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Bio-Rad criterion tris hcl precast sds page gels
Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by <t>SDS-PAGE</t> followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.
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1) Product Images from "Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation"

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

Journal: Nucleic Acids Research

doi: 10.1093/nar/gku1132

Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.
Figure Legend Snippet: Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

Techniques Used: Fluorescence, Confocal Microscopy, Expressing, Marker, Fractionation, SDS Page, Western Blot

Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.
Figure Legend Snippet: Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

Techniques Used: Western Blot, SDS Page, Polyacrylamide Gel Electrophoresis, Activity Assay, Staining

Related Articles

Isolation:

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: Afterwards, mitochondrial, cytoplasmic and nuclear fractions were separated by differential centrifugation. .. All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure. .. Each fraction was tested with the following primary antibodies: histone H3 (Sigma, dilution 1:200), VDAC (Mitosciences MSA03, dilution 1:1000), tubulin (Sigma, dilution 1:1000) and a polyclonal rabbit antiserum raised against DmLRPPRC2 (generated by PSL GmbH, dilution 1:1000).

SDS Page:

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: Afterwards, mitochondrial, cytoplasmic and nuclear fractions were separated by differential centrifugation. .. All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure. .. Each fraction was tested with the following primary antibodies: histone H3 (Sigma, dilution 1:200), VDAC (Mitosciences MSA03, dilution 1:1000), tubulin (Sigma, dilution 1:1000) and a polyclonal rabbit antiserum raised against DmLRPPRC2 (generated by PSL GmbH, dilution 1:1000).

Article Title: Expression and Localization of an Hsp70 Protein in the Microsporidian Encephalitozoon cuniculi
Article Snippet: The strips were focused using a Biorad Protean IEF cell and the standard recommendations for programming. .. For the second dimension, the gel strips were equilibrated in the kit Equilibration Buffer I and II and precast Criterion 8–16% Tris-HCl SDS-PAGE gels (Biorad) were used. ..

Article Title: Identification of Potential Glycoprotein Biomarkers in Estrogen Receptor Positive (ER+) and Negative (ER-) Human Breast Cancer Tissues by LC-LTQ/FT-ICR Mass Spectrometry
Article Snippet: By use of PROTEAN IEF Cell (Bio-Rad), isoelectric focusing was performed according to the following procedure: rehydration of the IPG strips was done at 20 ˚C and 50 V for 16 h followed by focusing the proteins at 250 V for 15 min and then at 8,000 V maintained for a total of 50,000 V h per gel. .. 10% SDS-PAGE Tris-HCl Criterion (Bio-Rad, Hercules, CA) gels were prepared for 2-DE. ..

Article Title: Identification of Conus
Article Snippet: Following IEF, strips were reduced in equilibration buffer (75 m m Tris-HCl, 6 m urea, 30% glycerol, 2% SDS, 0.002% bromphenol blue) containing 65 m m dithiothreitol for 15 min followed by alkylation for 15 min in the presence of 80 m m iodoacetamide. .. Second dimension gel electrophoreses were performed on 8–16% Tris-HCl SDS-PAGE (Criterion, Bio-Rad) for 50 min at 200 V. Gels were stained with Coomassie Brilliant Blue G-250 (Bio-Rad). ..

Article Title: Abl Kinase Constructs Expressed in Bacteria: facilitation of structural and functional studies including segmental labeling by expressed protein ligation
Article Snippet: SH3-SH2 was purified through HiTrap™ SP HP column (GE Healthcare) in 20 mM MOPS pH 7.0 with a linear gradient of NaCl from 0 to 50% in 52 min. .. Abl kinase samples at different purification stages were subjected to 12% Tris-HCl SDS-PAGE gels (Bio-Rad), then transferred to PVDF membranes (Bio-Rad) using a Trans-Blot SD Semi-Dry Transfer Cell (Bio-Rad). ..

