buffer  (Millipore)

 
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    Name:
    Triethylammonium acetate buffer
    Description:

    Catalog Number:
    90358
    Price:
    None
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    Structured Review

    Millipore buffer

    https://www.bioz.com/result/buffer/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    buffer - by Bioz Stars, 2021-06
    93/100 stars

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    Related Articles

    High Performance Liquid Chromatography:

    Article Title: Impact of charge state on 193 nm ultraviolet photodissociation of protein complexes
    Article Snippet: .. Reagents: Ammonium acetate, triethylammonium acetate (Sigma, St. Louis, MO), and m-nitrobenzyl alcohol (Aldrich) were dissolved in HPLC grade water (Millipore, Burlington, MA) to concentrations of 100 mM. .. Bovine Cu/Zn superoxide dismutase (SOD) was obtained from MP Biomedicals (Santa Ana, CA), streptavidin (SA) from ProteoChem (Hurricane, UT), human hemoglobin (Hb) from Sigma Aldrich (St. Louis, MO), transthyretin (TTR) from Lee BioSolutions (Maryland Heights, MO), and C-reactive protein (CRP) from EMD Millipore (Burlington, MA).

    other:

    Article Title: An improved strategy for the chemical synthesis of 3’, 5’-cyclic diguanylic acid
    Article Snippet: 40% CH3 CN in 0.1 M triethylammonium acetate buffer (pH 7.0)In a 2-L Erlenmeyer, add 600 mL 0.1 M triethylammonium acetate buffer (pH 7.0) and 400 mL acetonitrile.

    Article Title: Thermoreversible Polymer Gels in DMF Formed from Charge- and Crystallization-Induced Assembly
    Article Snippet: Triethylammonium acetate was prepared by dropping triethylamine into an equal mole of acetic acid at 5 °C.

    Incubation:

    Article Title: An Optimized and Versatile Counter-Flow Centrifugal Elutriation Workflow to Obtain Synchronized Eukaryotic Cells
    Article Snippet: EdU Labeling A 25 ml volume of elutriated cells (1 × 105 cells/ml) was continuously incubated with 100 μM EdU (5-ethynyl-2′-deoxyuridine, Code No. 1149-100, Click Chemistry Tools, Scottsdale, United States) with shaking at 30°C and 2 × 105 cells were collected after 0.25, 0.5, 1, 1.5, and 2 h. Cells were washed once with 10 mM Tris–HCl (pH 7.4) and resuspended in 70% ethanol. .. After fixation with 2% paraformaldehyde (PFA) in PBS and permeabilization with 1% Triton X-100, cells were incubated with 100 μl Click reactionTM cocktail 10 μl 2 M triethylammonium acetate pH 7.0, 10 μl dimethyl sulfoxide (DMSO, Code No. D8418, Sigma-Aldrich, Shanghai, China), 10 μl premixed 10 mM CuSO4 (Code No. 12849, Sigma-Aldrich, Shanghai, China) and 20 mM BTTAA (Code No. 1236-100, Click Chemistry Tools, Scottsdale, United States), 0.24 μl 1.3 mM AF488 Picolyl-Azide (Code No. 1276-1, Click Chemistry Tools, Scottsdale, United States) and 10 μl 200 mM sodium ascorbate (Code No. A7631-25G, Sigma-Aldrich, Shanghai, China) for 1 h in the dark. .. Cells were mounted with DAPI (Code No. P36935, Thermo Fisher Scientific, Shanghai, China).

    Purification:

    Article Title: Reverse Sanger sequencing of RNA by MALDI-TOF mass spectrometry after solid phase purification
    Article Snippet: RNA transcripts were purified by an Ethanol precipitation ( ). .. The precipitate was dissolved in 200 mM TEAA, pH 7, for reversed phase purification using ZipTips-C18 (Millipore, Bedford, MA) ( , ). ..

