two-dimensional (2d) gel analysis Search Results


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Bio-Rad 2d gel analysis software
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
2d Gel Analysis Software, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Scienta Omicron GmbH 2d angle-resolved time-of-flight electron spectrometer artof10k
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
2d Angle Resolved Time Of Flight Electron Spectrometer Artof10k, supplied by Scienta Omicron GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MetaCell Inc two-dimensional (2d) projection
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
Two Dimensional (2d) Projection, supplied by MetaCell Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Nikon 2d images
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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PHORETIX INTERNATIONAL LIMITED 2d gel analysis software phoretix 2005
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
2d Gel Analysis Software Phoretix 2005, supplied by PHORETIX INTERNATIONAL LIMITED, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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COMSOL Inc finite element algorithm (fem)
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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ANSYS inc finite element model
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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ScienCell 2d-page
Comparative <t>2D</t> <t>gel</t> electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.
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Fangman Specialties 2d gel electrophoresis
Analysis of low-copy-rDNA strains. (A) Southern hybridization analysis of rDNA copy numbers. DNA was digested with BglII and subjected to <t>electrophoresis</t> followed by Southern analysis using the rDNA probe (Fig. 1). A single-copy gene, MCM2, was used as an internal control for normalization. (B) Quantitation of the intensities of the bands. NOY408-1b (wild-type strain), NOY408-1bf (fob1), TAK300 (fob1; low-copy rDNA strain), TAK301 (fob1 pol1; low-copy rDNA strain). (C) Collision between the transcription and the replication machineries analyzed by <t>2D</t> gel analysis. DNA was prepared from the strains indicated, digested with BglII and SphI, and subjected to 2D agarose gel electrophoresis followed by Southern hybridization using the rDNA probe (see Fig. 1). A spot indicated by an arrowhead shows accumulation of Y-shaped DNA molecules at the RFB site (panel a). The slowdown region (SDR) is located between two arrows (panel c). The numbers in parentheses are copy numbers of rDNA in each strain. (Panel a) NOY408-1b (wild-type strain). (Panel b) NOY408-1bf (fob1). (Panel c) TAK300 (fob1; low-copy rDNA strain). (Panel d) TAK301 (fob1 pol1; low-copy rDNA strain). (Panel e) TAK301, complemented by a plasmid-borne RPA135 gene (fob1 POLI; low-copy rDNA strain).
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Comparative 2D gel electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.

Journal:

Article Title: Involvement of Superoxide Dismutases in the Response of Escherichia coli to Selenium Oxides

doi: 10.1128/JB.184.6.1556-1564.2002

Figure Lengend Snippet: Comparative 2D gel electrophoresis analyses of total E. coli proteins expressed in response to selenium oxide treatment. Autoradiograms of 2D gels performed with total E. coli extracts from [35S] methionine-labeled cells as described in Materials and Methods are shown. The extracts were prepared from control untreated cells (A), from cells exposed to SeO42− (2 mM) for 30 min (B), and from cells exposed to SeO32− (2 mM) for 30 min (C). Proteins whose synthesis rate is stimulated upon SeO42− or SeO32− exposure were identified by mass spectrometry and are indicated on the map. Protein spots induced but not characterized are also indicated by an arrow. Proteins repressed by SeO42− or SeO32− are indicated by a black bar in panel A.

Article Snippet: The spots on the radioactive gels were recorded by PhosphorImager technology (Molecular Dynamics) and analyzed with a 2D gel analysis software (MelanieII; Bio-Rad).

Techniques: Two-Dimensional Gel Electrophoresis, Electrophoresis, Labeling, Mass Spectrometry

Analysis of low-copy-rDNA strains. (A) Southern hybridization analysis of rDNA copy numbers. DNA was digested with BglII and subjected to electrophoresis followed by Southern analysis using the rDNA probe (Fig. 1). A single-copy gene, MCM2, was used as an internal control for normalization. (B) Quantitation of the intensities of the bands. NOY408-1b (wild-type strain), NOY408-1bf (fob1), TAK300 (fob1; low-copy rDNA strain), TAK301 (fob1 pol1; low-copy rDNA strain). (C) Collision between the transcription and the replication machineries analyzed by 2D gel analysis. DNA was prepared from the strains indicated, digested with BglII and SphI, and subjected to 2D agarose gel electrophoresis followed by Southern hybridization using the rDNA probe (see Fig. 1). A spot indicated by an arrowhead shows accumulation of Y-shaped DNA molecules at the RFB site (panel a). The slowdown region (SDR) is located between two arrows (panel c). The numbers in parentheses are copy numbers of rDNA in each strain. (Panel a) NOY408-1b (wild-type strain). (Panel b) NOY408-1bf (fob1). (Panel c) TAK300 (fob1; low-copy rDNA strain). (Panel d) TAK301 (fob1 pol1; low-copy rDNA strain). (Panel e) TAK301, complemented by a plasmid-borne RPA135 gene (fob1 POLI; low-copy rDNA strain).

Journal:

Article Title: Transcription-dependent recombination and the role of fork collision in yeast rDNA

doi: 10.1101/gad.1085403

Figure Lengend Snippet: Analysis of low-copy-rDNA strains. (A) Southern hybridization analysis of rDNA copy numbers. DNA was digested with BglII and subjected to electrophoresis followed by Southern analysis using the rDNA probe (Fig. 1). A single-copy gene, MCM2, was used as an internal control for normalization. (B) Quantitation of the intensities of the bands. NOY408-1b (wild-type strain), NOY408-1bf (fob1), TAK300 (fob1; low-copy rDNA strain), TAK301 (fob1 pol1; low-copy rDNA strain). (C) Collision between the transcription and the replication machineries analyzed by 2D gel analysis. DNA was prepared from the strains indicated, digested with BglII and SphI, and subjected to 2D agarose gel electrophoresis followed by Southern hybridization using the rDNA probe (see Fig. 1). A spot indicated by an arrowhead shows accumulation of Y-shaped DNA molecules at the RFB site (panel a). The slowdown region (SDR) is located between two arrows (panel c). The numbers in parentheses are copy numbers of rDNA in each strain. (Panel a) NOY408-1b (wild-type strain). (Panel b) NOY408-1bf (fob1). (Panel c) TAK300 (fob1; low-copy rDNA strain). (Panel d) TAK301 (fob1 pol1; low-copy rDNA strain). (Panel e) TAK301, complemented by a plasmid-borne RPA135 gene (fob1 POLI; low-copy rDNA strain).

Article Snippet: Replication fork blocking and slowdown activities were analyzed using 2D gel electrophoresis as described previously ( Brewer and Fangman 1987 ).

Techniques: Hybridization, Electrophoresis, Control, Quantitation Assay, Two-Dimensional Gel Electrophoresis, Agarose Gel Electrophoresis, Plasmid Preparation