Western Blot:

Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation
Article Snippet: Afterwards, mitochondrial, cytoplasmic and nuclear fractions were separated by differential centrifugation. .. All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure. .. Each fraction was tested with the following primary antibodies: histone H3 (Sigma, dilution 1:200), VDAC (Mitosciences MSA03, dilution 1:1000), tubulin (Sigma, dilution 1:1000) and a polyclonal rabbit antiserum raised against DmLRPPRC2 (generated by PSL GmbH, dilution 1:1000).

Staining:

Article Title: Myxoma Virus M11L Prevents Apoptosis through Constitutive Interaction with Bak
Article Snippet: .. The proteins were resolved on a 4 to 15% Tris-HCl gradient gel (Bio-Rad) and then stained with colloidal Coomassie blue (Gel-Code Blue; Pierce). ..

Article Title: The XcpV/GspI Pseudopilin Has a Central Role in the Assembly of a Quaternary Complex within the T2SS Pseudopilus *
Article Snippet: The digitalized gels were then analyzed with the free software “ImageJ for Mac” ( ) to quantify and compare the intensity of the protein bands. .. The eluted complex presented in C ( panel 1 , lane E ) has been electrophoresed on a Native 8–16% Tris-HCl PAGE (Bio-Rad) at 4 °C in a Tris/Glycine running buffer for 1 h at 50 V and a further 2 h at 125 V. The native-PAGE was then stained with Coomassie Brillant Blue R-250. ..

Article Title: Identification of Conus
Article Snippet: Following IEF, strips were reduced in equilibration buffer (75 m m Tris-HCl, 6 m urea, 30% glycerol, 2% SDS, 0.002% bromphenol blue) containing 65 m m dithiothreitol for 15 min followed by alkylation for 15 min in the presence of 80 m m iodoacetamide. .. Second dimension gel electrophoreses were performed on 8–16% Tris-HCl SDS-PAGE (Criterion, Bio-Rad) for 50 min at 200 V. Gels were stained with Coomassie Brilliant Blue G-250 (Bio-Rad). ..

Polyacrylamide Gel Electrophoresis:

Article Title: The XcpV/GspI Pseudopilin Has a Central Role in the Assembly of a Quaternary Complex within the T2SS Pseudopilus *
Article Snippet: The digitalized gels were then analyzed with the free software “ImageJ for Mac” ( ) to quantify and compare the intensity of the protein bands. .. The eluted complex presented in C ( panel 1 , lane E ) has been electrophoresed on a Native 8–16% Tris-HCl PAGE (Bio-Rad) at 4 °C in a Tris/Glycine running buffer for 1 h at 50 V and a further 2 h at 125 V. The native-PAGE was then stained with Coomassie Brillant Blue R-250. ..

Clear Native PAGE:

Article Title: The XcpV/GspI Pseudopilin Has a Central Role in the Assembly of a Quaternary Complex within the T2SS Pseudopilus *
Article Snippet: The digitalized gels were then analyzed with the free software “ImageJ for Mac” ( ) to quantify and compare the intensity of the protein bands. .. The eluted complex presented in C ( panel 1 , lane E ) has been electrophoresed on a Native 8–16% Tris-HCl PAGE (Bio-Rad) at 4 °C in a Tris/Glycine running buffer for 1 h at 50 V and a further 2 h at 125 V. The native-PAGE was then stained with Coomassie Brillant Blue R-250. ..

Purification:

Article Title: Abl Kinase Constructs Expressed in Bacteria: facilitation of structural and functional studies including segmental labeling by expressed protein ligation
Article Snippet: SH3-SH2 was purified through HiTrap™ SP HP column (GE Healthcare) in 20 mM MOPS pH 7.0 with a linear gradient of NaCl from 0 to 50% in 52 min. .. Abl kinase samples at different purification stages were subjected to 12% Tris-HCl SDS-PAGE gels (Bio-Rad), then transferred to PVDF membranes (Bio-Rad) using a Trans-Blot SD Semi-Dry Transfer Cell (Bio-Rad). ..

