ethylenediaminetetraacetic acid tripotassium salt dihydrate edta  (Millipore)


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    Name:
    Ethylenediaminetetraacetic acid tripotassium salt dihydrate
    Description:

    Catalog Number:
    e0270
    Price:
    None
    Applications:
    Used to eliminate inhibition of enzyme catalyzed reactions due to traces of heavy metals
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    Structured Review

    Millipore ethylenediaminetetraacetic acid tripotassium salt dihydrate edta
    Ethylenediaminetetraacetic acid tripotassium salt dihydrate

    https://www.bioz.com/result/ethylenediaminetetraacetic acid tripotassium salt dihydrate edta/product/Millipore
    Average 90 stars, based on 1 article reviews
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    Article Title: The Effect of Digestion and Drug Load on Halofantrine Absorption from Self-nanoemulsifying Drug Delivery System (SNEDDS)
    Article Snippet: Soybean oil (long-chain (LC) glycerides), glycerol, ethylenediaminetetraacetic acid tripotassium salt dihydrate (EDTA), 4-bromophenyl-boronic acid (BBBA), bile extract, tris-(hydroxymethyl)aminomethane (tris), maleic acid, calcium chloride, sodium hydroxide, and porcine pancreatic lipase were obtained from Sigma-Aldrich (St. Louis, MO, USA).

    Article Title: Prenatal administration of vitamin A alters pulmonary and plasma levels of vascular endothelial growth factor in the developing mouse
    Article Snippet: The needle and syringe were previously passed through a solution of ethylenediaminetetraacetic acid tripotassium salt dihydrate (Sigma, Steinheim, Germany) in NaCl 0.9% (B. Braun, Germany) at 25 mg/ml.

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    Millipore pbs edta
    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as <t>PBS-EDTA,</t> to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.
    Pbs Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    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: 95/100, based on 106 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    98
    Millipore m edta
    Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) induce Ca 2+ mobilization and phospholipase D (PLD) activation in type II alveolar epithelial cells. (a, c) A549 cells were labelled with 3 μ m Fluo-3/AM, treated or not with <t>EDTA,</t> <t>EGTA</t>
    M Edta, supplied by Millipore, used in various techniques. Bioz Stars score: 98/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore immunoprecipitation buffer
    Binding of Wt1 protein to the 5′-flanking region of the Adamts16 gene. ChIP was performed to detect Wt1 protein bound to the 5′-flanking region of the Adamts16 gene in its native chromosomal configuration. The drawing ( A ) delineates the three predicted Wt1 binding sites ( Wt1-A , Wt1-B , and Wt1-C ) in the promoter and 5′-UTR of the Adamts16 gene and allocates the PCR primers used for DNA amplification. Specific antibodies against Wt1 and histone proteins were chosen for <t>immunoprecipitation</t> of M15 whole cell lysates. Amplicons encompassing the 5′-flanking region of the Adamts16 gene were enriched ∼2.5-fold with the use of anti-Wt1 antibody compared with normal rabbit IgG (NRb-IgG). No differences in actin DNA were observed between anti-Wt1 antibody and normal rabbit IgG ( B ). The gene encoding anti-Müllerian hormone receptor 2 ( Amhr2 ), served as a positive control ( B ). Binding of Wt1(−KTS) protein to the Adamts16 promoter was confirmed in stimulated UB27 cells ( C ). Wt1(+KTS) protein failed to interact with the promoter of the Adamts16 gene in UD28 cells ( D ). Data shown are means ± S.E. ( error bars ). Statistical significances are indicated by asterisks (*, p
    Immunoprecipitation Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 187 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as PBS-EDTA, to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: Representative absorbance spectra of AMB-PEG 2 and unconjugated AMB formulations prepared in buffers with varying hydrophobicity. 20 mM AMB-PEG 2 and unconjugated AMB formulations were prepared in DMSO and resuspended in 20% and 48% ACN buffers containing 4.3% acetic acid, as well as PBS-EDTA, to a final concentration of 2 mM AMB. As buffer hydrophobicity increases with higher ACN concentrations, the A 348 /A 409 ratio decreases, implying that AMB-PEG is increasingly in its monomeric form. As AMB-PEG 1 and 2 have similar UV-visible absorption profiles, with identical peak height ratios in all buffers tested, data for AMB-PEG 1 is not shown. AMB-PEG formulations that have been subjected to buffer exchange to PBS-EDTA through a 10 kDa centrifugal filter have the same UV-visible absorption spectra as the initial formulation of AMB-PEG in PBS-EDTA, which contains 10% DMSO.

    Article Snippet: AMB-PEG Particle Size Determination Using DLS 2 mM solutions of AMB-PEG were prepared in PBS-EDTA, and diafiltration carried out with PBS-EDTA using 10 kDa centrifugal filters (Millipore).

    Techniques: Concentration Assay, Buffer Exchange

    (A) Reverse phase chromatogram of AMB-PEG and unconjugated AMB, with eluted peaks detected at 406 nm. 50 μL of AMB-PEG 1 and 2, and 10 μL of unconjugated AMB dispersed in PBS-EDTA and 48% ACN respectively were injected into a C18 reverse phase column and eluted isocratically in a 48% ACN buffer at a flow rate of 0.5 ml/min for 40 minutes. Peaks were detected at 406 nm. The AMB-PEG conjugate has a shorter retention time, implying that it is more hydrophilic. From the AMB-PEG samples, AMB-PEG conjugate and free AMB (based on the retention time of unconjugated AMB) fractions were collected for further analysis via size exclusion chromatography. (B) Size exclusion chromatogram of AMB-PEG 2 and unconjugated AMB, as well as the relevant fractions collected from RPC, in a 20% ACN mobile phase. 20 mM of AMB-PEG 2 formulations and unconjugated AMB in DMSO were prepared and resuspended at 2 mM in a 20% ACN buffer. 50 μL of these samples (unconjugated AMB diluted tenfold prior to analysis) and the peak fractions collected previously from RPC were passed through a size exclusion column and eluted peaks were detected at 406 nm. Unconjugated AMB was eluted later compared to the AMB-PEG conjugate, implying that it has a smaller hydrodynamic volume compared to AMB-PEG in 20% ACN. The previously collected AMB-PEG conjugate and free AMB peak fractions had similar retention times as the AMB-PEG 2 formulation and unconjugated AMB samples respectively, thus verifying their respective peak identities. AMB-PEG 1 and 2 have identical elution profiles. (C) Size exclusion chromatogram of AMB-PEG and unconjugated AMB dispersed in PBS-EDTA. 3 μL of 2 mM AMB-PEG formulations that have been retained by 10 kDa centrifugal filters (Millipore) and 50 μL of the supernatant obtained from unconjugated AMB were analysed using a Superdex 75 size exclusion column and eluted peaks detected at 406 nm. In a PBS-EDTA mobile phase, unconjugated AMB has a shorter retention time of 20 minutes compared to AMB-PEG at 40 minutes, implying that AMB-PEG has a smaller hydrodynamic volume under these experimental conditions.

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: (A) Reverse phase chromatogram of AMB-PEG and unconjugated AMB, with eluted peaks detected at 406 nm. 50 μL of AMB-PEG 1 and 2, and 10 μL of unconjugated AMB dispersed in PBS-EDTA and 48% ACN respectively were injected into a C18 reverse phase column and eluted isocratically in a 48% ACN buffer at a flow rate of 0.5 ml/min for 40 minutes. Peaks were detected at 406 nm. The AMB-PEG conjugate has a shorter retention time, implying that it is more hydrophilic. From the AMB-PEG samples, AMB-PEG conjugate and free AMB (based on the retention time of unconjugated AMB) fractions were collected for further analysis via size exclusion chromatography. (B) Size exclusion chromatogram of AMB-PEG 2 and unconjugated AMB, as well as the relevant fractions collected from RPC, in a 20% ACN mobile phase. 20 mM of AMB-PEG 2 formulations and unconjugated AMB in DMSO were prepared and resuspended at 2 mM in a 20% ACN buffer. 50 μL of these samples (unconjugated AMB diluted tenfold prior to analysis) and the peak fractions collected previously from RPC were passed through a size exclusion column and eluted peaks were detected at 406 nm. Unconjugated AMB was eluted later compared to the AMB-PEG conjugate, implying that it has a smaller hydrodynamic volume compared to AMB-PEG in 20% ACN. The previously collected AMB-PEG conjugate and free AMB peak fractions had similar retention times as the AMB-PEG 2 formulation and unconjugated AMB samples respectively, thus verifying their respective peak identities. AMB-PEG 1 and 2 have identical elution profiles. (C) Size exclusion chromatogram of AMB-PEG and unconjugated AMB dispersed in PBS-EDTA. 3 μL of 2 mM AMB-PEG formulations that have been retained by 10 kDa centrifugal filters (Millipore) and 50 μL of the supernatant obtained from unconjugated AMB were analysed using a Superdex 75 size exclusion column and eluted peaks detected at 406 nm. In a PBS-EDTA mobile phase, unconjugated AMB has a shorter retention time of 20 minutes compared to AMB-PEG at 40 minutes, implying that AMB-PEG has a smaller hydrodynamic volume under these experimental conditions.

    Article Snippet: AMB-PEG Particle Size Determination Using DLS 2 mM solutions of AMB-PEG were prepared in PBS-EDTA, and diafiltration carried out with PBS-EDTA using 10 kDa centrifugal filters (Millipore).

    Techniques: Injection, Flow Cytometry, Size-exclusion Chromatography

    (A) AMB-PEG reaction scheme. The NHS ester on MS(PEG) 4 reacts with the primary amine (–NH2) group on AMB at a 1:1 molar ratio, generating conjugated AMB-PEG via amide bond formation. (B) Solubility of AMB-PEG at varying AMB:PEG molar ratios. AMB-PEG mixtures and unreacted AMB were prepared in DMSO, incubated for 2 hours and then (i) dispersed to a final concentration of 2 mM in PBS-EDTA, containing 10% DMSO by volume. (ii) The mixtures were then centrifuged to facilitate the observation of insoluble precipitates. Higher molar ratios yielded a suspension of yellow particles that precipitated upon centrifugation, similar to what was observed with unconjugated AMB.

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: (A) AMB-PEG reaction scheme. The NHS ester on MS(PEG) 4 reacts with the primary amine (–NH2) group on AMB at a 1:1 molar ratio, generating conjugated AMB-PEG via amide bond formation. (B) Solubility of AMB-PEG at varying AMB:PEG molar ratios. AMB-PEG mixtures and unreacted AMB were prepared in DMSO, incubated for 2 hours and then (i) dispersed to a final concentration of 2 mM in PBS-EDTA, containing 10% DMSO by volume. (ii) The mixtures were then centrifuged to facilitate the observation of insoluble precipitates. Higher molar ratios yielded a suspension of yellow particles that precipitated upon centrifugation, similar to what was observed with unconjugated AMB.

    Article Snippet: AMB-PEG Particle Size Determination Using DLS 2 mM solutions of AMB-PEG were prepared in PBS-EDTA, and diafiltration carried out with PBS-EDTA using 10 kDa centrifugal filters (Millipore).

    Techniques: Mass Spectrometry, Solubility, Incubation, Concentration Assay, Centrifugation

    Aqueous solubility of AMB-PEG 1 and 2. Increasing amounts of AMB-PEG formulations were added to PBS-EDTA, and post-centrifugation, the concentration of soluble AMB-PEG in the supernatants quantified based on their absorbance at 365 nm. Error bars denote the standard deviation between 3 independent formulations. Dotted line represents the theoretical condition where AMB formulation is completely soluble (i.e. concentration of total AMB = concentration of soluble AMB).

    Journal: PLoS ONE

    Article Title: Characterization of a Polyethylene Glycol-Amphotericin B Conjugate Loaded with Free AMB for Improved Antifungal Efficacy

    doi: 10.1371/journal.pone.0152112

    Figure Lengend Snippet: Aqueous solubility of AMB-PEG 1 and 2. Increasing amounts of AMB-PEG formulations were added to PBS-EDTA, and post-centrifugation, the concentration of soluble AMB-PEG in the supernatants quantified based on their absorbance at 365 nm. Error bars denote the standard deviation between 3 independent formulations. Dotted line represents the theoretical condition where AMB formulation is completely soluble (i.e. concentration of total AMB = concentration of soluble AMB).

    Article Snippet: AMB-PEG Particle Size Determination Using DLS 2 mM solutions of AMB-PEG were prepared in PBS-EDTA, and diafiltration carried out with PBS-EDTA using 10 kDa centrifugal filters (Millipore).

    Techniques: Solubility, Centrifugation, Concentration Assay, Standard Deviation

    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

    Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) induce Ca 2+ mobilization and phospholipase D (PLD) activation in type II alveolar epithelial cells. (a, c) A549 cells were labelled with 3 μ m Fluo-3/AM, treated or not with EDTA, EGTA

    Journal: Immunology

    Article Title: Natural lysophospholipids reduce Mycobacterium tuberculosis-induced cytotoxicity and induce anti-mycobacterial activity by a phagolysosome maturation-dependent mechanism in A549 type II alveolar epithelial cells

    doi: 10.1111/j.1365-2567.2009.03145.x

    Figure Lengend Snippet: Lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P) induce Ca 2+ mobilization and phospholipase D (PLD) activation in type II alveolar epithelial cells. (a, c) A549 cells were labelled with 3 μ m Fluo-3/AM, treated or not with EDTA, EGTA

    Article Snippet: In several experiments, 2 m m EDTA or 3 m m EGTA (Calbiochem) were added 15 min before the addition of LPA or S1P, whereas 20 μ m 1,2-bis(2-aminophenoxy)ethane-N,N,N1,N1-tetraacetic acid tetraicis (acetoxymethyl ester) (BAPTA-AM) (Sigma-Aldrich, Milan, Italy) was added 30 min before stimulation with LPA or S1P.

    Techniques: Activation Assay

    Binding of Wt1 protein to the 5′-flanking region of the Adamts16 gene. ChIP was performed to detect Wt1 protein bound to the 5′-flanking region of the Adamts16 gene in its native chromosomal configuration. The drawing ( A ) delineates the three predicted Wt1 binding sites ( Wt1-A , Wt1-B , and Wt1-C ) in the promoter and 5′-UTR of the Adamts16 gene and allocates the PCR primers used for DNA amplification. Specific antibodies against Wt1 and histone proteins were chosen for immunoprecipitation of M15 whole cell lysates. Amplicons encompassing the 5′-flanking region of the Adamts16 gene were enriched ∼2.5-fold with the use of anti-Wt1 antibody compared with normal rabbit IgG (NRb-IgG). No differences in actin DNA were observed between anti-Wt1 antibody and normal rabbit IgG ( B ). The gene encoding anti-Müllerian hormone receptor 2 ( Amhr2 ), served as a positive control ( B ). Binding of Wt1(−KTS) protein to the Adamts16 promoter was confirmed in stimulated UB27 cells ( C ). Wt1(+KTS) protein failed to interact with the promoter of the Adamts16 gene in UD28 cells ( D ). Data shown are means ± S.E. ( error bars ). Statistical significances are indicated by asterisks (*, p

    Journal: The Journal of Biological Chemistry

    Article Title: Transcriptional Regulation by the Wilms Tumor Protein, Wt1, Suggests a Role of the Metalloproteinase Adamts16 in Murine Genitourinary Development *

    doi: 10.1074/jbc.M113.464644

    Figure Lengend Snippet: Binding of Wt1 protein to the 5′-flanking region of the Adamts16 gene. ChIP was performed to detect Wt1 protein bound to the 5′-flanking region of the Adamts16 gene in its native chromosomal configuration. The drawing ( A ) delineates the three predicted Wt1 binding sites ( Wt1-A , Wt1-B , and Wt1-C ) in the promoter and 5′-UTR of the Adamts16 gene and allocates the PCR primers used for DNA amplification. Specific antibodies against Wt1 and histone proteins were chosen for immunoprecipitation of M15 whole cell lysates. Amplicons encompassing the 5′-flanking region of the Adamts16 gene were enriched ∼2.5-fold with the use of anti-Wt1 antibody compared with normal rabbit IgG (NRb-IgG). No differences in actin DNA were observed between anti-Wt1 antibody and normal rabbit IgG ( B ). The gene encoding anti-Müllerian hormone receptor 2 ( Amhr2 ), served as a positive control ( B ). Binding of Wt1(−KTS) protein to the Adamts16 promoter was confirmed in stimulated UB27 cells ( C ). Wt1(+KTS) protein failed to interact with the promoter of the Adamts16 gene in UD28 cells ( D ). Data shown are means ± S.E. ( error bars ). Statistical significances are indicated by asterisks (*, p

    Article Snippet: The supernatants were diluted in immunoprecipitation buffer (0.01% SDS, 1.1% Triton X-100, 1.2 m m EDTA, 16.7 m m Tris-HCl, pH 8.1) and precleared for 1 h at 4 °C with DNA-blocked protein G-agarose (Millipore).

    Techniques: Binding Assay, Chromatin Immunoprecipitation, Polymerase Chain Reaction, Amplification, Immunoprecipitation, Positive Control