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Millipore ferrozine
Ferrozine, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1425 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ferrozine/product/Millipore
Average 95 stars, based on 1425 article reviews
Price from $9.99 to $1999.99
ferrozine - by Bioz Stars, 2020-04
95/100 stars

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Clone Assay:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The cyc-2.1 (NCBI accession ) or cyc-2.2 (NCBI accession ) genes were cloned into the pET-20b(+) plasmid (AmpR , Novagen) following the pelB leader sequence for periplasmic protein localization.

Incubation:

Article Title: Human mitochondrial transcriptional factor A breaks the mitochondria-mediated vicious cycle in Alzheimer’s disease
Article Snippet: .. Histochemical detection of mitochondrial cytochrome c oxidase activity For detection of mitochondrial cytochrome c oxidase activity in frozen sections, brain sections (100 μm thick) were incubated for 2.5 h at 37 °C in a solution containing cytochrome c (0.5 mg/mL, Sigma-Aldrich, C2506) and DAB (0.5 mg/mL, K-4100, Vector Laboratories Inc., Burlingame, CA, USA), and sucrose (40 mg/mL) in PBS. ..

Activity Assay:

Article Title: Human mitochondrial transcriptional factor A breaks the mitochondria-mediated vicious cycle in Alzheimer’s disease
Article Snippet: .. Histochemical detection of mitochondrial cytochrome c oxidase activity For detection of mitochondrial cytochrome c oxidase activity in frozen sections, brain sections (100 μm thick) were incubated for 2.5 h at 37 °C in a solution containing cytochrome c (0.5 mg/mL, Sigma-Aldrich, C2506) and DAB (0.5 mg/mL, K-4100, Vector Laboratories Inc., Burlingame, CA, USA), and sucrose (40 mg/mL) in PBS. ..

Article Title: Differential Regulation of Smac/DIABLO and Hsp-70 during Brain Maturation
Article Snippet: Briefly, 50 µg of cell-free extracts of mouse brain at different stages of maturation were activated with 10 µM horse heart cyt c (Sigma, #C7752) and 1 mM dATP (Invitrogen, #10216-018) at 37°C for 60 min. Control samples in the absence of cyt c and dATP were run under the same conditions. .. The residual activity was continuously monitored for 30 min at 37°C in a thermostated Molecular Devices SpectraMax Gemini spectrofluorimeter, at excitation and emission wavelengths of 405 and 510 nm, respectively.

Article Title: Cardiomyopathy-associated mutation in the ADP/ATP carrier reveals translation-dependent regulation of cytochrome c oxidase activity
Article Snippet: Paragraph title: Spectrophotometric activity assay ... Briefly, 5 µg of mitochondria solubilized in 0.5% (wt/vol) n -dodecyl β- d -maltoside (Anatrace) and spiked with protease inhibitors was added to reaction buffer (50 mM KPi, 2 mM EDTA, pH 7.4) with 0.08% (wt/vol) equine heart cytochrome c (Sigma).

Article Title: Superoxide Anion Production and Bioenergetic Profile in Young and Elderly Human Primary Myoblasts
Article Snippet: Superoxide dismutase (SOD) activity was determined using the modified method of L'Abbé and Fischer [ , ]. .. The final assay volume (1 ml) contained 20 mM Na2 CO3 , pH 10, 10 mM cytochrome c (number C7752, Sigma Aldrich), and 1 mM xanthine (number X0626, Sigma-Aldrich) and xanthine oxidase (number X4500, Sigma-Aldrich).

Expressing:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: Paragraph title: Protein Expression and Purification ... Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described.

Modification:

Article Title: Superoxide Anion Production and Bioenergetic Profile in Young and Elderly Human Primary Myoblasts
Article Snippet: Superoxide dismutase (SOD) activity was determined using the modified method of L'Abbé and Fischer [ , ]. .. The final assay volume (1 ml) contained 20 mM Na2 CO3 , pH 10, 10 mM cytochrome c (number C7752, Sigma Aldrich), and 1 mM xanthine (number X0626, Sigma-Aldrich) and xanthine oxidase (number X4500, Sigma-Aldrich).

Electron Microscopy:

Article Title: Understanding the Impact of Extracellular Polymeric Substances on Lead Release in Drinking Water Systems
Article Snippet: Scanning electron microscopy images from previous studies , show that the corrosion scales on lead service lines are often porous, especially when a phosphate corrosion inhibitor is applied. .. Within each group, three different sEPS conditions were examined: 100 mg/L alginate + 100 mg/L BSA (labeled sEPS1); 200 mg/L alginate + 200 mg/L BSA (labeled sEPS2); and 100 mg/L alginate + 100 mg/L BSA + 123.84 mg/L cytochrome c (C7752, Sigma-Aldrich) (labeled Cyto. c).

