tris  (Millipore)

 
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    Name:
    Tris 2 carboxyethyl phosphine hydrochloride
    Description:
    Tris 2 carboxyethyl phosphine hydrochloride TCEP HCl is a non volatile solid It is a strong reducing agent 1 It can be synthesized by the acid hydrolysis of tris 2 cyanoethyl phosphine in refluxing aqueous HCl 1 It has various biological applications such as in vitro and in vivo reduction of disulfide bonds in various peptides and proteins 1 TCEP is a useful chelating agent for various heavy metal ions as Zn II Cd II Pb II and Ni II
    Catalog Number:
    C4706
    Price:
    None
    Applications:
    Reagent for the selective reduction of disulfides in water.
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    Structured Review

    Millipore tris
    Tris 2 carboxyethyl phosphine hydrochloride
    Tris 2 carboxyethyl phosphine hydrochloride TCEP HCl is a non volatile solid It is a strong reducing agent 1 It can be synthesized by the acid hydrolysis of tris 2 cyanoethyl phosphine in refluxing aqueous HCl 1 It has various biological applications such as in vitro and in vivo reduction of disulfide bonds in various peptides and proteins 1 TCEP is a useful chelating agent for various heavy metal ions as Zn II Cd II Pb II and Ni II
    https://www.bioz.com/result/tris/product/Millipore
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tris - by Bioz Stars, 2021-05
    86/100 stars

    Images

    1) Product Images from "Quantum and electrochemical interplays in hydrogenated graphene"

    Article Title: Quantum and electrochemical interplays in hydrogenated graphene

    Journal: Nature Communications

    doi: 10.1038/s41467-018-03026-0

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

    Techniques Used: Standard Deviation

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

    Techniques Used: Standard Deviation

    Related Articles

    other:

    Article Title: 3D-Printed Flow Cells for Aptamer-Based Impedimetric Detection of E. coli Crooks Strain
    Article Snippet: One µM aptamer solution was preconditioned with 200 µM Tris-(2-carboxyethyl)-phosphine-hydrochloride (TCEP) for 20 min for the reduction of disulfides, as described by Reich et al. [ ].

    Concentration Assay:

    Article Title: Dual radiosensitization and anti-STAT3 anti-proliferative strategy based on delivery of gold nanoparticle - oligonucleotide nanoconstructs to head and neck cancer cells.
    Article Snippet: .. The reduction of 3'-disulfide was performed by adding tris-(2-carboxyethyl)phosphine hydrochloride (Sigma-Aldrich) at a final concentration of 50 mM followed by an incubation for 15-20 min at room temperature. .. The ODN was purified using a P6 column equilibrated with 0.1M MES buffer pH 6.

    Incubation:

    Article Title: Dual radiosensitization and anti-STAT3 anti-proliferative strategy based on delivery of gold nanoparticle - oligonucleotide nanoconstructs to head and neck cancer cells.
    Article Snippet: .. The reduction of 3'-disulfide was performed by adding tris-(2-carboxyethyl)phosphine hydrochloride (Sigma-Aldrich) at a final concentration of 50 mM followed by an incubation for 15-20 min at room temperature. .. The ODN was purified using a P6 column equilibrated with 0.1M MES buffer pH 6.

    Article Title: Expression of Heat Shock and Other Stress Response Proteins in Ticks and Cultured Tick Cells in Response to Anaplasma spp. Infection and Heat Shock
    Article Snippet: Two-Dimensional Difference in Gel Electrophoresis (2D DIGE) CyDye DIGE fluor labeling kit for scarce protein samples (GE Healthcare) was used to label tick proteins according to the manufacturer's protocol. .. Briefly, for cysteine reduction before labeling, 5 μ g of protein of each sample were incubated with 2 nmol Tris (2carboxyethyl) phosphine hydrochloride (TCEP; Sigma) at 37°C for 1 hour in the dark and, for labeling, 4 nmol of Cy5 dye in 2 μ l of anhydrous DMF (Sigma) were added and the samples were incubated at 37°C for 30 min in the dark. .. For internal standardization, a pool of equal amounts of all samples (5 μ g per sample) was created and labeled with Cy3 dye with the same procedure but scaling adjusted the quantities of reagents according to the amount of protein (10 μ g).

    Labeling:

    Article Title: Expression of Heat Shock and Other Stress Response Proteins in Ticks and Cultured Tick Cells in Response to Anaplasma spp. Infection and Heat Shock
    Article Snippet: Two-Dimensional Difference in Gel Electrophoresis (2D DIGE) CyDye DIGE fluor labeling kit for scarce protein samples (GE Healthcare) was used to label tick proteins according to the manufacturer's protocol. .. Briefly, for cysteine reduction before labeling, 5 μ g of protein of each sample were incubated with 2 nmol Tris (2carboxyethyl) phosphine hydrochloride (TCEP; Sigma) at 37°C for 1 hour in the dark and, for labeling, 4 nmol of Cy5 dye in 2 μ l of anhydrous DMF (Sigma) were added and the samples were incubated at 37°C for 30 min in the dark. .. For internal standardization, a pool of equal amounts of all samples (5 μ g per sample) was created and labeled with Cy3 dye with the same procedure but scaling adjusted the quantities of reagents according to the amount of protein (10 μ g).