Electrophoresis:

Article Title: Conditional Disruption of the Peroxisome Proliferator-Activated Receptor ? Gene in Mice Results in Lowered Expression of ABCA1, ABCG1, and apoE in Macrophages and Reduced Cholesterol Efflux
Article Snippet: Protein contained in the nuclear extracts of macrophages or total protein of Hepa-1 cells was assayed by the BCA protein assay (Pierce Chemical Co., Rockford, Ill.). .. Then, 10 μg of total protein from Hepa-1 cells and 10 μg of protein from nuclear extracts of macrophages were subjected to electrophoresis on a 4 to 15% Tris-HCl gradient gel (Bio-Rad, Hercules, Calif.), transferred to Immobilon-P membranes (Millipore, Bedford, Mass.), and probed according to the manufacturer's recommendations with anti-PPARγ antibodies (E-8 and H-100; Santa Cruz Biotechnology, Inc., Santa Cruz, Calif.) as indicated. .. Detection of immunoreactive proteins was done by an enhanced chemiluminescence blot detection system (Amersham, Inc., Arlington Heights, Ill.).

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  • 96
    Bio-Rad tris hcl sds page gels
    Heterologous expression of E. cuniculi C1 Hsp70 protein as a histidine fusion protein in E. coli and Western blot analysis using purified C1 antibodies. A Coomassie stained <t>SDS-PAGE</t> gel ((a), right panel) of uninduced and IPTG induced expression of the recombinant protein shows a ~76 kDa protein in the induced lane. A Western blot of the SDS-PAGE gel was performed using histidine-tag-specific antibodies ((a), left panel) confirmed the recombinant protein induction. (b) A single ~76 kDa band was detected on 1D Western blot of E. cuniculi and E. intestinalis total spore protein using purified C1 Hsp70 protein antibodies. (c) The C1 (ECU02_0100) and B1 (ECU03_0520) Hsp70-related proteins were identified from a Coomassie stained 2D SDS-PAGE gel of E. cuniculi total spore protein by MALDI-MS analysis of trypsin digested gel spots. (d) Western analysis of the 2D gel using the C1 specific antibodies detected only the C1 protein (d).
    Tris Hcl Sds Page Gels, 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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    97
    Bio-Rad criterion tris hcl precast sodium dodecyl sulphate polyacrylamide gel electrophoresis sds page gels
    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by <t>SDS-PAGE</t> followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.
    Criterion Tris Hcl Precast Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis Sds Page Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    96
    Bio-Rad criterion tris hcl precast sds page gels
    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by <t>SDS-PAGE</t> followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.
    Criterion Tris Hcl Precast Sds Page Gels, 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
    https://www.bioz.com/result/criterion tris hcl precast sds page gels/product/Bio-Rad
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    criterion tris hcl precast sds page gels - by Bioz Stars, 2021-04
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    Heterologous expression of E. cuniculi C1 Hsp70 protein as a histidine fusion protein in E. coli and Western blot analysis using purified C1 antibodies. A Coomassie stained SDS-PAGE gel ((a), right panel) of uninduced and IPTG induced expression of the recombinant protein shows a ~76 kDa protein in the induced lane. A Western blot of the SDS-PAGE gel was performed using histidine-tag-specific antibodies ((a), left panel) confirmed the recombinant protein induction. (b) A single ~76 kDa band was detected on 1D Western blot of E. cuniculi and E. intestinalis total spore protein using purified C1 Hsp70 protein antibodies. (c) The C1 (ECU02_0100) and B1 (ECU03_0520) Hsp70-related proteins were identified from a Coomassie stained 2D SDS-PAGE gel of E. cuniculi total spore protein by MALDI-MS analysis of trypsin digested gel spots. (d) Western analysis of the 2D gel using the C1 specific antibodies detected only the C1 protein (d).