Flow Cytometry:

Article Title: Spectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation
Article Snippet: Both myoglobin (Sigma Aldrich M1882, ≥90%) and ferric cytochrome c (Sigma Aldrich 30396, ≥90%) from equine heart were used without further purification. .. Oxymyoglobin solution was prepared by bubbling a steady flow of 100% O2 gas at 5 ml min−1 through the deoxymyoglobin solution for 30 min.

Concentration Assay:

Article Title: Differential Regulation of Smac/DIABLO and Hsp-70 during Brain Maturation
Article Snippet: Briefly, 50 µg of cell-free extracts of mouse brain at different stages of maturation were activated with 10 µM horse heart cyt c (Sigma, #C7752) and 1 mM dATP (Invitrogen, #10216-018) at 37°C for 60 min. Control samples in the absence of cyt c and dATP were run under the same conditions. .. About 20 µl samples were loaded in a 96-well microplate and the reaction started by addition of 80 µl of substrate Acetyl-Asp-Glu-Val-Asp-7-amino-4-trifluoromethylcoumarin (Ac-DEVD-AFC) (Ana-spec, #25273) dissolved in caspase buffer (100 µM final concentration).

Article Title: Understanding the Impact of Extracellular Polymeric Substances on Lead Release in Drinking Water Systems
Article Snippet: Within each group, three different sEPS conditions were examined: 100 mg/L alginate + 100 mg/L BSA (labeled sEPS1); 200 mg/L alginate + 200 mg/L BSA (labeled sEPS2); and 100 mg/L alginate + 100 mg/L BSA + 123.84 mg/L cytochrome c (C7752, Sigma-Aldrich) (labeled Cyto. c). .. Since heavy-metal-resistant microorganisms mostly inhabit copper and lead pipelines, , , the lower end of a commonly studied EPS concentration range (a few hundreds to 10 000 mg/L) , , was selected.

Article Title: Biomolecular Clusters Distribution up to Mega Dalton Region Using MALDI-Quadrupole Ion Trap Mass Spectrometer
Article Snippet: In the present study, cytochrome c (C2506, Sigma-Aldrich Co., St. Louis, MO, USA) and BSA (A0281, Sigma-Aldrich Co., St. Louis, MO, USA) were employed for obtaining the cluster size distributions. .. SA was dissolved in a 50:50 water/acetonitrile solution at a concentration of 10 mg/mL.

other:

Article Title: Improved Protein Surface Mapping Using Diethylpyrocarbonate with Mass Spectrometric Detection
Article Snippet: Diethylpyrocarbonate (DEPC), imidazole, dithiothreitol (DTT), copper(II) sulfate (CuSO4 ), 3-morpholinopropanesulfonic acid (MOPS), potassium acetate, equine heart cytochrome c, and equine skeletal muscle myoglobin were obtained from Sigma-Aldrich (St. Louis, MO).

Imaging:

Article Title: Human mitochondrial transcriptional factor A breaks the mitochondria-mediated vicious cycle in Alzheimer’s disease
Article Snippet: Histochemical detection of mitochondrial cytochrome c oxidase activity For detection of mitochondrial cytochrome c oxidase activity in frozen sections, brain sections (100 μm thick) were incubated for 2.5 h at 37 °C in a solution containing cytochrome c (0.5 mg/mL, Sigma-Aldrich, C2506) and DAB (0.5 mg/mL, K-4100, Vector Laboratories Inc., Burlingame, CA, USA), and sucrose (40 mg/mL) in PBS. .. Digital images were acquired using an Axioskop2 Plus microscope, equipped with an AxioCam CCD camera and Axiovision 3.1 imaging software (Carl Zeiss MicroImaging, Tokyo, Japan).

Article Title: Spectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation
Article Snippet: Paragraph title: 2.2. Cell perfusion and bright-field imaging ... Both myoglobin (Sigma Aldrich M1882, ≥90%) and ferric cytochrome c (Sigma Aldrich 30396, ≥90%) from equine heart were used without further purification.

Protein Concentration:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The Soret band extinction coefficient (ε410 = 106,100 M−1 cm−1 ) was used to determine the protein concentration of HRC solutions.

Sequencing:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The cyc-2.1 (NCBI accession ) or cyc-2.2 (NCBI accession ) genes were cloned into the pET-20b(+) plasmid (AmpR , Novagen) following the pelB leader sequence for periplasmic protein localization.

Recombinant:

Article Title: Cytochrome c is an oxidative stress–activated plasmalogenase that cleaves plasmenylcholine and plasmenylethanolamine at the sn-1 vinyl ether linkage
Article Snippet: Equine cytochrome c (catalog number C7752) purified utilizing acetic acid according to the method of Hagihara et al. ( ) and catalase (catalog number C40) from bovine liver (used without further purification) were obtained from Sigma-Aldrich. .. Recombinant bovine endothelial nitric-oxide synthase (catalog number 60880) was purchased from Cayman Chemical.

Ion Exchange Chromatography:

Article Title: Astacin Family Metallopeptidases and Serine Peptidase Inhibitors in Spider Digestive Fluid
Article Snippet: The fractionation of SDF was evaluated by size-exclusion chromatography, ion-exchange chromatography followed by size-exclusion chromatography, and sucrose density gradient centrifugation. .. Size-exclusion columns were calibrated with various combinations of blue dextran (Sigma-Aldrich D4772, St. Louis MO, USA; MW 2,000 kDa), bovine serum albumin (Sigma A8531; 66 kDa), carbonic anhydrase (Sigma C7025; 29 kDa), cytochrome C (Sigma C7150; 12.4 kDa), and vitamin B12 (Sigma V2876; 1.355 kDa), run separately from SDF components.,

Fluorescence:

Article Title: Spectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation
Article Snippet: Fluorescence background was subtracted from Raman spectra using a polynomial-fitting algorithm in O rigin 9.1 software (OriginLab Corp.). .. Both myoglobin (Sigma Aldrich M1882, ≥90%) and ferric cytochrome c (Sigma Aldrich 30396, ≥90%) from equine heart were used without further purification.

Isolation:

Article Title: Neutrophils exhibit distinct phenotypes toward chitosans with different degrees of deacetylation: implications for cartilage repair
Article Snippet: Ficoll-Paque and dextran used for the isolation of PMN were obtained from Pharmacia (Kirkland, Québec, Canada) and fetal bovine serum (FBS) as well as RPMI 1640 were purchased from Wisent (St-Bruno, Québec, Canada). .. Cytochrome c equine heart and pyrrolidine-1 were purchased from Calbiochem (Gibbstown, New Jersey, USA).

Size-exclusion Chromatography:

Article Title: Astacin Family Metallopeptidases and Serine Peptidase Inhibitors in Spider Digestive Fluid
Article Snippet: The fractionation of SDF was evaluated by size-exclusion chromatography, ion-exchange chromatography followed by size-exclusion chromatography, and sucrose density gradient centrifugation. .. Size-exclusion columns were calibrated with various combinations of blue dextran (Sigma-Aldrich D4772, St. Louis MO, USA; MW 2,000 kDa), bovine serum albumin (Sigma A8531; 66 kDa), carbonic anhydrase (Sigma C7025; 29 kDa), cytochrome C (Sigma C7150; 12.4 kDa), and vitamin B12 (Sigma V2876; 1.355 kDa), run separately from SDF components.,

Microscopy:

Article Title: Human mitochondrial transcriptional factor A breaks the mitochondria-mediated vicious cycle in Alzheimer’s disease
Article Snippet: Histochemical detection of mitochondrial cytochrome c oxidase activity For detection of mitochondrial cytochrome c oxidase activity in frozen sections, brain sections (100 μm thick) were incubated for 2.5 h at 37 °C in a solution containing cytochrome c (0.5 mg/mL, Sigma-Aldrich, C2506) and DAB (0.5 mg/mL, K-4100, Vector Laboratories Inc., Burlingame, CA, USA), and sucrose (40 mg/mL) in PBS. .. Digital images were acquired using an Axioskop2 Plus microscope, equipped with an AxioCam CCD camera and Axiovision 3.1 imaging software (Carl Zeiss MicroImaging, Tokyo, Japan).

Purification:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: .. Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The Soret band extinction coefficient (ε410 = 106,100 M−1 cm−1 ) was used to determine the protein concentration of HRC solutions.

Article Title: Cytochrome c is an oxidative stress–activated plasmalogenase that cleaves plasmenylcholine and plasmenylethanolamine at the sn-1 vinyl ether linkage
Article Snippet: .. Equine cytochrome c (catalog number C7752) purified utilizing acetic acid according to the method of Hagihara et al. ( ) and catalase (catalog number C40) from bovine liver (used without further purification) were obtained from Sigma-Aldrich. .. Recombinant bovine endothelial nitric-oxide synthase (catalog number 60880) was purchased from Cayman Chemical.