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  • 99
    Millipore buffer a
    Binding of lectins to L4 . ( A ) For each lectin, 4, 20 and 100 ng were spotted in triplicate. One set of a total of four sets is shown in the figure. Spots in rows A-C, columns 1–3 contained H. pomatia lectin (HPA), rows A-C, columns 4–6 contained T. vulgare lectin (WGA), rows D-F, columns 1–3 contained B. simplicifolia B 4 (BS) and rows D-F, columns 4–6 contained C. ensiformis lectin (ConA). The slide was incubated with 2% gelatin to block non-specific sites. Biotin-tagged peptide was incubated with the slide and then the amount of peptide bound was detected by binding of Cy3-conjugated streptavidin and measuring fluorescence of the spots. In columns marked B, <t>buffer</t> A was spotted as blanks. ( B ) Biotin-tagged L4 or control peptide was bound in wells of a streptavidin-coated microtiter plate. The wells were blocked with 2% gelatin, washed, and then equal amounts (50 ng) of lectins conjugated with peroxidase were added. After washing, the amount of lectin bound was detected by peroxidase activity. Standard curves were determined with each lectin-peroxidase conjugate to quantitate binding. Data are expressed as the amount of lectin bound minus a blank without peptide. Light blue bars, peptide L4; dark blue bars, control peptide.
    Buffer A, 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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    93
    Millipore buffers β gal
    Michaelis–Menten kinetics of the investigated biocatalytic reactions with freely dissolved enzymes. Kinetic parameters v max and K m were calculated by fitting the data to the Michaelis–Menten function, which is shown including 95% confidence bounds. In the whole figure, each data point represents one sample. (A) <t>β-Gal</t> kinetics for the cleavage of ONPG at pH 4.6 ( n = 3 separate runs). (B) BFD kinetics for the carboligation of benzaldehyde and a respective 2.5-fold excess of acetaldehyde ( n = 2 separate runs). Estimation of the confidence bounds was omitted because of limited data for substrate excess. (C) ADH kinetics for the reduction of acetophenone. (D) ADH kinetics for the reduction of ( S )-HPP, which was previously synthesized by BFD. For ADH kinetics, data points were generated in one batch due to shortage of the enzyme.
    Buffers β Gal, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Millipore laemmli sds page buffer
    Disulfide bonds of chlamydial T3S apparatus proteins are reduced in RBs. C. trachomatis L2 DG-purified RBs were treated with TCA in the presence of IAM, and protein pellets were resuspended in <t>SDS-PAGE</t> solubilization buffer containing (R) or lacking (NR)
    Laemmli Sds Page Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Millipore phosphate buffered saline pbs
    Representative examples of iNOS (1 st row), RANK (2 nd row) and TRAP (3 rd row) immunostainning in experimental periodontitis in rats. Staining was performed using periodontal tissues from normal control animals (b, g, l, q), animals subjected to experimental periodontitis that received topical applications of <t>HPMC</t> (c, h, m, r) or 10 mM HPMC/GSNO (d, i, n, s). Negative controls were samples of periodontal tissue where the primary antibody was replaced with <t>PBS-BSA</t> (5%); no immunostaining was detected (a, f, k, p). Magnification x200. Arrows points to immunostaining osteoclasts in the periodontal tissue of the control HPMC solution group (Magnification x1000).
    Phosphate Buffered Saline Pbs, 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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    Image Search Results


    Binding of lectins to L4 . ( A ) For each lectin, 4, 20 and 100 ng were spotted in triplicate. One set of a total of four sets is shown in the figure. Spots in rows A-C, columns 1–3 contained H. pomatia lectin (HPA), rows A-C, columns 4–6 contained T. vulgare lectin (WGA), rows D-F, columns 1–3 contained B. simplicifolia B 4 (BS) and rows D-F, columns 4–6 contained C. ensiformis lectin (ConA). The slide was incubated with 2% gelatin to block non-specific sites. Biotin-tagged peptide was incubated with the slide and then the amount of peptide bound was detected by binding of Cy3-conjugated streptavidin and measuring fluorescence of the spots. In columns marked B, buffer A was spotted as blanks. ( B ) Biotin-tagged L4 or control peptide was bound in wells of a streptavidin-coated microtiter plate. The wells were blocked with 2% gelatin, washed, and then equal amounts (50 ng) of lectins conjugated with peroxidase were added. After washing, the amount of lectin bound was detected by peroxidase activity. Standard curves were determined with each lectin-peroxidase conjugate to quantitate binding. Data are expressed as the amount of lectin bound minus a blank without peptide. Light blue bars, peptide L4; dark blue bars, control peptide.

