tris hcl  (Carl Roth GmbH)

 
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    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: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tris hcl/product/Carl Roth GmbH
    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

    Images

    1) Product Images from "Combining Electrochemical Impedance Spectroscopy and Surface Plasmon Resonance into one Simultaneous Read-Out System for the Detection of Surface Interactions"

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

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s131114650

    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 ).
    Figure Legend 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 ).

    Techniques Used:

    2) Product Images from "rsEGFP2 enables fast RESOLFT nanoscopy of living cells"

    Article Title: rsEGFP2 enables fast RESOLFT nanoscopy of living cells

    Journal: eLife

    doi: 10.7554/eLife.00248

    Semi-native polyacrylamide gel electrophoresis of rsEGFP2. Purified monomeric EGFP, dimeric dTomato, tetrameric DsRed, and rsEGFP2 were separated on a semi-native gel (a two-phase polyacrylamide gel) consisting out of a 12.5% separation gel (6.3 ml H 2 O, 5 ml 1.5 M Tris–HCl pH 8.8, 8.3 ml Rotiphorese Gel 30 solution [Roth, Karlsruhe, Germany], 200 μl 10% [wt/vol] sodiumdodecyl sulphate [SDS], 200 μl 10% [wt/vol] ammonium persulfate (APS), 20 μl Tetramethylethylendiamin [TEMED]) and a 5% loading gel (5.6 ml H 2 O, 2.5ml 1.5 M Tris–HCl pH 6.8, 1.7 ml Rotiphorese Gel 30 solution, 100 μl 10% [wt/vol] SDS, 100 μl 10% [wt/vol] APS, 10 μl TEMED). Images were taken with a custom-built gel documentation system. To detect green fluorescence (EGFP and rsEGFP2) the gel was irradiated with light of 470 ± 5 nm and fluorescence was detected at 525 ± 30 nm. To detect red fluorescence (dTomato and DsRed) the gel was irradiated with light of 545 ± 10 nm and fluorescence was recorded at 617 ± 37. Both images were overlaid and are represented in false colors. DOI: http://dx.doi.org/10.7554/eLife.00248.009
    Figure Legend Snippet: Semi-native polyacrylamide gel electrophoresis of rsEGFP2. Purified monomeric EGFP, dimeric dTomato, tetrameric DsRed, and rsEGFP2 were separated on a semi-native gel (a two-phase polyacrylamide gel) consisting out of a 12.5% separation gel (6.3 ml H 2 O, 5 ml 1.5 M Tris–HCl pH 8.8, 8.3 ml Rotiphorese Gel 30 solution [Roth, Karlsruhe, Germany], 200 μl 10% [wt/vol] sodiumdodecyl sulphate [SDS], 200 μl 10% [wt/vol] ammonium persulfate (APS), 20 μl Tetramethylethylendiamin [TEMED]) and a 5% loading gel (5.6 ml H 2 O, 2.5ml 1.5 M Tris–HCl pH 6.8, 1.7 ml Rotiphorese Gel 30 solution, 100 μl 10% [wt/vol] SDS, 100 μl 10% [wt/vol] APS, 10 μl TEMED). Images were taken with a custom-built gel documentation system. To detect green fluorescence (EGFP and rsEGFP2) the gel was irradiated with light of 470 ± 5 nm and fluorescence was detected at 525 ± 30 nm. To detect red fluorescence (dTomato and DsRed) the gel was irradiated with light of 545 ± 10 nm and fluorescence was recorded at 617 ± 37. Both images were overlaid and are represented in false colors. DOI: http://dx.doi.org/10.7554/eLife.00248.009

    Techniques Used: Polyacrylamide Gel Electrophoresis, Purification, Fluorescence, Irradiation

    3) Product Images from "Combining Electrochemical Impedance Spectroscopy and Surface Plasmon Resonance into one Simultaneous Read-Out System for the Detection of Surface Interactions"

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

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s131114650

    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 ).
    Figure Legend 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 ).

    Techniques Used:

    4) Product Images from "Combining Electrochemical Impedance Spectroscopy and Surface Plasmon Resonance into one Simultaneous Read-Out System for the Detection of Surface Interactions"

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

    Journal: Sensors (Basel, Switzerland)

    doi: 10.3390/s131114650

    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 ).
    Figure Legend 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 ).

    Techniques Used:

    5) Product Images from "A comprehensive transcriptome and immune-gene repertoire of the lepidopteran model host Galleria mellonella"

    Article Title: A comprehensive transcriptome and immune-gene repertoire of the lepidopteran model host Galleria mellonella

    Journal: BMC Genomics

    doi: 10.1186/1471-2164-12-308

    Two-dimensional SDS-Page map of immunized Galleria larvae . Hemolymph protein from untreated and LPS-immunized larvae was loaded on 24-cm pH 3 to 11 NL isoelectric focusing strips, followed by Tris-Tricine-SDS-polyacrylamide gel electrophoresis on a 15% gel. Image analysis enabled visualization of new or enhanced spots present in hemolymph samples from immunized larvae depicted in orange color. Putative identifications of immune-inducible proteins by MALDI-TOF analysis and according to our recent study [ 21 ] are depicted next to the respective spots. Molecular mass standards are indicated in kDa (left), and the pI range by an arrow. PGRP, peptidoglycan recognition protein; GNBP, Gram negative bacteria binding protein; GST, Glutathione-S-transferase; Apo III, apolipophorin III; DLS..., unknown protein.
    Figure Legend Snippet: Two-dimensional SDS-Page map of immunized Galleria larvae . Hemolymph protein from untreated and LPS-immunized larvae was loaded on 24-cm pH 3 to 11 NL isoelectric focusing strips, followed by Tris-Tricine-SDS-polyacrylamide gel electrophoresis on a 15% gel. Image analysis enabled visualization of new or enhanced spots present in hemolymph samples from immunized larvae depicted in orange color. Putative identifications of immune-inducible proteins by MALDI-TOF analysis and according to our recent study [ 21 ] are depicted next to the respective spots. Molecular mass standards are indicated in kDa (left), and the pI range by an arrow. PGRP, peptidoglycan recognition protein; GNBP, Gram negative bacteria binding protein; GST, Glutathione-S-transferase; Apo III, apolipophorin III; DLS..., unknown protein.

    Techniques Used: SDS Page, Polyacrylamide Gel Electrophoresis, Binding Assay

    6) Product Images from "Thermodynamics of nanodisc formation mediated by styrene/maleic acid (2:1) copolymer"

    Article Title: Thermodynamics of nanodisc formation mediated by styrene/maleic acid (2:1) copolymer

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-11616-z

    SDS-PAGE showing the solubilisation of E. coli BL21(DE3) membranes by 10 mM (0.5% ( w / v )) DDM, 9.3 mM (2.5% ( w / v )) SMA(2:1), 6.3 mM (2.5% ( w / v )) SMA(3:1), or 3.0 mM (2.5% ( w / v )) DIBMA. Buffer conditions were 50 mM Tris, 200 mM NaCl, 20 °C. Shown are the solubilised membrane-protein fractions after removal of cell debris, intrinsically soluble proteins, and unsolubilised material by serial centrifugation. Data for DDM, SMA(3:1), and DIBMA are reproduced from Oluwole et al. 18 For clarity and conciseness, the gel was cropped as indicated. The full-length gel is presented in Supplementary Figure 2 .
    Figure Legend Snippet: SDS-PAGE showing the solubilisation of E. coli BL21(DE3) membranes by 10 mM (0.5% ( w / v )) DDM, 9.3 mM (2.5% ( w / v )) SMA(2:1), 6.3 mM (2.5% ( w / v )) SMA(3:1), or 3.0 mM (2.5% ( w / v )) DIBMA. Buffer conditions were 50 mM Tris, 200 mM NaCl, 20 °C. Shown are the solubilised membrane-protein fractions after removal of cell debris, intrinsically soluble proteins, and unsolubilised material by serial centrifugation. Data for DDM, SMA(3:1), and DIBMA are reproduced from Oluwole et al. 18 For clarity and conciseness, the gel was cropped as indicated. The full-length gel is presented in Supplementary Figure 2 .

    Techniques Used: SDS Page, Centrifugation

    Related Articles

    Microscopy:

    Article Title: The CsrA-FliW network controls polar localization of the dual-function flagellin mRNA in Campylobacter jejuni
    Article Snippet: Labelled cells were immobilized on poly-D -lysine (Sigma-Aldrich)-coated eight-well chambered cover glasses (Sarstedt). .. For fluorophore photo switching, a buffer with a pH of 8.3–8.5 was used containing 50 mM Tris-HCl (pH 8), 10% glucose, 1% 2-mercaptoethanol (Carl Roth), 3 U ml−1 pyranose oxidase (Sigma-Aldrich) and 90 U ml−1 catalase (Sigma-Aldrich) in 2 × SSC. d STORM was performed on a wide-field setup for localization microscopy . .. An optically pumped semiconductor laser (Genesis MX STM-Series, Coherent) with a wavelength of 639 nm (maximum power of 1 W) was used for excitation of Cy5 and a diode laser (iBeam smart Family, TOPTICA Photonics) with a wavelength of 405 nm (maximum power of 120 mW) was used for reactivation of Cy5.

    Western Blot:

    Article Title: Pro-hepcidin: expression and cell specific localisation in the liver and its regulation in hereditary haemochromatosis, chronic renal insufficiency, and renal anaemia
    Article Snippet: .. For western blot analysis, protein extracts were incubated for seven minutes at 94°C in sample buffer with 4% (wt/vol) sodium dodecyl sulphate (Merck, Darmstadt, Germany), 50 mM Tris HCl (pH 8.45), 1 mM EDTA, 3.24 mM dithiothreitol (Roth, Karlsruhe, Germany), 12.5% (wt/vol) glycerol (Merck), and 0.002% bromophenol blue (Merck). ..

    Incubation:

    Article Title: Pro-hepcidin: expression and cell specific localisation in the liver and its regulation in hereditary haemochromatosis, chronic renal insufficiency, and renal anaemia
    Article Snippet: .. For western blot analysis, protein extracts were incubated for seven minutes at 94°C in sample buffer with 4% (wt/vol) sodium dodecyl sulphate (Merck, Darmstadt, Germany), 50 mM Tris HCl (pH 8.45), 1 mM EDTA, 3.24 mM dithiothreitol (Roth, Karlsruhe, Germany), 12.5% (wt/vol) glycerol (Merck), and 0.002% bromophenol blue (Merck). ..

    Article Title: The E3 ubiquitin ligase RNF40 suppresses apoptosis in colorectal cancer cells
    Article Snippet: Sepharose beads with Protein A (GE Healthcare) were added and incubated for 2 h, and immunocomplexes were washed twice with Wash Buffer (20 mM EDTA, 500 mM LiCl, 1% (v /v ) 20 mM NaF, NP-40, 1% (w /v ) sodium deoxycholate, 100 mM Tris (pH 8.5)) and twice with TE buffer. .. Next, samples were incubated with RNase A (Qiagen) in 10 mM Tris (pH 8.0) at 37 °C for 30 min. For de-crosslinking, samples were incubated in 20 mM EDTA, 2% SDS, 100 mM Tris/HCl (pH 8), and 20 μg Proteinase K at 65 °C for 4 h. Samples were extracted with Roti® phenol/chloroform/isoamylalcohol (Roth) and DNA was precipitated with ethanol. .. ChIP-seq and data analysis ChIP libraries were prepared using the NEBNext® Ultra DNA library preparation Kit (NEB) according to the manufacturer’s instructions and samples were sequenced (single-end 50 bp) on a HiSeq2000 (Illumina).

    Article Title: Cofilin1-dependent actin dynamics control DRP1-mediated mitochondrial fission
    Article Snippet: After separation, proteins were blotted onto polyvinylidene fluoride membranes (Roti-PVDF; Roth, Karlsruhe, Germany) by using a wet blot apparatus (BioRad). .. For protein detection, membranes were incubated for 30 min at RT in 5% milk powder in T-TBS containing 150 mM KCl, 20 mM Tris-HCl (pH 7.4), 0.1% Tween-20 (Roth), followed by an incubation step with the primary antibody in 5% milk powder in T-TBS. .. After washing, membranes were incubated for 1 h at RT with the appropriate horseradish peroxidase-conjugated secondary antibody (Pierce, Rockford, IL, USA), diluted 1:1000 in 5% milk powder in T-TBS.

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    • tris hcl  (Carl Roth GmbH)
    86
    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: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tris hcl/product/Carl Roth GmbH
    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
    		  Buy from Supplier

    Image Search Results


    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: The results have shown that these media changes could be detected both by EIS and SPR and when changing the medium from 10 mM Tris-HCl to 1× PBS and then back to 10 mM Tris-HCl, no shift in minimum or impedance occurs.

    Techniques: