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Fisher Scientific tris hcl
Activities of recombinant E. coli native and mutant (K192A) YjeF proteins ( A ) Assays (100 µl) contained 25 mM <t>Tris-HCl,</t> pH 8.0, 5 mM KCl, 2 mM MgCl 2 , 0.1 mg mL −1 BSA, 40 µM <t>NADHX</t> (containing approximately equal amounts of S and R forms), and 1 mM ADP. Reactions were started by adding 2 µg of native YjeF and absorbance was monitored at 340 nm at 22°C. ( B ) Assays were performed as above except that reactions were started by adding 2 µg of K192A YjeF (closed circles). In separate assays, 2 µg of Arabidopsis NAD(P)HX epimerase domain protein (E) was added at 4 min (open diamonds). Spontaneous epimerization of NAD(P)HX was undetectable in the conditions and time frame of the assay. Data are means of three replicates; S.E. was
Tris Hcl, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Evidence that the metabolite repair enzyme NAD(P)HX epimerase has a moonlighting function"

Article Title: Evidence that the metabolite repair enzyme NAD(P)HX epimerase has a moonlighting function

Journal: Bioscience Reports

doi: 10.1042/BSR20180223

Activities of recombinant E. coli native and mutant (K192A) YjeF proteins ( A ) Assays (100 µl) contained 25 mM Tris-HCl, pH 8.0, 5 mM KCl, 2 mM MgCl 2 , 0.1 mg mL −1 BSA, 40 µM NADHX (containing approximately equal amounts of S and R forms), and 1 mM ADP. Reactions were started by adding 2 µg of native YjeF and absorbance was monitored at 340 nm at 22°C. ( B ) Assays were performed as above except that reactions were started by adding 2 µg of K192A YjeF (closed circles). In separate assays, 2 µg of Arabidopsis NAD(P)HX epimerase domain protein (E) was added at 4 min (open diamonds). Spontaneous epimerization of NAD(P)HX was undetectable in the conditions and time frame of the assay. Data are means of three replicates; S.E. was
Figure Legend Snippet: Activities of recombinant E. coli native and mutant (K192A) YjeF proteins ( A ) Assays (100 µl) contained 25 mM Tris-HCl, pH 8.0, 5 mM KCl, 2 mM MgCl 2 , 0.1 mg mL −1 BSA, 40 µM NADHX (containing approximately equal amounts of S and R forms), and 1 mM ADP. Reactions were started by adding 2 µg of native YjeF and absorbance was monitored at 340 nm at 22°C. ( B ) Assays were performed as above except that reactions were started by adding 2 µg of K192A YjeF (closed circles). In separate assays, 2 µg of Arabidopsis NAD(P)HX epimerase domain protein (E) was added at 4 min (open diamonds). Spontaneous epimerization of NAD(P)HX was undetectable in the conditions and time frame of the assay. Data are means of three replicates; S.E. was

Techniques Used: Recombinant, Mutagenesis

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Centrifugation:

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Article Snippet: The cells were then pelleted, washed twice in PBS, and resuspened in hypotonic lysis buffer containing 0.5% Triton X100 [10 mM Hepes (pH 7.5), 10 mM KCl, 3 mM MgCl2, 1 mM EDTA, 10 mM NaF, 1 mM DTT, 0.1 mM Na3VO4, and 10 mM β-glycerophosphate]. .. After 20 min on ice, the insoluble material was harvested by centrifugation and resuspended in low-salt binding and wash buffer [50 mM Tris·HCl (pH 8.0), 150 mM NaCl, 1 mM EDTA, 1% Nonidet P-40, and 0.25% deoxycholic acid] and sonicated on ice to disrupt the nuclear membrane with the aid of a Fisher Scientific Ultrasonic Dismembrator. .. Each sonication step was carried out for 10 s, and samples were kept on ice for at least 1 min between sonications.

