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Merck KGaA ethylene glycol tetraacetic acid egta
Ethylene Glycol Tetraacetic Acid Egta, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ethylene glycol tetraacetic acid egta/product/Merck KGaA
Average 92 stars, based on 2 article reviews
Price from $9.99 to $1999.99
ethylene glycol tetraacetic acid egta - by Bioz Stars, 2020-07
92/100 stars

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Article Snippet: .. Following low-spin centrifugation, the pellet was resuspended in ice-cold buffer (pH 7.0), containing 1 mmol/l ethylene glycol tetraacetic acid (EGTA), 150 mmol/l sucrose and protease inhibitor cocktail (Merck Millipore). ..

Centrifugation:

Article Title: Pioglitazone restores the homocysteine-impaired function of endothelial progenitor cells via the inhibition of the protein kinase C/NADPH oxidase pathway
Article Snippet: .. Following low-spin centrifugation, the pellet was resuspended in ice-cold buffer (pH 7.0), containing 1 mmol/l ethylene glycol tetraacetic acid (EGTA), 150 mmol/l sucrose and protease inhibitor cocktail (Merck Millipore). ..

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    Merck KGaA egta
    Purification of recombinant human non-muscle actins and fission yeast Act1. (A) CBB gel image showing purified recombinant human β-actin (Actb), human γ-actin (Actg1) and Schizosaccharomyces pombe (SpAct1) actin. Immunoblotting in the bottom panels was performed with antibodies against Actb or Actg1 raised against peptides corresponding to the N-terminus of human β- and γ-actins. Since the N-terminus of S. pombe Act1 has strong similarity to human γ-actin, the anti-Actg1 antibody can recognize S. pombe Act1 as well as γ-actin (see sequence alignment shown at the bottom). (B) Actin sedimentation assays. Purified actin in low-ionic strength buffer (G-buffer) was mixed with <t>KCl,</t> <t>EGTA</t> and Mg 2+ to induce actin polymerization. Actin sedimentation was tested in the presence of 0.5 mM LatA or in solvent control (DMSO) and in the absence of DMSO or Latrunculin A (‘−’). After ultracentrifugation, actin in the pellet (Pellet) and supernatant (Sup) fractions were detected by CBB staining following SDS-PAGE. Rabbit muscle actin was used as a positive control. (C) Visualization of F-actin. The specified actins were incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG. F-actin in all cases was then stained with Rhodamine–phalloidin and imaged by using a Nikon inverted microscope fitted with a Yokogawa spinning-disc head and an Andor iXon camera. Scale bars: 5 µm.
    Egta, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 93/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/egta/product/Merck KGaA
    Average 93 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    egta - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    93
    Merck KGaA m egta am
    Purification of recombinant human non-muscle actins and fission yeast Act1. (A) CBB gel image showing purified recombinant human β-actin (Actb), human γ-actin (Actg1) and Schizosaccharomyces pombe (SpAct1) actin. Immunoblotting in the bottom panels was performed with antibodies against Actb or Actg1 raised against peptides corresponding to the N-terminus of human β- and γ-actins. Since the N-terminus of S. pombe Act1 has strong similarity to human γ-actin, the anti-Actg1 antibody can recognize S. pombe Act1 as well as γ-actin (see sequence alignment shown at the bottom). (B) Actin sedimentation assays. Purified actin in low-ionic strength buffer (G-buffer) was mixed with <t>KCl,</t> <t>EGTA</t> and Mg 2+ to induce actin polymerization. Actin sedimentation was tested in the presence of 0.5 mM LatA or in solvent control (DMSO) and in the absence of DMSO or Latrunculin A (‘−’). After ultracentrifugation, actin in the pellet (Pellet) and supernatant (Sup) fractions were detected by CBB staining following SDS-PAGE. Rabbit muscle actin was used as a positive control. (C) Visualization of F-actin. The specified actins were incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG. F-actin in all cases was then stained with Rhodamine–phalloidin and imaged by using a Nikon inverted microscope fitted with a Yokogawa spinning-disc head and an Andor iXon camera. Scale bars: 5 µm.
    M Egta Am, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m egta am/product/Merck KGaA
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    m egta am - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    92
    Merck KGaA lysis buffer
    Purification of recombinant human non-muscle actins and fission yeast Act1. (A) CBB gel image showing purified recombinant human β-actin (Actb), human γ-actin (Actg1) and Schizosaccharomyces pombe (SpAct1) actin. Immunoblotting in the bottom panels was performed with antibodies against Actb or Actg1 raised against peptides corresponding to the N-terminus of human β- and γ-actins. Since the N-terminus of S. pombe Act1 has strong similarity to human γ-actin, the anti-Actg1 antibody can recognize S. pombe Act1 as well as γ-actin (see sequence alignment shown at the bottom). (B) Actin sedimentation assays. Purified actin in low-ionic strength buffer (G-buffer) was mixed with <t>KCl,</t> <t>EGTA</t> and Mg 2+ to induce actin polymerization. Actin sedimentation was tested in the presence of 0.5 mM LatA or in solvent control (DMSO) and in the absence of DMSO or Latrunculin A (‘−’). After ultracentrifugation, actin in the pellet (Pellet) and supernatant (Sup) fractions were detected by CBB staining following SDS-PAGE. Rabbit muscle actin was used as a positive control. (C) Visualization of F-actin. The specified actins were incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG. F-actin in all cases was then stained with Rhodamine–phalloidin and imaged by using a Nikon inverted microscope fitted with a Yokogawa spinning-disc head and an Andor iXon camera. Scale bars: 5 µm.
    Lysis Buffer, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 188 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lysis buffer/product/Merck KGaA
    Average 92 stars, based on 188 article reviews
    Price from $9.99 to $1999.99
    lysis buffer - by Bioz Stars, 2020-07
    92/100 stars
      Buy from Supplier

