Structured Review

GE Healthcare ethylene glycol tetraacetic acid egta
Ethylene Glycol Tetraacetic Acid Egta, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/ethylene glycol tetraacetic acid egta/product/GE Healthcare
Average 93 stars, based on 10 article reviews
Price from $9.99 to $1999.99
ethylene glycol tetraacetic acid egta - by Bioz Stars, 2020-07
93/100 stars

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Lysis:

Article Title: Neuronal deletion of GSK3β increases microtubule speed in the growth cone and enhances axon regeneration via CRMP-2 and independently of MAP1B and CLASP2
Article Snippet: .. DRG were homogenized in lysis buffer (20 mM 4-morpholinepropanesulfonic acid (MOPS), 2 mM ethylene glycol tetraacetic acid (EGTA), 5 mM ethylenediaminetetraacetic acid (EDTA), 30 mM NaF, 60 mM β-glycerophosphate, 20 mM sodium pyrophosphate, 1 mM sodium orthovanadate, 1% Triton X-100, 1% dithiothreitol (DTT), 1 mM phenylmethylsulfonyl fluoride (PMSF) and protease inhibitor cocktail (GE Healthcare, Carnaxide, Portugal)). .. Protein extracts (500 μg) were analyzed using the Kinexus phospho-site broad signaling pathway screen version 1.3 (KPSS-1.3, Kinexus Bioinformatics Corp, Vancouver, Canada).

Protease Inhibitor:

Article Title: Neuronal deletion of GSK3β increases microtubule speed in the growth cone and enhances axon regeneration via CRMP-2 and independently of MAP1B and CLASP2
Article Snippet: .. DRG were homogenized in lysis buffer (20 mM 4-morpholinepropanesulfonic acid (MOPS), 2 mM ethylene glycol tetraacetic acid (EGTA), 5 mM ethylenediaminetetraacetic acid (EDTA), 30 mM NaF, 60 mM β-glycerophosphate, 20 mM sodium pyrophosphate, 1 mM sodium orthovanadate, 1% Triton X-100, 1% dithiothreitol (DTT), 1 mM phenylmethylsulfonyl fluoride (PMSF) and protease inhibitor cocktail (GE Healthcare, Carnaxide, Portugal)). .. Protein extracts (500 μg) were analyzed using the Kinexus phospho-site broad signaling pathway screen version 1.3 (KPSS-1.3, Kinexus Bioinformatics Corp, Vancouver, Canada).

Article Title: Poly(Trimethylene Carbonate-co-?-Caprolactone) Promotes Axonal Growth
Article Snippet: .. 4.8 Western Blot Cortical neuron lysates were prepared by washing cells with PBS and further lysed in buffer containing 20 mM 3-(n-morpholino)propanesulfonic acid (MOPS), 2 mM ethylene glycol tetraacetic acid (EGTA), 5 mM ethylenediaminetetraacetic acid (EDTA), 30 mM NaF, 60 mM β-glycerophosphate, 20 mM sodium pyrophosphate, 1 mM sodium orthovanadate, 1% (v/v) Triton X-100, 1% (v/v) DL-dithiothreitol (DTT), 1 mM phenylmethanesulfonyl fluoride (PMSF) and protease inhibitor cocktail (Amersham). .. Protein lysates (25–100 µg/lane) were run on a 12% SDS-PAGE gel and then transferred to a nitrocellulose membrane (Amersham).

Western Blot:

Article Title: Poly(Trimethylene Carbonate-co-?-Caprolactone) Promotes Axonal Growth
Article Snippet: .. 4.8 Western Blot Cortical neuron lysates were prepared by washing cells with PBS and further lysed in buffer containing 20 mM 3-(n-morpholino)propanesulfonic acid (MOPS), 2 mM ethylene glycol tetraacetic acid (EGTA), 5 mM ethylenediaminetetraacetic acid (EDTA), 30 mM NaF, 60 mM β-glycerophosphate, 20 mM sodium pyrophosphate, 1 mM sodium orthovanadate, 1% (v/v) Triton X-100, 1% (v/v) DL-dithiothreitol (DTT), 1 mM phenylmethanesulfonyl fluoride (PMSF) and protease inhibitor cocktail (Amersham). .. Protein lysates (25–100 µg/lane) were run on a 12% SDS-PAGE gel and then transferred to a nitrocellulose membrane (Amersham).