    Journal: BMC Research Notes

    Article Title: A biologically active peptide mimetic of N-acetylgalactosamine/galactose

    doi: 10.1186/1756-0500-2-23

    Figure Lengend Snippet: Binding of lectins to L4 . ( A ) For each lectin, 4, 20 and 100 ng were spotted in triplicate. One set of a total of four sets is shown in the figure. Spots in rows A-C, columns 1–3 contained H. pomatia lectin (HPA), rows A-C, columns 4–6 contained T. vulgare lectin (WGA), rows D-F, columns 1–3 contained B. simplicifolia B 4 (BS) and rows D-F, columns 4–6 contained C. ensiformis lectin (ConA). The slide was incubated with 2% gelatin to block non-specific sites. Biotin-tagged peptide was incubated with the slide and then the amount of peptide bound was detected by binding of Cy3-conjugated streptavidin and measuring fluorescence of the spots. In columns marked B, buffer A was spotted as blanks. ( B ) Biotin-tagged L4 or control peptide was bound in wells of a streptavidin-coated microtiter plate. The wells were blocked with 2% gelatin, washed, and then equal amounts (50 ng) of lectins conjugated with peroxidase were added. After washing, the amount of lectin bound was detected by peroxidase activity. Standard curves were determined with each lectin-peroxidase conjugate to quantitate binding. Data are expressed as the amount of lectin bound minus a blank without peptide. Light blue bars, peptide L4; dark blue bars, control peptide.

    Article Snippet: The slide was washed 3 times with buffer A and then incubated with streptavidin conjugated with Cy3 (Sigma-Aldrich) for 1 h. The slide was again washed 3 times with buffer A and fluorescence detected in a microarray reader.

    Techniques: Binding Assay, Whole Genome Amplification, Incubation, Blocking Assay, Fluorescence, Activity Assay

    Michaelis–Menten kinetics of the investigated biocatalytic reactions with freely dissolved enzymes. Kinetic parameters v max and K m were calculated by fitting the data to the Michaelis–Menten function, which is shown including 95% confidence bounds. In the whole figure, each data point represents one sample. (A) β-Gal kinetics for the cleavage of ONPG at pH 4.6 ( n = 3 separate runs). (B) BFD kinetics for the carboligation of benzaldehyde and a respective 2.5-fold excess of acetaldehyde ( n = 2 separate runs). Estimation of the confidence bounds was omitted because of limited data for substrate excess. (C) ADH kinetics for the reduction of acetophenone. (D) ADH kinetics for the reduction of ( S )-HPP, which was previously synthesized by BFD. For ADH kinetics, data points were generated in one batch due to shortage of the enzyme.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Advantages of Hydrogel-Based 3D-Printed Enzyme Reactors and Their Limitations for Biocatalysis

    doi: 10.3389/fbioe.2018.00211

    Figure Lengend Snippet: Michaelis–Menten kinetics of the investigated biocatalytic reactions with freely dissolved enzymes. Kinetic parameters v max and K m were calculated by fitting the data to the Michaelis–Menten function, which is shown including 95% confidence bounds. In the whole figure, each data point represents one sample. (A) β-Gal kinetics for the cleavage of ONPG at pH 4.6 ( n = 3 separate runs). (B) BFD kinetics for the carboligation of benzaldehyde and a respective 2.5-fold excess of acetaldehyde ( n = 2 separate runs). Estimation of the confidence bounds was omitted because of limited data for substrate excess. (C) ADH kinetics for the reduction of acetophenone. (D) ADH kinetics for the reduction of ( S )-HPP, which was previously synthesized by BFD. For ADH kinetics, data points were generated in one batch due to shortage of the enzyme.

    Article Snippet: Enzymes and Buffers β-Gal (EC 3.2.1.23) from A. oryzae and the substrate ONPG were obtained from Sigma-Aldrich (Darmstadt, Germany) and used without further purification.