Binding Assay:

Article Title: Use of biotinylated plasmid DNA as a surrogate for HSV DNA to identify proteins that repress or activate viral gene expression
Article Snippet: The cells were then pelleted, washed twice in PBS, and resuspened in hypotonic lysis buffer containing 0.5% Triton X100 [10 mM Hepes (pH 7.5), 10 mM KCl, 3 mM MgCl2, 1 mM EDTA, 10 mM NaF, 1 mM DTT, 0.1 mM Na3VO4, and 10 mM β-glycerophosphate]. .. After 20 min on ice, the insoluble material was harvested by centrifugation and resuspended in low-salt binding and wash buffer [50 mM Tris·HCl (pH 8.0), 150 mM NaCl, 1 mM EDTA, 1% Nonidet P-40, and 0.25% deoxycholic acid] and sonicated on ice to disrupt the nuclear membrane with the aid of a Fisher Scientific Ultrasonic Dismembrator. .. Each sonication step was carried out for 10 s, and samples were kept on ice for at least 1 min between sonications.

Sonication:

Article Title: Use of biotinylated plasmid DNA as a surrogate for HSV DNA to identify proteins that repress or activate viral gene expression
Article Snippet: The cells were then pelleted, washed twice in PBS, and resuspened in hypotonic lysis buffer containing 0.5% Triton X100 [10 mM Hepes (pH 7.5), 10 mM KCl, 3 mM MgCl2, 1 mM EDTA, 10 mM NaF, 1 mM DTT, 0.1 mM Na3VO4, and 10 mM β-glycerophosphate]. .. After 20 min on ice, the insoluble material was harvested by centrifugation and resuspended in low-salt binding and wash buffer [50 mM Tris·HCl (pH 8.0), 150 mM NaCl, 1 mM EDTA, 1% Nonidet P-40, and 0.25% deoxycholic acid] and sonicated on ice to disrupt the nuclear membrane with the aid of a Fisher Scientific Ultrasonic Dismembrator. .. Each sonication step was carried out for 10 s, and samples were kept on ice for at least 1 min between sonications.

Article Title: Gleevec inhibits ?-amyloid production but not Notch cleavage
Article Snippet: .. Pellets were further solubilized in 3% SDS in water containing 8 μl of 2-mercaptoethanol (Sigma) per ml and subjected to vortexing and heating at 95°C for 10 min. Solubilized cell pellets were sonicated and centrifuged at 100,000 × g for 15 min. Supernatants were diluted 10-fold in buffer consisting of 190 mM NaCl, 20 mM Tris·HCl (pH 8.8), 2 mM EDTA, and 2% Triton X-100 (Fisher Scientific). .. Samples were normalized to total protein and assayed for Aβ40/42 by sandwich ELISA according to the manufacturer's instructions (BioSource International, Camarillo, California).

Article Title: Targeted analysis and discovery of posttranslational modifications in proteins from methanogenic archaea by top-down MS
Article Snippet: .. Two to three grams of wet cells were resuspended in 6 ml of 100 mM Tris·HCl (Fisher Scientific), pH 8.0, and lysed by using pulsed microtip sonication on ice. .. Fifty units of DNase (Sigma) and various protease inhibitors were added, and the mixture was incubated for 30 min at 37°C.

Concentration Assay:

Article Title: Targeted analysis and discovery of posttranslational modifications in proteins from methanogenic archaea by top-down MS
Article Snippet: .. The resulting pellet was washed three times with 100 mM Tris·HCl, pH 8.0 buffer with increasing KCl concentration: 0, 0.5, and 1.0 M KCl. ..

Incubation:

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Article Snippet: Protein concentration was determined as described above. .. Total protein (50 μg) was incubated for 10 min at 37°C in a reaction mixture containing 50 mM Tris·HCl (pH 7.5; Fisher Scientific, Pittsburgh, PA), 4 mM MgCl2 (Fisher Scientific), 0.5 mM 3-isobutyl-1-methylxanthine (Biomol), 7.5 mM creatine phosphate (Sigma), 0.2 mg/ml creatine phosphokinase (Sigma), 1 mM sodium nitroprusside (Sigma), and 1 mM GTP (Sigma). .. The reaction was terminated by the addition of HCl (Sigma) to a final concentration of 0.1 N. Each sample was dried in a Speed-Vac and resuspended in 100 μl of cGMP enzyme immunoassay (EIA) buffer (Cayman Chemical, Ann Arbor, MI). cGMP in the reaction mixture was measured by EIA in duplicate using a commercially available kit (Cayman Chemical).