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    Purification of recombinant human non-muscle actins and fission yeast Act1. (A) CBB gel image showing purified recombinant human β-actin (Actb), human γ-actin (Actg1) and Schizosaccharomyces pombe (SpAct1) actin. Immunoblotting in the bottom panels was performed with antibodies against Actb or Actg1 raised against peptides corresponding to the N-terminus of human β- and γ-actins. Since the N-terminus of S. pombe Act1 has strong similarity to human γ-actin, the anti-Actg1 antibody can recognize S. pombe Act1 as well as γ-actin (see sequence alignment shown at the bottom). (B) Actin sedimentation assays. Purified actin in low-ionic strength buffer (G-buffer) was mixed with KCl, EGTA and Mg 2+ to induce actin polymerization. Actin sedimentation was tested in the presence of 0.5 mM LatA or in solvent control (DMSO) and in the absence of DMSO or Latrunculin A (‘−’). After ultracentrifugation, actin in the pellet (Pellet) and supernatant (Sup) fractions were detected by CBB staining following SDS-PAGE. Rabbit muscle actin was used as a positive control. (C) Visualization of F-actin. The specified actins were incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG. F-actin in all cases was then stained with Rhodamine–phalloidin and imaged by using a Nikon inverted microscope fitted with a Yokogawa spinning-disc head and an Andor iXon camera. Scale bars: 5 µm.

    Journal: Journal of Cell Science

    Article Title: Rapid production of pure recombinant actin isoforms in Pichia pastoris

    doi: 10.1242/jcs.213827

    Figure Lengend Snippet: Purification of recombinant human non-muscle actins and fission yeast Act1. (A) CBB gel image showing purified recombinant human β-actin (Actb), human γ-actin (Actg1) and Schizosaccharomyces pombe (SpAct1) actin. Immunoblotting in the bottom panels was performed with antibodies against Actb or Actg1 raised against peptides corresponding to the N-terminus of human β- and γ-actins. Since the N-terminus of S. pombe Act1 has strong similarity to human γ-actin, the anti-Actg1 antibody can recognize S. pombe Act1 as well as γ-actin (see sequence alignment shown at the bottom). (B) Actin sedimentation assays. Purified actin in low-ionic strength buffer (G-buffer) was mixed with KCl, EGTA and Mg 2+ to induce actin polymerization. Actin sedimentation was tested in the presence of 0.5 mM LatA or in solvent control (DMSO) and in the absence of DMSO or Latrunculin A (‘−’). After ultracentrifugation, actin in the pellet (Pellet) and supernatant (Sup) fractions were detected by CBB staining following SDS-PAGE. Rabbit muscle actin was used as a positive control. (C) Visualization of F-actin. The specified actins were incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG. F-actin in all cases was then stained with Rhodamine–phalloidin and imaged by using a Nikon inverted microscope fitted with a Yokogawa spinning-disc head and an Andor iXon camera. Scale bars: 5 µm.