    Techniques: Synthesized, Generated

    Conversion curves in batch with enzymes entrapped in hydrogel lattices by following the formation of the respective product over time. (A) β-Gal kinetics for the cleavage of 2.2 mM ONPG at pH 4.6 ( n = 3 separate runs). (B) Formation of ( S )-HPP by BFD starting from 35 mM benzaldehyde and 87.5 mM acetaldehyde ( n = 2 separate runs). (C) ADH-catalyzed reduction of three different concentrations of acetophenone ( n = 2 separate runs). (D) ADH-catalyzed reduction of three different concentrations of ( S )-HPP, provided by BFD reactor experiments ( n = 1). Linear regression with a 95% confidence interval of the slope was applied.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Advantages of Hydrogel-Based 3D-Printed Enzyme Reactors and Their Limitations for Biocatalysis

    doi: 10.3389/fbioe.2018.00211

    Figure Lengend Snippet: Conversion curves in batch with enzymes entrapped in hydrogel lattices by following the formation of the respective product over time. (A) β-Gal kinetics for the cleavage of 2.2 mM ONPG at pH 4.6 ( n = 3 separate runs). (B) Formation of ( S )-HPP by BFD starting from 35 mM benzaldehyde and 87.5 mM acetaldehyde ( n = 2 separate runs). (C) ADH-catalyzed reduction of three different concentrations of acetophenone ( n = 2 separate runs). (D) ADH-catalyzed reduction of three different concentrations of ( S )-HPP, provided by BFD reactor experiments ( n = 1). Linear regression with a 95% confidence interval of the slope was applied.

    Article Snippet: Enzymes and Buffers β-Gal (EC 3.2.1.23) from A. oryzae and the substrate ONPG were obtained from Sigma-Aldrich (Darmstadt, Germany) and used without further purification.

    Techniques:

    Detected conversion to the respective product compound at the exit of the 3 ml reactor system of one exemplary run. Parameters were (A) β-Gal ( m = 0.38 mg/reactor) with ONPG substrate 2.2 mM, flow rate 0.05 ml/min. (B) BFD ( m = 56 mg/reactor) catalyzing the carboligation of benzaldehyde (25 mM) and acetaldehyde (62.5 mM), flow rate 0.017 ml/min. (C) ADH ( m = 42 mg/reactor) reducing acetophenone (50 mM), flow rate 0.017 ml/min. Reproducibility is shown by a second experiment with identical parameters. (D) ADH ( m = 58 mg/reactor) reducing ( S )-HPP provided by BFD reactor experiments (11 mM), flow rate 0.017 ml/min.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Advantages of Hydrogel-Based 3D-Printed Enzyme Reactors and Their Limitations for Biocatalysis

    doi: 10.3389/fbioe.2018.00211

    Figure Lengend Snippet: Detected conversion to the respective product compound at the exit of the 3 ml reactor system of one exemplary run. Parameters were (A) β-Gal ( m = 0.38 mg/reactor) with ONPG substrate 2.2 mM, flow rate 0.05 ml/min. (B) BFD ( m = 56 mg/reactor) catalyzing the carboligation of benzaldehyde (25 mM) and acetaldehyde (62.5 mM), flow rate 0.017 ml/min. (C) ADH ( m = 42 mg/reactor) reducing acetophenone (50 mM), flow rate 0.017 ml/min. Reproducibility is shown by a second experiment with identical parameters. (D) ADH ( m = 58 mg/reactor) reducing ( S )-HPP provided by BFD reactor experiments (11 mM), flow rate 0.017 ml/min.

    Article Snippet: Enzymes and Buffers β-Gal (EC 3.2.1.23) from A. oryzae and the substrate ONPG were obtained from Sigma-Aldrich (Darmstadt, Germany) and used without further purification.

    Techniques: Flow Cytometry

    Overview of the studied reactions. (A) Hydrolysis of o-Nitrophenyl-β- d -galactopyranoside (ONPG) by β-Gal yields the monosaccharides galactose and o-nitrophenol. (B) Activity of ADH can be determined by enantioselective reduction of acetophenone to ( R )-phenylethanol. (C) The combination of BFD and ADH in a 2-step cascade reaction. Carboligation of the educts benzaldehyde and acetaldehyde catalyzed by BFD yields the intermediate ( S )-2-hydroxy-1-phenyl-propanone (( S )-HPP), which can be further reduced to the product (1 S ,2 S )-1-phenylpropane-1,2-diol (( S,S )-PPD) by ADH. The redox equivalents are delivered by the cofactor NADPH that is oxidized to NADP + . For in situ regeneration of NADPH 2-propanol was added in excess which is oxidized to acetone by the same ADH.