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  • 97
    Millipore bis tris
    Oligomers of purified MBP-5-HT 3A -ICD, <t>BSA</t> and heterodimer characterized by p CN-PAGE using a NativePAGE™ 3–12% <t>Bis-Tris</t> gel (Invitrogen). 3 μg of each protein, mixed prior with 0.03% or 0.04% or 0.05% (w/v) of the dye, was resolved per lane of a native gel indicated above. The corresponding oligomeric state of the proteins is denoted by an appropriate number of circles [black closed circle (MBP-5-HT 3A -ICD), red closed circle (BSA) and blue or gray closed circle (heterodimer)]. The gels were stained with Biorad Bio-Safe™ Coomassie G-250, and documented in gray color by Gel Doc EZ Imager.
    Bis Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 97 stars, based on 1 article reviews
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    99
    Millipore m tris hcl
    Immunochemistry of whole-cell extracts with anti-(1→5)-α-arabinan probe, LM6. A, Immunoblotting on nitrocellulose with LM6 of material separated by SDS-PAGE. Material (10 μg of protein per lane) from WT MG fruit (lanes 1–3) and Cnr MG fruit (lanes 4–6) were prepared in sample buffer immediately (lanes 1 and 4) or after incubation in <t>Tris-buffer</t> (lanes 2 and 5) or incubation in Tris-buffer plus <t>Pronase</t> E (lanes 3 and 6). Significant amounts of LM6-reactive, Pronase E-sensitive material entered the gel from Cnr , but not WT material. R indicates top of resolving gel. M shows M r markers. B, Immunodot assay on nitrocellulose of material (0.4 μg of protein per dot) analyzed in A showing abundance of LM6 epitope in all samples.
    M Tris Hcl, supplied by Millipore, 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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    Price from $9.99 to $1999.99
    m tris hcl - by Bioz Stars, 2021-05
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    97
    Millipore tris
    A) <t>Tris</t> absorbance change for myoglobin samples without <t>MES</t> scavenger, with 10 mM MES scavenger, and compensated conditions with 10 mM MES scavenger and increased laser fluence to obtain a ΔAbs 265 ≈ 4.97. B) (Blue) Peptide oxidation for myoglobin peptides in the absence of MES; (Orange) Peptide oxidation for myoglobin peptides in the presence of 10 mM MES; (Grey) Peptide oxidation for myoglobin in the presence of 10 mM MES under compensating laser fluence conditions, using Tris as a doseimeter for radical compensation. No statistically significant differences were detected in peptide oxidation between no MES samples and with MES-containing samples compensated using Tris dosimetry.
    Tris, supplied by Millipore, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tris/product/Millipore
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    tris - by Bioz Stars, 2021-05
    97/100 stars
      Buy from Supplier

    N/A
    SRM 723E cert SRM 723E SDS
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    Image Search Results


    Oligomers of purified MBP-5-HT 3A -ICD, BSA and heterodimer characterized by p CN-PAGE using a NativePAGE™ 3–12% Bis-Tris gel (Invitrogen). 3 μg of each protein, mixed prior with 0.03% or 0.04% or 0.05% (w/v) of the dye, was resolved per lane of a native gel indicated above. The corresponding oligomeric state of the proteins is denoted by an appropriate number of circles [black closed circle (MBP-5-HT 3A -ICD), red closed circle (BSA) and blue or gray closed circle (heterodimer)]. The gels were stained with Biorad Bio-Safe™ Coomassie G-250, and documented in gray color by Gel Doc EZ Imager.

    Journal: Protein expression and purification

    Article Title: A modified clear-native polyacrylamide gel electrophoresis technique to investigate the oligomeric state of MBP-5-HT3A-intracellular domain chimeras

    doi: 10.1016/j.pep.2018.08.010

    Figure Lengend Snippet: Oligomers of purified MBP-5-HT 3A -ICD, BSA and heterodimer characterized by p CN-PAGE using a NativePAGE™ 3–12% Bis-Tris gel (Invitrogen). 3 μg of each protein, mixed prior with 0.03% or 0.04% or 0.05% (w/v) of the dye, was resolved per lane of a native gel indicated above. The corresponding oligomeric state of the proteins is denoted by an appropriate number of circles [black closed circle (MBP-5-HT 3A -ICD), red closed circle (BSA) and blue or gray closed circle (heterodimer)]. The gels were stained with Biorad Bio-Safe™ Coomassie G-250, and documented in gray color by Gel Doc EZ Imager.