    Article Snippet: For imaging actin filaments, actin (8.33 µM) in G-buffer was polymerized by addition of 2 mM MgCl2 , 5 mM EGTA, 100 mM KCl and 2% polyethylene glycol 20,000 (#8.17018.1000, Merck Millipore) followed by incubation at 24°C for 1 h. 5% (v/v) Rhodamine–phalloidin (#R415, Thermo Fisher Scientific) or phalloidin–CF633 (#00046, Biotium) was added, and F-actin was imaged using an Andor Revolution XD spinning-disc confocal system on a Nikon Eclipse Ti inverted microscope, with a Nikon Plan Apo Lambda 100×1.45 NA oil immersion objective lens, a spinning-disc system (CSU-X1; Yokogawa) and an Andor iXon Ultra EMCCD camera.

    Techniques: Purification, Recombinant, Sequencing, Sedimentation, Staining, SDS Page, Positive Control, Incubation, Inverted Microscopy

    Purification of arginylated β-actin. (A) Schematic representation of expression of arginylated β-actin (R-Actb). (B) Immunoblotting and CBB staining showing purified R-Actb. Immunoblotting was performed with polyclonal antibodies against arginylated β-actin. (C) Representative mass spectra of the unique N-terminal tryptic peptide of β-actin, γ-actin and arginylated β-actin [(R) β-actin] as obtained after HCD fragmentation. The N-terminal (R) β-actin tryptic unique peptide shows the replacement of Met-Asp by Arg. (D) Visualization of arginylated actin (R-Actb) filament. R-Actb was incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG and stained with Cy5–phalloidin. Scale bar: 5 µm.

    Journal: Journal of Cell Science

    Article Title: Rapid production of pure recombinant actin isoforms in Pichia pastoris

    doi: 10.1242/jcs.213827

    Figure Lengend Snippet: Purification of arginylated β-actin. (A) Schematic representation of expression of arginylated β-actin (R-Actb). (B) Immunoblotting and CBB staining showing purified R-Actb. Immunoblotting was performed with polyclonal antibodies against arginylated β-actin. (C) Representative mass spectra of the unique N-terminal tryptic peptide of β-actin, γ-actin and arginylated β-actin [(R) β-actin] as obtained after HCD fragmentation. The N-terminal (R) β-actin tryptic unique peptide shows the replacement of Met-Asp by Arg. (D) Visualization of arginylated actin (R-Actb) filament. R-Actb was incubated with KCl, EGTA and Mg 2+ in the presence of 2% PEG and stained with Cy5–phalloidin. Scale bar: 5 µm.

    Article Snippet: For imaging actin filaments, actin (8.33 µM) in G-buffer was polymerized by addition of 2 mM MgCl2 , 5 mM EGTA, 100 mM KCl and 2% polyethylene glycol 20,000 (#8.17018.1000, Merck Millipore) followed by incubation at 24°C for 1 h. 5% (v/v) Rhodamine–phalloidin (#R415, Thermo Fisher Scientific) or phalloidin–CF633 (#00046, Biotium) was added, and F-actin was imaged using an Andor Revolution XD spinning-disc confocal system on a Nikon Eclipse Ti inverted microscope, with a Nikon Plan Apo Lambda 100×1.45 NA oil immersion objective lens, a spinning-disc system (CSU-X1; Yokogawa) and an Andor iXon Ultra EMCCD camera.

    Techniques: Purification, Expressing, Staining, Incubation