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  • 93
    GE Healthcare percoll solution
    MAM accommodates DRMs associated with Sig-1R. A, purification of MAM and microsomal fractions from CHO cells. Nuclear (P1), mitochondrial (Mito), MAM, microsomal (P3), and cytosolic (Cyt) fractions were prepared by differential centrifugation combined with a <t>Percoll</t> gradient fractionation. Five micrograms of proteins was applied to SDS-PAGE, followed by immunoblotting. COX, cytochrome c oxidase subunit I. Asterisks indicate ER chaperones involved in vesicular transport. Graphs represent fraction distributions of proteins in which the sum of five fractions was taken as 100% for each protein. B, Sig-1R-associated DRMs in the MAM. MAM and microsomes (P3) (25 μg of total proteins in each) were extracted by 0.5% Tx (Tx-100) or Triton X-114 at 4°C. DRMs and detergent-soluble supernatant (S) were prepared by differential centrifugations. The numbers represent the average of optical density (O.D.) measured in each protein band ( n = 3). C, silver staining for total proteins associated with DRMs in MAM and microsomal fractions. MAM and microsomes (25 μg of total proteins in each) were extracted in 0.5% Tx at 4°C, and DRMs and soluble supernatants (S) were prepared. Proteins were visualized by 13% SDS-PAGE, followed by silver staining. The numbers represent the average of O.D. measured in each lane ( n = 3). MW, molecular weight of standard proteins. D, lipid contents in MAM and microsomal fractions. Lipids were extracted and analyzed by HPTLC. Cholesterol (Chol) was detected using a ferric chloride spray; GlcCer using a diphenylamine-aniline spray. Lipids in the second panel were visualized under UV light after an ANS spray. In the lipid overlay assay for ceramides (Cer, bottom), ceramides extracted from HPTLC plates were immobilized on a nitrocellulose membrane followed by immunoblotting with anti-ceramide antibodies. SM, sphingomyelin.
    Percoll Solution, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 174 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/percoll solution/product/GE Healthcare
    Average 93 stars, based on 174 article reviews
    Price from $9.99 to $1999.99
    percoll solution - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    93
    GE Healthcare egta
    Oligomerization analysis of in vitro synthesized WT and mutant Vp1s. (A) Electron micrographs of VLPs (VLP; scale bar, 10 nm) and pentamers <t>(EGTA</t> + DTT; scale bar, 10 nm) formed by WT JCV <t>Vp1.</t> (B) The mixtures resulting from the in vitro transcription-coupled-translation of the empty pURE2 plasmid (Mock) and of the Vp1-encoding pURE2-Vp1 (WT) were supplemented with DTT, boiled, separated by SDS-PAGE, and immunoblotted with a rabbit anti-Vp1 antibody. An arrowhead marks the position of monomeric Vp1. An arrow indicates nonspecific bands. (C) Sedimentation profiles of in vitro translated single cysteine substitution mutants. Monomeric Vp1s, pentameric Vp1s, and the in vitro translation products for WT Vp1 or cysteine point mutant Vp1s (C42A, C80A, C97A, C200A, C247A, C260A, or C80T) were separated by 5–20% sucrose gradient sedimentation under denaturing conditions, and the resulting fractions were examined for the presence of Vp1 by SDS-PAGE and immunoblotting.
    Egta, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 93/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/egta/product/GE Healthcare
    Average 93 stars, based on 32 article reviews
    Price from $9.99 to $1999.99
    egta - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

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    MAM accommodates DRMs associated with Sig-1R. A, purification of MAM and microsomal fractions from CHO cells. Nuclear (P1), mitochondrial (Mito), MAM, microsomal (P3), and cytosolic (Cyt) fractions were prepared by differential centrifugation combined with a Percoll gradient fractionation. Five micrograms of proteins was applied to SDS-PAGE, followed by immunoblotting. COX, cytochrome c oxidase subunit I. Asterisks indicate ER chaperones involved in vesicular transport. Graphs represent fraction distributions of proteins in which the sum of five fractions was taken as 100% for each protein. B, Sig-1R-associated DRMs in the MAM. MAM and microsomes (P3) (25 μg of total proteins in each) were extracted by 0.5% Tx (Tx-100) or Triton X-114 at 4°C. DRMs and detergent-soluble supernatant (S) were prepared by differential centrifugations. The numbers represent the average of optical density (O.D.) measured in each protein band ( n = 3). C, silver staining for total proteins associated with DRMs in MAM and microsomal fractions. MAM and microsomes (25 μg of total proteins in each) were extracted in 0.5% Tx at 4°C, and DRMs and soluble supernatants (S) were prepared. Proteins were visualized by 13% SDS-PAGE, followed by silver staining. The numbers represent the average of O.D. measured in each lane ( n = 3). MW, molecular weight of standard proteins. D, lipid contents in MAM and microsomal fractions. Lipids were extracted and analyzed by HPTLC. Cholesterol (Chol) was detected using a ferric chloride spray; GlcCer using a diphenylamine-aniline spray. Lipids in the second panel were visualized under UV light after an ANS spray. In the lipid overlay assay for ceramides (Cer, bottom), ceramides extracted from HPTLC plates were immobilized on a nitrocellulose membrane followed by immunoblotting with anti-ceramide antibodies. SM, sphingomyelin.

    Journal: Molecular Pharmacology

    Article Title: Detergent-Resistant Microdomains Determine the Localization of ?-1 Receptors to the Endoplasmic Reticulum-Mitochondria Junction S⃞

    doi: 10.1124/mol.109.062539

    Figure Lengend Snippet: MAM accommodates DRMs associated with Sig-1R. A, purification of MAM and microsomal fractions from CHO cells. Nuclear (P1), mitochondrial (Mito), MAM, microsomal (P3), and cytosolic (Cyt) fractions were prepared by differential centrifugation combined with a Percoll gradient fractionation. Five micrograms of proteins was applied to SDS-PAGE, followed by immunoblotting. COX, cytochrome c oxidase subunit I. Asterisks indicate ER chaperones involved in vesicular transport. Graphs represent fraction distributions of proteins in which the sum of five fractions was taken as 100% for each protein. B, Sig-1R-associated DRMs in the MAM. MAM and microsomes (P3) (25 μg of total proteins in each) were extracted by 0.5% Tx (Tx-100) or Triton X-114 at 4°C. DRMs and detergent-soluble supernatant (S) were prepared by differential centrifugations. The numbers represent the average of optical density (O.D.) measured in each protein band ( n = 3). C, silver staining for total proteins associated with DRMs in MAM and microsomal fractions. MAM and microsomes (25 μg of total proteins in each) were extracted in 0.5% Tx at 4°C, and DRMs and soluble supernatants (S) were prepared. Proteins were visualized by 13% SDS-PAGE, followed by silver staining. The numbers represent the average of O.D. measured in each lane ( n = 3). MW, molecular weight of standard proteins. D, lipid contents in MAM and microsomal fractions. Lipids were extracted and analyzed by HPTLC. Cholesterol (Chol) was detected using a ferric chloride spray; GlcCer using a diphenylamine-aniline spray. Lipids in the second panel were visualized under UV light after an ANS spray. In the lipid overlay assay for ceramides (Cer, bottom), ceramides extracted from HPTLC plates were immobilized on a nitrocellulose membrane followed by immunoblotting with anti-ceramide antibodies. SM, sphingomyelin.

    Article Snippet: Crude mitochondrial membranes were suspended in 0.5 ml of isolation medium (250 mM mannitol, 5 mM HEPES/KOH pH 7.4, and 0.5 mM EGTA/KOH), layered on Percoll solution [225 mM mannitol, 25 mM HEPES/KOH, pH 7.4, 1 mM EGTA/KOH, and 30% (v/v) Percoll (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK)], and centrifuged at 95,000 g for 30 min in an SW 55Ti rotor.

    Techniques: Purification, Centrifugation, Fractionation, SDS Page, Silver Staining, Molecular Weight, High Performance Thin Layer Chromatography, Overlay Assay

    Oligomerization analysis of in vitro synthesized WT and mutant Vp1s. (A) Electron micrographs of VLPs (VLP; scale bar, 10 nm) and pentamers (EGTA + DTT; scale bar, 10 nm) formed by WT JCV Vp1. (B) The mixtures resulting from the in vitro transcription-coupled-translation of the empty pURE2 plasmid (Mock) and of the Vp1-encoding pURE2-Vp1 (WT) were supplemented with DTT, boiled, separated by SDS-PAGE, and immunoblotted with a rabbit anti-Vp1 antibody. An arrowhead marks the position of monomeric Vp1. An arrow indicates nonspecific bands. (C) Sedimentation profiles of in vitro translated single cysteine substitution mutants. Monomeric Vp1s, pentameric Vp1s, and the in vitro translation products for WT Vp1 or cysteine point mutant Vp1s (C42A, C80A, C97A, C200A, C247A, C260A, or C80T) were separated by 5–20% sucrose gradient sedimentation under denaturing conditions, and the resulting fractions were examined for the presence of Vp1 by SDS-PAGE and immunoblotting.

    Journal: PLoS ONE

    Article Title: Cysteine Residues in the Major Capsid Protein, Vp1, of the JC Virus Are Important for Protein Stability and Oligomer Formation

    doi: 10.1371/journal.pone.0076668

    Figure Lengend Snippet: Oligomerization analysis of in vitro synthesized WT and mutant Vp1s. (A) Electron micrographs of VLPs (VLP; scale bar, 10 nm) and pentamers (EGTA + DTT; scale bar, 10 nm) formed by WT JCV Vp1. (B) The mixtures resulting from the in vitro transcription-coupled-translation of the empty pURE2 plasmid (Mock) and of the Vp1-encoding pURE2-Vp1 (WT) were supplemented with DTT, boiled, separated by SDS-PAGE, and immunoblotted with a rabbit anti-Vp1 antibody. An arrowhead marks the position of monomeric Vp1. An arrow indicates nonspecific bands. (C) Sedimentation profiles of in vitro translated single cysteine substitution mutants. Monomeric Vp1s, pentameric Vp1s, and the in vitro translation products for WT Vp1 or cysteine point mutant Vp1s (C42A, C80A, C97A, C200A, C247A, C260A, or C80T) were separated by 5–20% sucrose gradient sedimentation under denaturing conditions, and the resulting fractions were examined for the presence of Vp1 by SDS-PAGE and immunoblotting.

    Article Snippet: For preparation of the Vp1 pentamer, purified VLPs were adjusted to 25 mM EGTA and 30 mM DTT, incubated for 1 h at 37°C, and separated on a Superdex 200 gel filtration chromatography column (GE Healthcare, Uppsala, Sweden) in 20 mM Tris-HCl (pH 8.0), 150 mM NaCl, 5 mM EGTA, and 5 mM DTT at 4°C.

    Techniques: In Vitro, Synthesized, Mutagenesis, Plasmid Preparation, SDS Page, Sedimentation

    Myo5a-HMM and the MD-IQ1 bind to GST-GTD in a Ca 2+ -dependent manner. FLAG-tagged MD-IQ1 or Myo5a-HMM was incubated with GST-GTD or GST and was pulled down by GSH-Sepharose under EGTA or pCa4 conditions. The pulled-down samples (20 μL each) were

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Calmodulin in complex with the first IQ motif of myosin-5a functions as an intact calcium sensor

    doi: 10.1073/pnas.1607702113

    Figure Lengend Snippet: Myo5a-HMM and the MD-IQ1 bind to GST-GTD in a Ca 2+ -dependent manner. FLAG-tagged MD-IQ1 or Myo5a-HMM was incubated with GST-GTD or GST and was pulled down by GSH-Sepharose under EGTA or pCa4 conditions. The pulled-down samples (20 μL each) were

    Article Snippet: For the pull-down assay under EGTA conditions, 100 μL of 0.5 μM GST-GTD or GST and 1 μM FLAG-tagged MD-IQ1 or Myo5a-HMM in washing buffer [20 mM 3-(N-morpholino)propanesulfonic acid (Mops)-KOH (pH 7.0), 50 mM NaCl, 1 mM MgCl2 , 1 mM EGTA, and 1 mM DTT] were mixed with 10 μL of glutathione (GSH)-Sepharose (GE Healthcare) and incubated with rotation at 4 °C for 2 h. After three washings with 200 μL washing buffer to remove the unbound proteins, the bound proteins were eluted with 40 μL elution buffer [10 mM GSH, 50 mM Tris⋅HCl (pH 7.5), 50 mM NaCl, and 1 mM DTT].

    Techniques: Incubation