Article Title: Hydration-State Change of Horse Heart Cytochrome c Corresponding to Trifluoroacetic-Acid-Induced Unfolding
Article Snippet: Horse-heart cyt c (C2506) was purchased from Sigma (St. Louis, MO), with manufacturer-guaranteed purity of > 95%. .. Other chemicals were of reagent grade and used without further purification.

Article Title: Neutrophils exhibit distinct phenotypes toward chitosans with different degrees of deacetylation: implications for cartilage repair
Article Snippet: Migration was assessed using the ChemoTx system from Neuroprobe (Gaithersburg, MD, USA) and the purified myeloperoxidase (MPO), O -dianisidine dihydrochloride, hydrogen peroxide, and cytochalasin B used in the MPO assay were obtained from Sigma-Aldrich (Oakville, Ontario, Canada). .. Cytochrome c equine heart and pyrrolidine-1 were purchased from Calbiochem (Gibbstown, New Jersey, USA).

Article Title: Spectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation
Article Snippet: .. Both myoglobin (Sigma Aldrich M1882, ≥90%) and ferric cytochrome c (Sigma Aldrich 30396, ≥90%) from equine heart were used without further purification. ..

Labeling:

Article Title: Understanding the Impact of Extracellular Polymeric Substances on Lead Release in Drinking Water Systems
Article Snippet: .. Within each group, three different sEPS conditions were examined: 100 mg/L alginate + 100 mg/L BSA (labeled sEPS1); 200 mg/L alginate + 200 mg/L BSA (labeled sEPS2); and 100 mg/L alginate + 100 mg/L BSA + 123.84 mg/L cytochrome c (C7752, Sigma-Aldrich) (labeled Cyto. c). ..

Article Title: Subtle Change in the Charge Distribution of Surface Residues May Affect the Secondary Functions of Cytochrome c *
Article Snippet: The two proteins, namely h-cyt c (catalog No. C7752-100MG) and y-cyt c (catalog No. C2436-100MG), and CDL disodium salt from bovine heart (catalog No. 21979-25-MG-F) were purchased from Sigma. .. All other reagents used were of the highest purity. y-cyt c contains one free cysteine (Cys-102), which was labeled with TMR using published procedures ( ). h-cyt c was labeled at the N-terminal using the succinimidyl ester derivative of TMR ( ).

Plasmid Preparation:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The cyc-2.1 (NCBI accession ) or cyc-2.2 (NCBI accession ) genes were cloned into the pET-20b(+) plasmid (AmpR , Novagen) following the pelB leader sequence for periplasmic protein localization.

Software:

Article Title: Human mitochondrial transcriptional factor A breaks the mitochondria-mediated vicious cycle in Alzheimer’s disease
Article Snippet: Histochemical detection of mitochondrial cytochrome c oxidase activity For detection of mitochondrial cytochrome c oxidase activity in frozen sections, brain sections (100 μm thick) were incubated for 2.5 h at 37 °C in a solution containing cytochrome c (0.5 mg/mL, Sigma-Aldrich, C2506) and DAB (0.5 mg/mL, K-4100, Vector Laboratories Inc., Burlingame, CA, USA), and sucrose (40 mg/mL) in PBS. .. Digital images were acquired using an Axioskop2 Plus microscope, equipped with an AxioCam CCD camera and Axiovision 3.1 imaging software (Carl Zeiss MicroImaging, Tokyo, Japan).

Article Title: Spectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation
Article Snippet: Fluorescence background was subtracted from Raman spectra using a polynomial-fitting algorithm in O rigin 9.1 software (OriginLab Corp.). .. Both myoglobin (Sigma Aldrich M1882, ≥90%) and ferric cytochrome c (Sigma Aldrich 30396, ≥90%) from equine heart were used without further purification.

Positron Emission Tomography:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The cyc-2.1 (NCBI accession ) or cyc-2.2 (NCBI accession ) genes were cloned into the pET-20b(+) plasmid (AmpR , Novagen) following the pelB leader sequence for periplasmic protein localization.

Sample Prep:

Article Title: Biomolecular Clusters Distribution up to Mega Dalton Region Using MALDI-Quadrupole Ion Trap Mass Spectrometer
Article Snippet: Paragraph title: 3.2. Sample Preparation ... In the present study, cytochrome c (C2506, Sigma-Aldrich Co., St. Louis, MO, USA) and BSA (A0281, Sigma-Aldrich Co., St. Louis, MO, USA) were employed for obtaining the cluster size distributions.