Homogenization:

Article Title: Formation of Vascular S-Nitrosothiols and Plasma Nitrates/Nitrites Following Inhalation of Diesel Emissions
Article Snippet: Aortic cytosolic protein was isolated from frozen tissues. .. Aorta segments were homogenized in cold Tris·HCl homogenization buffer containing a complete protease inhibitor cocktail (Pierce) using a motorized homogenizer (Fisher Scientific). .. The supernatant was analyzed for protein concentration using the Bradford method (Pierce).

Protease Inhibitor:

Article Title: Formation of Vascular S-Nitrosothiols and Plasma Nitrates/Nitrites Following Inhalation of Diesel Emissions
Article Snippet: Aortic cytosolic protein was isolated from frozen tissues. .. Aorta segments were homogenized in cold Tris·HCl homogenization buffer containing a complete protease inhibitor cocktail (Pierce) using a motorized homogenizer (Fisher Scientific). .. The supernatant was analyzed for protein concentration using the Bradford method (Pierce).

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    Fisher Scientific tris hcl
    Activities of recombinant E. coli native and mutant (K192A) YjeF proteins ( A ) Assays (100 µl) contained 25 mM <t>Tris-HCl,</t> pH 8.0, 5 mM KCl, 2 mM MgCl 2 , 0.1 mg mL −1 BSA, 40 µM <t>NADHX</t> (containing approximately equal amounts of S and R forms), and 1 mM ADP. Reactions were started by adding 2 µg of native YjeF and absorbance was monitored at 340 nm at 22°C. ( B ) Assays were performed as above except that reactions were started by adding 2 µg of K192A YjeF (closed circles). In separate assays, 2 µg of Arabidopsis NAD(P)HX epimerase domain protein (E) was added at 4 min (open diamonds). Spontaneous epimerization of NAD(P)HX was undetectable in the conditions and time frame of the assay. Data are means of three replicates; S.E. was
    Tris Hcl, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tris hcl/product/Fisher Scientific
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tris hcl - by Bioz Stars, 2021-03
    86/100 stars
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    Activities of recombinant E. coli native and mutant (K192A) YjeF proteins ( A ) Assays (100 µl) contained 25 mM Tris-HCl, pH 8.0, 5 mM KCl, 2 mM MgCl 2 , 0.1 mg mL −1 BSA, 40 µM NADHX (containing approximately equal amounts of S and R forms), and 1 mM ADP. Reactions were started by adding 2 µg of native YjeF and absorbance was monitored at 340 nm at 22°C. ( B ) Assays were performed as above except that reactions were started by adding 2 µg of K192A YjeF (closed circles). In separate assays, 2 µg of Arabidopsis NAD(P)HX epimerase domain protein (E) was added at 4 min (open diamonds). Spontaneous epimerization of NAD(P)HX was undetectable in the conditions and time frame of the assay. Data are means of three replicates; S.E. was

    Journal: Bioscience Reports

    Article Title: Evidence that the metabolite repair enzyme NAD(P)HX epimerase has a moonlighting function

    doi: 10.1042/BSR20180223

    Figure Lengend Snippet: Activities of recombinant E. coli native and mutant (K192A) YjeF proteins ( A ) Assays (100 µl) contained 25 mM Tris-HCl, pH 8.0, 5 mM KCl, 2 mM MgCl 2 , 0.1 mg mL −1 BSA, 40 µM NADHX (containing approximately equal amounts of S and R forms), and 1 mM ADP. Reactions were started by adding 2 µg of native YjeF and absorbance was monitored at 340 nm at 22°C. ( B ) Assays were performed as above except that reactions were started by adding 2 µg of K192A YjeF (closed circles). In separate assays, 2 µg of Arabidopsis NAD(P)HX epimerase domain protein (E) was added at 4 min (open diamonds). Spontaneous epimerization of NAD(P)HX was undetectable in the conditions and time frame of the assay. Data are means of three replicates; S.E. was

    Article Snippet: For assay of NADHX activity, cell pellets were resuspended in 1 ml of 25 mM Tris-HCl, pH 8.0, 300 mM KCl, 1 mM 2-mercaptoethanol on ice and sonicated (Fisher Scientific Ultrasonic Dismembrator, model 150E; 5 × 3 s pulses at 70% power, cooling on ice for 30–60 s between pulses).

    Techniques: Recombinant, Mutagenesis