    Article Snippet: Prospect, IL); TCEP-HCl (Oakwood Chemical, N. Estill, SC); lysozyme (MP Biomedicals, Solon, OH); Protease inhibitor cocktail III (Research Products International); DNAse I (Alfa Aesar, Ward Hill, MA); BSA (Biorad); Serva Blue G (Sigma-Aldrich, St. Louis, MO), Bis-Tris (Sigma-Aldrich); Tricine (Sigma-Aldrich); 6-aminohexanoic acid (Sigma-Aldrich).

    Techniques: Purification, Clear Native PAGE, Staining

    Immunochemistry of whole-cell extracts with anti-(1→5)-α-arabinan probe, LM6. A, Immunoblotting on nitrocellulose with LM6 of material separated by SDS-PAGE. Material (10 μg of protein per lane) from WT MG fruit (lanes 1–3) and Cnr MG fruit (lanes 4–6) were prepared in sample buffer immediately (lanes 1 and 4) or after incubation in Tris-buffer (lanes 2 and 5) or incubation in Tris-buffer plus Pronase E (lanes 3 and 6). Significant amounts of LM6-reactive, Pronase E-sensitive material entered the gel from Cnr , but not WT material. R indicates top of resolving gel. M shows M r markers. B, Immunodot assay on nitrocellulose of material (0.4 μg of protein per dot) analyzed in A showing abundance of LM6 epitope in all samples.

    Journal: Plant Physiology

    Article Title: Altered Middle Lamella Homogalacturonan and Disrupted Deposition of (1- > 5)-?-l-Arabinan in the Pericarp of Cnr, a Ripening Mutant of Tomato 1

    doi:

    Figure Lengend Snippet: Immunochemistry of whole-cell extracts with anti-(1→5)-α-arabinan probe, LM6. A, Immunoblotting on nitrocellulose with LM6 of material separated by SDS-PAGE. Material (10 μg of protein per lane) from WT MG fruit (lanes 1–3) and Cnr MG fruit (lanes 4–6) were prepared in sample buffer immediately (lanes 1 and 4) or after incubation in Tris-buffer (lanes 2 and 5) or incubation in Tris-buffer plus Pronase E (lanes 3 and 6). Significant amounts of LM6-reactive, Pronase E-sensitive material entered the gel from Cnr , but not WT material. R indicates top of resolving gel. M shows M r markers. B, Immunodot assay on nitrocellulose of material (0.4 μg of protein per dot) analyzed in A showing abundance of LM6 epitope in all samples.

    Article Snippet: The powder (2 mL) was suspended in 50 m m Tris-HCl, pH 6.5, or 50 m m Tris-HCl, pH 6.5, containing Pronase E (Sigma) at 1 mg mL−1 .

    Techniques: SDS Page, Incubation

    A) Tris absorbance change for myoglobin samples without MES scavenger, with 10 mM MES scavenger, and compensated conditions with 10 mM MES scavenger and increased laser fluence to obtain a ΔAbs 265 ≈ 4.97. B) (Blue) Peptide oxidation for myoglobin peptides in the absence of MES; (Orange) Peptide oxidation for myoglobin peptides in the presence of 10 mM MES; (Grey) Peptide oxidation for myoglobin in the presence of 10 mM MES under compensating laser fluence conditions, using Tris as a doseimeter for radical compensation. No statistically significant differences were detected in peptide oxidation between no MES samples and with MES-containing samples compensated using Tris dosimetry.

    Journal: bioRxiv

    Article Title: Intrinsic Buffer Hydroxyl Radical Dosimetry Using Tris(Hydroxymethyl)Aminomethane

    doi: 10.1101/825463

    Figure Lengend Snippet: A) Tris absorbance change for myoglobin samples without MES scavenger, with 10 mM MES scavenger, and compensated conditions with 10 mM MES scavenger and increased laser fluence to obtain a ΔAbs 265 ≈ 4.97. B) (Blue) Peptide oxidation for myoglobin peptides in the absence of MES; (Orange) Peptide oxidation for myoglobin peptides in the presence of 10 mM MES; (Grey) Peptide oxidation for myoglobin in the presence of 10 mM MES under compensating laser fluence conditions, using Tris as a doseimeter for radical compensation. No statistically significant differences were detected in peptide oxidation between no MES samples and with MES-containing samples compensated using Tris dosimetry.

    Article Snippet: Material and Methods Tris, myoglobin, Glu1-fibrinopeptide B (GluB), and MES hydrate were purchased from Sigma-Aldrich Corporation (St. Louis, MO, USA).

    Techniques: