ethylenediaminetetraacetic acid edta disodium salt  (Millipore)


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    Name:
    Ethylenediaminetetraacetic acid
    Description:
    Ethylenediaminetetraacetic acid EDTA is a hydrophilic metal chelating agent that transforms metal ions into inactive cyclic metal complexes Hence it has industrial application for resolving metal contamination
    Catalog Number:
    e9884
    Price:
    None
    Applications:
    Ethylenediaminetetraacetic acid has been used: . as a component of labeling buffer, which is used in the washing step during cell fractionation{155) . for investigating the effect of papain enzyme on wound debridement and other skin issues . for harvesting rat arterial smooth muscle cell after its pre-treatment for its use in flow cytometry analysis
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    Structured Review

    Millipore ethylenediaminetetraacetic acid edta disodium salt
    Ethylenediaminetetraacetic acid
    Ethylenediaminetetraacetic acid EDTA is a hydrophilic metal chelating agent that transforms metal ions into inactive cyclic metal complexes Hence it has industrial application for resolving metal contamination
    https://www.bioz.com/result/ethylenediaminetetraacetic acid edta disodium salt/product/Millipore
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    ethylenediaminetetraacetic acid edta disodium salt - by Bioz Stars, 2020-07
    99/100 stars

    Images

    1) Product Images from "Monitoring bone changes due to calcium, magnesium, and phosphorus loss in rat femurs using Quantitative Ultrasound"

    Article Title: Monitoring bone changes due to calcium, magnesium, and phosphorus loss in rat femurs using Quantitative Ultrasound

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-30327-7

    Experimental diagram. Progressive demineralization each day. EDTA - Ethylenediaminetetraacetic Acid solutions; QUS - Quantitative Ultrasound; QCT - Quantitative Computed Tomography; ICP OES - coupled plasma optical emission spectrometry. Day 0 - integer bone. Demineralization occurs from Day 1 to Day 5.
    Figure Legend Snippet: Experimental diagram. Progressive demineralization each day. EDTA - Ethylenediaminetetraacetic Acid solutions; QUS - Quantitative Ultrasound; QCT - Quantitative Computed Tomography; ICP OES - coupled plasma optical emission spectrometry. Day 0 - integer bone. Demineralization occurs from Day 1 to Day 5.

    Techniques Used: Computed Tomography

    2) Product Images from "Monitoring bone changes due to calcium, magnesium, and phosphorus loss in rat femurs using Quantitative Ultrasound"

    Article Title: Monitoring bone changes due to calcium, magnesium, and phosphorus loss in rat femurs using Quantitative Ultrasound

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-30327-7

    Experimental diagram. Progressive demineralization each day. EDTA - Ethylenediaminetetraacetic Acid solutions; QUS - Quantitative Ultrasound; QCT - Quantitative Computed Tomography; ICP OES - coupled plasma optical emission spectrometry. Day 0 - integer bone. Demineralization occurs from Day 1 to Day 5.
    Figure Legend Snippet: Experimental diagram. Progressive demineralization each day. EDTA - Ethylenediaminetetraacetic Acid solutions; QUS - Quantitative Ultrasound; QCT - Quantitative Computed Tomography; ICP OES - coupled plasma optical emission spectrometry. Day 0 - integer bone. Demineralization occurs from Day 1 to Day 5.

    Techniques Used: Computed Tomography

    Related Articles

    Concentration Assay:

    Article Title: Monitoring bone changes due to calcium, magnesium, and phosphorus loss in rat femurs using Quantitative Ultrasound
    Article Snippet: .. The demineralization protocol consisted of immersing the rat femur samples in a 25-mL solution of Ethylenediaminetetraacetic Acid (EDTA) disodium salt (Sigma-Aldrich®, Missouri, USA) at pH = 8 and 0.376 M concentration for 24 h at 25.0 ± 1.5 °C, and a new solution and new reservoir were used each day . ..

    Protein Extraction:

    Article Title: SUMOylation of HNF4? regulates protein stability and hepatocyte function
    Article Snippet: .. Cellular protein extraction Cells grown in a six-well plate were lysed in 150 µl of SUMO lysis buffer [2% SDS, 50 mM Tris-HCl, pH 8, 1 mM ethylenediaminetetraacetic acid (EDTA) and 10 mM iodoacetamide (all from Sigma-Aldrich)] for 5 minutes at room temperature. ..

    Sulforhodamine B Assay:

    Article Title: Enhanced uptake and transport of (+)-catechin and (-)-epigallocatechin gallate in niosomal formulation by human intestinal Caco-2 cells
    Article Snippet: .. Chemicals and reagents Catechin, EGCG, sorbitan monostearate (Span 60), CH, dihexadecyl phosphate, fluorescein isothiocyanate (FITC), sulforhodamine B (SRB), fluorescein sodium salt, ascorbic acid (AA), sodium azide, verapamil, 5-(3-(2-(7-chloroquinolin-2-yl)ethenyl)phenyl)-8-dimethylcarbamyl-4,6-dithiaoctanoic acid sodium salt hydrate (MK-571), and ethylenediaminetetraacetic acid (EDTA) were purchased from Sigma-Aldrich (St Louis, MO, USA). ..

    Lysis:

    Article Title: SUMOylation of HNF4? regulates protein stability and hepatocyte function
    Article Snippet: .. Cellular protein extraction Cells grown in a six-well plate were lysed in 150 µl of SUMO lysis buffer [2% SDS, 50 mM Tris-HCl, pH 8, 1 mM ethylenediaminetetraacetic acid (EDTA) and 10 mM iodoacetamide (all from Sigma-Aldrich)] for 5 minutes at room temperature. ..

    Article Title: Internalization Mechanisms of the Epidermal Growth Factor Receptor after Activation with Different Ligands
    Article Snippet: .. Cells were rinsed in cold PBS and scraped off in RIPA lysis buffer (1% NP40, 20 mM MOPS, 0.1% SDS, 1% Na-deoxycholate, 150 mM NaCl, and 1 mM ethylenediaminetetraacetic acid) supplemented with Protease Inhibitor Cocktail Set II and Phosphatase Inhibitor Cocktail Set III (Calbiochem). .. Cell debris was removed by centrifugation.

    Protease Inhibitor:

    Article Title: Internalization Mechanisms of the Epidermal Growth Factor Receptor after Activation with Different Ligands
    Article Snippet: .. Cells were rinsed in cold PBS and scraped off in RIPA lysis buffer (1% NP40, 20 mM MOPS, 0.1% SDS, 1% Na-deoxycholate, 150 mM NaCl, and 1 mM ethylenediaminetetraacetic acid) supplemented with Protease Inhibitor Cocktail Set II and Phosphatase Inhibitor Cocktail Set III (Calbiochem). .. Cell debris was removed by centrifugation.

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    Millipore nmr buffer
    The m 6 A modification has minor effects on RREIIB structure and dynamics. (A) Secondary structure of RRE2Bm 6A68 , with the residues showing line-broadening with m 6 A, highlighted in red (with Mg 2+ ) and blue (no Mg 2+ ). Comparison of the 1D 1 H <t>NMR</t> spectrum of RREIIB m6A68 with or without Mg 2+ with the methyl peak indicated by arrows. The comparison of 1D imino spectra (B) and 2D [ 1 H, 13 C]-HSQC spectra (C) of RREIIB m6A68 and RREIIB in the presence (red) and absence (blue) of 3 mM Mg 2+ . Resonances exhibiting shifting are indicated using arrows, and those with ambiguous assignments denoted using an asterisk. (D) Normalized resonance intensities in 2D [ 1 H, 13 C]-HSQC spectra of RREIIB m6A68 and RREIIB in the presence (red) and absence (blue) of 3 mM Mg 2+ . A52-C8H8, A52-C2H2 and U56-C6H6 were used as a reference and normalized to 0.1. The sample conditions were 1.2–1.5 mM RREIIB m6A68 or RREIIB in 15 mM sodium phosphate, 25 mM <t>NaCl,</t> 0.1 mM EDTA, pH 6.4 with or without 3 mM MgCl 2 .
    Nmr Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nmr buffer/product/Millipore
    Average 99 stars, based on 124 article reviews
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    nmr buffer - by Bioz Stars, 2020-07
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    91
    Millipore calpain reaction buffer
    Schematic diagram showing the relationship of <t>calpain/NF-κB/inflammation/NVU</t> damage after CCI in mice. Traumatic brain injury induces calcium overload, which, in turn, upregulates calpain. Calpain may downregulate IκB and activate NF-κB. NF-κB induces activation of TNF-α, iNOS, ICAM-1, and MMP-9. These inflammatory substances induce degradation of basal lamina and tight junction proteins, resulting in NVU disruption, leading to brain edema. MDL28170 could reverse those changes. NF-κB: Nuclear factor-κB; NVU: Neurovascular unit; CCI: Controlled cortical impact; IκB: Inhibitory-κB; TNF-α: Tumor necrosis factor-α; iNOS: Inducible nitric oxide synthase; ICAM-1: Intracellular adhesion molecule-1; MMP-9: Matrix metalloproteinase-9.
    Calpain Reaction Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore p50 storage buffer
    E3330 inhibits both repair and redox activity of APE1. Shown are data from steady-state kinetics experiments for (A) APE1 ΔN38 (2.5 nM) and (B) full-length APE1 (1 nM) collected with 1 μM AP DNA substrate in the absence (black) or presence (red) of 100 μM E3330. For APE1 ΔN38 , rate constants are k obs = 0.53 ± 0.02 s −1 without E3330 and k obs = 0.29 ± 0.02 s −1 with E3330. For APE1, k obs = 0.39 ± 0.01 s −1 without E3330 and k obs = 0.13 ± 0.01 s −1 with E3330. (C) EMSA results show E3330 inhibits the redox activity of APE1 ΔN38 and APE1. Binding of <t>p50</t> to its cognate DNA (0.1 μM) is much weaker for oxidized p50 (lane 2) relative to reduced p50 (lane 5). DNA binding of oxidized p50 (1.5 μM) is activated by APE1 ΔN38 (20 μM, lane 6) and by APE1 (20 μM, lane 13), and activation of p50 by APE1 is inhibited by E3330 (concentrations are 0.2, 0.4, 0.6, 0.8, and 1.0 mM E3330 in lanes 7–11 and 14–18). The protein-DNA bands are annotated as follows: 1:1 p50:DNA, (°); 2:1 p50:DNA, (●); non-specific APE1-DNA binding, (*).
    P50 Storage Buffer, 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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    Image Search Results


    The m 6 A modification has minor effects on RREIIB structure and dynamics. (A) Secondary structure of RRE2Bm 6A68 , with the residues showing line-broadening with m 6 A, highlighted in red (with Mg 2+ ) and blue (no Mg 2+ ). Comparison of the 1D 1 H NMR spectrum of RREIIB m6A68 with or without Mg 2+ with the methyl peak indicated by arrows. The comparison of 1D imino spectra (B) and 2D [ 1 H, 13 C]-HSQC spectra (C) of RREIIB m6A68 and RREIIB in the presence (red) and absence (blue) of 3 mM Mg 2+ . Resonances exhibiting shifting are indicated using arrows, and those with ambiguous assignments denoted using an asterisk. (D) Normalized resonance intensities in 2D [ 1 H, 13 C]-HSQC spectra of RREIIB m6A68 and RREIIB in the presence (red) and absence (blue) of 3 mM Mg 2+ . A52-C8H8, A52-C2H2 and U56-C6H6 were used as a reference and normalized to 0.1. The sample conditions were 1.2–1.5 mM RREIIB m6A68 or RREIIB in 15 mM sodium phosphate, 25 mM NaCl, 0.1 mM EDTA, pH 6.4 with or without 3 mM MgCl 2 .

    Journal: PLoS ONE

    Article Title: m6A minimally impacts the structure, dynamics, and Rev ARM binding properties of HIV-1 RRE stem IIB

    doi: 10.1371/journal.pone.0224850

    Figure Lengend Snippet: The m 6 A modification has minor effects on RREIIB structure and dynamics. (A) Secondary structure of RRE2Bm 6A68 , with the residues showing line-broadening with m 6 A, highlighted in red (with Mg 2+ ) and blue (no Mg 2+ ). Comparison of the 1D 1 H NMR spectrum of RREIIB m6A68 with or without Mg 2+ with the methyl peak indicated by arrows. The comparison of 1D imino spectra (B) and 2D [ 1 H, 13 C]-HSQC spectra (C) of RREIIB m6A68 and RREIIB in the presence (red) and absence (blue) of 3 mM Mg 2+ . Resonances exhibiting shifting are indicated using arrows, and those with ambiguous assignments denoted using an asterisk. (D) Normalized resonance intensities in 2D [ 1 H, 13 C]-HSQC spectra of RREIIB m6A68 and RREIIB in the presence (red) and absence (blue) of 3 mM Mg 2+ . A52-C8H8, A52-C2H2 and U56-C6H6 were used as a reference and normalized to 0.1. The sample conditions were 1.2–1.5 mM RREIIB m6A68 or RREIIB in 15 mM sodium phosphate, 25 mM NaCl, 0.1 mM EDTA, pH 6.4 with or without 3 mM MgCl 2 .

    Article Snippet: After measuring the concentration, the RNA samples were buffer-exchanged into NMR buffer (15 mM sodium phosphate, 25 mM NaCl, 0.1 mM EDTA, with or without 3 mM MgCl2 at pH = 6.4) three times using 3kDa Amicon Ultra centrifugal filters (EMD Millipore).

    Techniques: Modification, Nuclear Magnetic Resonance

    Schematic diagram showing the relationship of calpain/NF-κB/inflammation/NVU damage after CCI in mice. Traumatic brain injury induces calcium overload, which, in turn, upregulates calpain. Calpain may downregulate IκB and activate NF-κB. NF-κB induces activation of TNF-α, iNOS, ICAM-1, and MMP-9. These inflammatory substances induce degradation of basal lamina and tight junction proteins, resulting in NVU disruption, leading to brain edema. MDL28170 could reverse those changes. NF-κB: Nuclear factor-κB; NVU: Neurovascular unit; CCI: Controlled cortical impact; IκB: Inhibitory-κB; TNF-α: Tumor necrosis factor-α; iNOS: Inducible nitric oxide synthase; ICAM-1: Intracellular adhesion molecule-1; MMP-9: Matrix metalloproteinase-9.

    Journal: Chinese Medical Journal

    Article Title: Protective Effects of Calpain Inhibition on Neurovascular Unit Injury through Downregulating Nuclear Factor-κB-related Inflammation during Traumatic Brain Injury in Mice

    doi: 10.4103/0366-6999.198001

    Figure Lengend Snippet: Schematic diagram showing the relationship of calpain/NF-κB/inflammation/NVU damage after CCI in mice. Traumatic brain injury induces calcium overload, which, in turn, upregulates calpain. Calpain may downregulate IκB and activate NF-κB. NF-κB induces activation of TNF-α, iNOS, ICAM-1, and MMP-9. These inflammatory substances induce degradation of basal lamina and tight junction proteins, resulting in NVU disruption, leading to brain edema. MDL28170 could reverse those changes. NF-κB: Nuclear factor-κB; NVU: Neurovascular unit; CCI: Controlled cortical impact; IκB: Inhibitory-κB; TNF-α: Tumor necrosis factor-α; iNOS: Inducible nitric oxide synthase; ICAM-1: Intracellular adhesion molecule-1; MMP-9: Matrix metalloproteinase-9.

    Article Snippet: [ ] In brief, cytosolic and mitochondrial proteins (30 μg) were incubated with calpain reaction buffer (20 mmol/L HEPES, 1 mmol/L EDTA, 50 mmol/L NaCl, and 0.1% (v/v) 2-mercaptoethanol, containing 10 μmol/L calpain I fluorescent substrate [Calbiochem Co., La Jolla, CA, USA], pH 7.6).

    Techniques: Mouse Assay, Activation Assay

    MDL28170 treatment suppresses the calpain activity in the cytosolic and mitochondrial fractions and upregulates the expression of calpastatin in the cytosolic fractions. (a and b) The bar graphs reflect the calpain activity in the cytosolic fractions and mitochondrial fractions at 6 h and 24 h. (c) Representative Western blots of calpastatin and β-actin from each group; (d) the results were quantified and are shown as the mean ± SD. * P

    Journal: Chinese Medical Journal

    Article Title: Protective Effects of Calpain Inhibition on Neurovascular Unit Injury through Downregulating Nuclear Factor-κB-related Inflammation during Traumatic Brain Injury in Mice

    doi: 10.4103/0366-6999.198001

    Figure Lengend Snippet: MDL28170 treatment suppresses the calpain activity in the cytosolic and mitochondrial fractions and upregulates the expression of calpastatin in the cytosolic fractions. (a and b) The bar graphs reflect the calpain activity in the cytosolic fractions and mitochondrial fractions at 6 h and 24 h. (c) Representative Western blots of calpastatin and β-actin from each group; (d) the results were quantified and are shown as the mean ± SD. * P

    Article Snippet: [ ] In brief, cytosolic and mitochondrial proteins (30 μg) were incubated with calpain reaction buffer (20 mmol/L HEPES, 1 mmol/L EDTA, 50 mmol/L NaCl, and 0.1% (v/v) 2-mercaptoethanol, containing 10 μmol/L calpain I fluorescent substrate [Calbiochem Co., La Jolla, CA, USA], pH 7.6).

    Techniques: Activity Assay, Expressing, Western Blot

    E3330 inhibits both repair and redox activity of APE1. Shown are data from steady-state kinetics experiments for (A) APE1 ΔN38 (2.5 nM) and (B) full-length APE1 (1 nM) collected with 1 μM AP DNA substrate in the absence (black) or presence (red) of 100 μM E3330. For APE1 ΔN38 , rate constants are k obs = 0.53 ± 0.02 s −1 without E3330 and k obs = 0.29 ± 0.02 s −1 with E3330. For APE1, k obs = 0.39 ± 0.01 s −1 without E3330 and k obs = 0.13 ± 0.01 s −1 with E3330. (C) EMSA results show E3330 inhibits the redox activity of APE1 ΔN38 and APE1. Binding of p50 to its cognate DNA (0.1 μM) is much weaker for oxidized p50 (lane 2) relative to reduced p50 (lane 5). DNA binding of oxidized p50 (1.5 μM) is activated by APE1 ΔN38 (20 μM, lane 6) and by APE1 (20 μM, lane 13), and activation of p50 by APE1 is inhibited by E3330 (concentrations are 0.2, 0.4, 0.6, 0.8, and 1.0 mM E3330 in lanes 7–11 and 14–18). The protein-DNA bands are annotated as follows: 1:1 p50:DNA, (°); 2:1 p50:DNA, (●); non-specific APE1-DNA binding, (*).

    Journal: Biochemistry

    Article Title: NMR Studies Reveal an Unexpected Binding Site for a Redox Inhibitor of AP Endonuclease 1

    doi: 10.1021/bi201071g

    Figure Lengend Snippet: E3330 inhibits both repair and redox activity of APE1. Shown are data from steady-state kinetics experiments for (A) APE1 ΔN38 (2.5 nM) and (B) full-length APE1 (1 nM) collected with 1 μM AP DNA substrate in the absence (black) or presence (red) of 100 μM E3330. For APE1 ΔN38 , rate constants are k obs = 0.53 ± 0.02 s −1 without E3330 and k obs = 0.29 ± 0.02 s −1 with E3330. For APE1, k obs = 0.39 ± 0.01 s −1 without E3330 and k obs = 0.13 ± 0.01 s −1 with E3330. (C) EMSA results show E3330 inhibits the redox activity of APE1 ΔN38 and APE1. Binding of p50 to its cognate DNA (0.1 μM) is much weaker for oxidized p50 (lane 2) relative to reduced p50 (lane 5). DNA binding of oxidized p50 (1.5 μM) is activated by APE1 ΔN38 (20 μM, lane 6) and by APE1 (20 μM, lane 13), and activation of p50 by APE1 is inhibited by E3330 (concentrations are 0.2, 0.4, 0.6, 0.8, and 1.0 mM E3330 in lanes 7–11 and 14–18). The protein-DNA bands are annotated as follows: 1:1 p50:DNA, (°); 2:1 p50:DNA, (●); non-specific APE1-DNA binding, (*).

    Article Snippet: Briefly, p50 was reduced by incubation in p50 storage buffer (0.02 M HEPES, pH 7.9, 0.1 M KCl, 0.2 mM EDTA, 10% glycerol) with 1 mM tris(2-carboxyethyl)phosphine (TCEP; Calbiochem) for 30 min at 16 °C, and p50 was oxidized in the same buffer but with 1 mM diamide (Sigma) for 30 min at 16 °C.

    Techniques: Activity Assay, Binding Assay, Activation Assay