MPO Assay:

Article Title: Neutrophils exhibit distinct phenotypes toward chitosans with different degrees of deacetylation: implications for cartilage repair
Article Snippet: Migration was assessed using the ChemoTx system from Neuroprobe (Gaithersburg, MD, USA) and the purified myeloperoxidase (MPO), O -dianisidine dihydrochloride, hydrogen peroxide, and cytochalasin B used in the MPO assay were obtained from Sigma-Aldrich (Oakville, Ontario, Canada). .. Cytochrome c equine heart and pyrrolidine-1 were purchased from Calbiochem (Gibbstown, New Jersey, USA).

Produced:

Article Title: Spectroscopic analysis of myoglobin and cytochrome c dynamics in isolated cardiomyocytes during hypoxia and reoxygenation
Article Snippet: Both myoglobin (Sigma Aldrich M1882, ≥90%) and ferric cytochrome c (Sigma Aldrich 30396, ≥90%) from equine heart were used without further purification. .. Addition of sodium dithionite to the stock solution under 100% nitrogen gas for 5 min produced a solution of deoxymyoglobin.

Activation Assay:

Article Title: Differential Regulation of Smac/DIABLO and Hsp-70 during Brain Maturation
Article Snippet: Paragraph title: Kinetics of Activation ... Briefly, 50 µg of cell-free extracts of mouse brain at different stages of maturation were activated with 10 µM horse heart cyt c (Sigma, #C7752) and 1 mM dATP (Invitrogen, #10216-018) at 37°C for 60 min. Control samples in the absence of cyt c and dATP were run under the same conditions.

Fractionation:

Article Title: Astacin Family Metallopeptidases and Serine Peptidase Inhibitors in Spider Digestive Fluid
Article Snippet: Paragraph title: 2.2. Fractionation of SDF: Peptidases ... Size-exclusion columns were calibrated with various combinations of blue dextran (Sigma-Aldrich D4772, St. Louis MO, USA; MW 2,000 kDa), bovine serum albumin (Sigma A8531; 66 kDa), carbonic anhydrase (Sigma C7025; 29 kDa), cytochrome C (Sigma C7150; 12.4 kDa), and vitamin B12 (Sigma V2876; 1.355 kDa), run separately from SDF components.,

Migration:

Article Title: Neutrophils exhibit distinct phenotypes toward chitosans with different degrees of deacetylation: implications for cartilage repair
Article Snippet: Migration was assessed using the ChemoTx system from Neuroprobe (Gaithersburg, MD, USA) and the purified myeloperoxidase (MPO), O -dianisidine dihydrochloride, hydrogen peroxide, and cytochalasin B used in the MPO assay were obtained from Sigma-Aldrich (Oakville, Ontario, Canada). .. Cytochrome c equine heart and pyrrolidine-1 were purchased from Calbiochem (Gibbstown, New Jersey, USA).

Gradient Centrifugation:

Article Title: Astacin Family Metallopeptidases and Serine Peptidase Inhibitors in Spider Digestive Fluid
Article Snippet: The fractionation of SDF was evaluated by size-exclusion chromatography, ion-exchange chromatography followed by size-exclusion chromatography, and sucrose density gradient centrifugation. .. Size-exclusion columns were calibrated with various combinations of blue dextran (Sigma-Aldrich D4772, St. Louis MO, USA; MW 2,000 kDa), bovine serum albumin (Sigma A8531; 66 kDa), carbonic anhydrase (Sigma C7025; 29 kDa), cytochrome C (Sigma C7150; 12.4 kDa), and vitamin B12 (Sigma V2876; 1.355 kDa), run separately from SDF components.,

Fast Protein Liquid Chromatography:

Article Title: Recombinant Expression, Biophysical Characterization, and Cardiolipin-Induced Changes of Two Caenorhabditis elegans Cytochrome c Proteins
Article Snippet: .. Horse heart cyt c (HRC, Sigma C2506) was dissolved in a 10 mM sodium phosphate buffer at pH 7.0, oxidized by the addition of solid potassium ferricyanide, and purified on a HiTrapTM SP HP cation exchange column (GE Healthcare) connected to an ÄKTA purifier fast protein liquid chromatography (FPLC) system as described. .. The Soret band extinction coefficient (ε410 = 106,100 M−1 cm−1 ) was used to determine the protein concentration of HRC solutions.

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  • 96
    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
    https://www.bioz.com/result/pbs edta/product/Millipore
    Average 96 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    pbs edta - by Bioz Stars, 2020-04
    96/100 stars
      Buy from Supplier

    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
    https://www.bioz.com/result/nmr buffer/product/Millipore
    Average 95 stars, based on 106 article reviews
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    nmr buffer - by Bioz Stars, 2020-04
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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
    https://www.bioz.com/result/m edta/product/Millipore
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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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    Image Search Results


    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