of a a blank cream matrix sample. b A calibration spiked cream sample containing 19.7 μg mL −1 aluminium and c a cream sample containing 17.0 μg mL −1 aluminium. Chromatographic conditions: RP-HPLC on an XTerraMS C18 analytical column; mobile phase: acetonitrile:water (15:85, v/v) containing 0.08 % trifluoroacetic acid; flow rate 0.30 mL min −1 and a UV detector at 415 nm

    Journal: Chromatographia

    Article Title: Pre-Column Derivatization HPLC Procedure for the Quantitation of Aluminium Chlorohydrate in Antiperspirant Creams Using Quercetin as Chromogenic Reagent

    doi: 10.1007/s10337-014-2722-9

    Figure Lengend Snippet: a Representative RP-HPLC chromatograms obtained from the analysis of a a blank cream matrix sample. b A calibration spiked cream sample containing 19.7 μg mL −1 aluminium and c a cream sample containing 17.0 μg mL −1 aluminium. Chromatographic conditions: RP-HPLC on an XTerraMS C18 analytical column; mobile phase: acetonitrile:water (15:85, v/v) containing 0.08 % trifluoroacetic acid; flow rate 0.30 mL min −1 and a UV detector at 415 nm

    Article Snippet: Trifluoroacetic acid and ammonium acetate of analytical reagent grade were obtained from Merck (Darmstadt, Germany).

    Techniques: High Performance Liquid Chromatography, Flow Cytometry

    HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and trifluoroacetic acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.

    Journal: Frontiers in Pharmacology

    Article Title: The Relation between Hepatotoxicity and the Total Coumarin Intake from Traditional Japanese Medicines Containing Cinnamon Bark

    doi: 10.3389/fphar.2016.00174

    Figure Lengend Snippet: HPLC chromatograms of (A) coumarin (10 mg/mL, standard) and (B) TJ-125. Chromatographic peaks were detected at a wavelength of 273 nm. The mobile phase consisted of water, acetonitrile and trifluoroacetic acid (750:250:0.5, v/v/v). The flow rate of the mobile phase was 0.5 ml/min. The injection volume was 10 μL. The column temperature was set at 40°C. The retention time of coumarin was 13.7 min.

    Article Snippet: Materials Coumarin, acetonitrile (HPLC grade), methanol (HPLC grade), and trifluoroacetic acid were purchased from Wako Pure Chemical Industries (Osaka, Japan).

    Techniques: High Performance Liquid Chromatography, Flow Cytometry, Injection

    TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% trifluoroacetic acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.

    Journal: Biochemical Journal

    Article Title: Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

    doi: 10.1042/BJ20140334

    Figure Lengend Snippet: TcPINK1 phosphorylates ubiquitin at Ser 65 ( A ) Mapping of phosphopeptide on ubiquitin after phosphorylation by TcPINK1 in vitro . Ubiquitin (10 μg) was incubated with 10 μg of either wild-type TcPINK1 or kinase-inactive TcPINK1 (D359A) in the presence of Mg 2+ -[γ- 32 P]ATP for 80 min. Assays were terminated by the addition of SDS loading buffer and products were separated by SDS/PAGE. Proteins were detected by Colloidal Coomassie Blue staining and phosphorylated ubiquitin was digested with trypsin. Peptides were chromatographed on a reverse-phase HPLC Vydac C 18 column equilibrated in 0.1% trifluoroacetic acid and the column developed with a linear acetonitrile gradient at a flow rate of 0.2 ml/min and fractions (0.1 ml each) were collected and analysed for 32 P radioactivity by Cerenkov counting. One major 32 P-labelled peak was identified following incubation with wild-type TcPINK1, whereas no peaks were identified following incubation with kinase-inactive TcPINK1 (results not shown). ( B ) The phosphopeptide identified in ( A ) was analysed by solid-phase Edman sequencing and MS. The amino acid sequence deduced from the single phosphopeptide seen in the LC–MS/MS analysis is shown using the single-letter amino acid code. ( C ) The S65A mutation abolishes ubiquitin phosphorylation by TcPINK1. Wild-type or S65A mutant ubiquitin (1 μg) was incubated in the presence of wild-type or kinase-inactive TcPINK1 (1 μg) and Mg 2+ -[γ- 32 P]ATP for the times indicated and assays were terminated by the addition of SDS loading buffer. Samples were subjected to SDS/PAGE and proteins detected by Colloidal Coomassie Blue staining (bottom panels) and incorporation of [γ- 32 P]ATP was detected by autoradiography (top panels). Cerenkov counting was used to calculate the stoichiometry of ubiquitin phosphorylation indicated above autoradiographs as mol of [γ- 32 P]ATP incorporated/mol of ubiquitin. KI, kinase-inactive; WT, wild-type.

    Article Snippet: An aliquot of the reaction (2 μl, 400–600 fmol) was added to 2 μl of the matrix [2,5-dihydroxyacetophenone, 15 mg/ml in 80% ethanol and 20% 12 mg/ml ammonium citrate dibasic] and 2 μl of 2% (v/v) trifluoroacetic acid was added before spotting 0.5 μl of the sample on to an AnchorChip target (Bruker Daltonics).

    Techniques: In Vitro, Incubation, SDS Page, Staining, High Performance Liquid Chromatography, Flow Cytometry, Radioactivity, Sequencing, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Mutagenesis, Autoradiography

    Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M trifluoroacetic acid (TFA), then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P

    Journal: Biotechnology for Biofuels

    Article Title: Increased drought tolerance in plants engineered for low lignin and low xylan content

    doi: 10.1186/s13068-018-1196-7

    Figure Lengend Snippet: Monosaccharide composition of the cell wall from the Col-0 and engineered plants with low xylan under drought stress treatment. Cell wall material (AIR) was prepared from fresh main stem, hydrolyzed with 2 M trifluoroacetic acid (TFA), then analyzed by high-performance anion-exchange chromatography. Values show average ± SD ( n shown in the picture). Asterisks indicate significant differences between well-watered and drought stress conditions ( t test, * P

    Article Snippet: Dried AIR (2 mg) was hydrolyzed in 2 M trifluoroacetic acid (TFA) at 121 °C for 1 h and analyzed by high-performance anion-exchange chromatography (HPAEC) on an ICS-5000 instrument (Thermo Fisher Scientific) equipped with a CarboPac PA20 (3 mm × 150 mm, Thermo Fisher Scientific) analytical anion-exchange column, PA20 guard column (3 mm × 30 mm), borate trap, and a 500-pulsed amperometric detector (PAD), as described previously [ ].

    Techniques: Chromatography