    Journal: Frontiers in Bioengineering and Biotechnology

    Article Title: Advantages of Hydrogel-Based 3D-Printed Enzyme Reactors and Their Limitations for Biocatalysis

    doi: 10.3389/fbioe.2018.00211

    Figure Lengend Snippet: Overview of the studied reactions. (A) Hydrolysis of o-Nitrophenyl-β- d -galactopyranoside (ONPG) by β-Gal yields the monosaccharides galactose and o-nitrophenol. (B) Activity of ADH can be determined by enantioselective reduction of acetophenone to ( R )-phenylethanol. (C) The combination of BFD and ADH in a 2-step cascade reaction. Carboligation of the educts benzaldehyde and acetaldehyde catalyzed by BFD yields the intermediate ( S )-2-hydroxy-1-phenyl-propanone (( S )-HPP), which can be further reduced to the product (1 S ,2 S )-1-phenylpropane-1,2-diol (( S,S )-PPD) by ADH. The redox equivalents are delivered by the cofactor NADPH that is oxidized to NADP + . For in situ regeneration of NADPH 2-propanol was added in excess which is oxidized to acetone by the same ADH.

    Article Snippet: Enzymes and Buffers β-Gal (EC 3.2.1.23) from A. oryzae and the substrate ONPG were obtained from Sigma-Aldrich (Darmstadt, Germany) and used without further purification.

    Techniques: Activity Assay, In Situ

    Disulfide bonds of chlamydial T3S apparatus proteins are reduced in RBs. C. trachomatis L2 DG-purified RBs were treated with TCA in the presence of IAM, and protein pellets were resuspended in SDS-PAGE solubilization buffer containing (R) or lacking (NR)

    Journal: Journal of Bacteriology

    Article Title: Disulfide Bonding within Components of the Chlamydia Type III Secretion Apparatus Correlates with Development ▿

    doi: 10.1128/JB.05163-11

    Figure Lengend Snippet: Disulfide bonds of chlamydial T3S apparatus proteins are reduced in RBs. C. trachomatis L2 DG-purified RBs were treated with TCA in the presence of IAM, and protein pellets were resuspended in SDS-PAGE solubilization buffer containing (R) or lacking (NR)

    Article Snippet: For immunoblot analysis of ectopically expressed CdsF constructs, samples were normalized for cell content based on the final OD600 of bacterial cultures and solubilized in the appropriate volume of Laemmli SDS-PAGE buffer plus or minus 5% (vol/vol) β-ME (Sigma).

    Techniques: Purification, SDS Page

    Representative examples of iNOS (1 st row), RANK (2 nd row) and TRAP (3 rd row) immunostainning in experimental periodontitis in rats. Staining was performed using periodontal tissues from normal control animals (b, g, l, q), animals subjected to experimental periodontitis that received topical applications of HPMC (c, h, m, r) or 10 mM HPMC/GSNO (d, i, n, s). Negative controls were samples of periodontal tissue where the primary antibody was replaced with PBS-BSA (5%); no immunostaining was detected (a, f, k, p). Magnification x200. Arrows points to immunostaining osteoclasts in the periodontal tissue of the control HPMC solution group (Magnification x1000).

    Journal: PLoS ONE

    Article Title: Topical HPMC/S-Nitrosoglutathione Solution Decreases Inflammation and Bone Resorption in Experimental Periodontal Disease in Rats

    doi: 10.1371/journal.pone.0153716

    Figure Lengend Snippet: Representative examples of iNOS (1 st row), RANK (2 nd row) and TRAP (3 rd row) immunostainning in experimental periodontitis in rats. Staining was performed using periodontal tissues from normal control animals (b, g, l, q), animals subjected to experimental periodontitis that received topical applications of HPMC (c, h, m, r) or 10 mM HPMC/GSNO (d, i, n, s). Negative controls were samples of periodontal tissue where the primary antibody was replaced with PBS-BSA (5%); no immunostaining was detected (a, f, k, p). Magnification x200. Arrows points to immunostaining osteoclasts in the periodontal tissue of the control HPMC solution group (Magnification x1000).

    Article Snippet: Reagents and drugs Hydroxypropylmethylcellulose (HPMC; Mn 90000), glutathione (GSH), sodium nitrite (NaNO2 ), phosphate-buffered saline (PBS) pH 7.4, acetone and hydrochloric acid (HCl) were purchased from Sigma-Aldrich (St. Louis, MO, USA).

    Techniques: Staining, Immunostaining