    Journal: International Journal of Microbiology

    Article Title: Expression and Localization of an Hsp70 Protein in the Microsporidian Encephalitozoon cuniculi

    doi: 10.1155/2010/523654

    Figure Lengend Snippet: Heterologous expression of E. cuniculi C1 Hsp70 protein as a histidine fusion protein in E. coli and Western blot analysis using purified C1 antibodies. A Coomassie stained SDS-PAGE gel ((a), right panel) of uninduced and IPTG induced expression of the recombinant protein shows a ~76 kDa protein in the induced lane. A Western blot of the SDS-PAGE gel was performed using histidine-tag-specific antibodies ((a), left panel) confirmed the recombinant protein induction. (b) A single ~76 kDa band was detected on 1D Western blot of E. cuniculi and E. intestinalis total spore protein using purified C1 Hsp70 protein antibodies. (c) The C1 (ECU02_0100) and B1 (ECU03_0520) Hsp70-related proteins were identified from a Coomassie stained 2D SDS-PAGE gel of E. cuniculi total spore protein by MALDI-MS analysis of trypsin digested gel spots. (d) Western analysis of the 2D gel using the C1 specific antibodies detected only the C1 protein (d).

    Article Snippet: For the second dimension, the gel strips were equilibrated in the kit Equilibration Buffer I and II and precast Criterion 8–16% Tris-HCl SDS-PAGE gels (Biorad) were used.

    Techniques: Expressing, Western Blot, Purification, Staining, SDS Page, Recombinant, Mass Spectrometry, Two-Dimensional Gel Electrophoresis

    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Article Snippet: All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure.

    Techniques: Fluorescence, Confocal Microscopy, Expressing, Marker, Fractionation, SDS Page, Western Blot

    Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Article Snippet: All isolated fractions were separated in 4–15% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad) and tested by a standard western blotting procedure.

    Techniques: Western Blot, SDS Page, Polyacrylamide Gel Electrophoresis, Activity Assay, Staining

    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Article Snippet: Protein extracts, 20–40 μg, were denatured at 95°C for 5 min and separated in 4–20% Criterion Tris-HCl precast sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) gels (Bio-Rad).

    Techniques: Fluorescence, Confocal Microscopy, Expressing, Marker, Fractionation, SDS Page, Western Blot

    Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Article Snippet: Protein extracts, 20–40 μg, were denatured at 95°C for 5 min and separated in 4–20% Criterion Tris-HCl precast sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) gels (Bio-Rad).

    Techniques: Western Blot, SDS Page, Polyacrylamide Gel Electrophoresis, Activity Assay, Staining

    Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Subcellular localization of DmLRPPRC2. (A) Fluorescence confocal microscopy images showing HeLa cells ( n = 15) expressing a DmLRPPRC2-GFP fusion protein and counterstained with the mitochondrial marker MitoTracker Deep Red. Scale bar: 10 μm. (B) Subcellular fractionation showing the presence of DmLRPPRC2 in the mitochondrial fraction. Subcellular fractions were separated by SDS-PAGE followed by western blot analysis to detect histone H3 (a nuclear marker), tubulin (a cytosolic marker), VDAC (a mitochondrial marker) and DmLRPPRC2. See also Supplementary Figure S1A and B.

    Article Snippet: For mass spectrometry analyses, samples were denatured at 95°C for 5 min followed by SDS-PAGE on 4–20% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad).

    Techniques: Fluorescence, Confocal Microscopy, Expressing, Marker, Fractionation, SDS Page, Western Blot

    Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Journal: Nucleic Acids Research

    Article Title: Drosophila melanogaster LRPPRC2 is involved in coordination of mitochondrial translation

    doi: 10.1093/nar/gku1132

    Figure Lengend Snippet: Steady-state levels and activities of the OXPHOS complexes. (A) Western blot analysis of the Lrpprc2 RNAi#1 line (left side) and the Lrpprc2 RNAi#2 line (right side) performed on 20–40 μg whole-body protein extracts from controls and DmLrpprc2 KD third-instar larvae and 6-day-old adults. Protein extracts were separated by standard SDS-PAGE followed by western blot analysis with antibodies against the nuclear-encoded subunit NDUFS3 of complex I, the α-subunit of complex V and VDAC, the latter used as reference for loading. (B) BN-PAGE combined with complex I, complex IV and complex V in-gel activity analyses on the Lrpprc2 RNAi#1 line and the Lrpprc2 RNAi#2 line. BN-PAGE was performed on 75 μg for complex I, 100 μg for complex IV and 150 μg for complex V of mitochondrial protein extracts from control and DmLrpprc2 KD third-instar larvae. The assembly status of complex V (right panel) is black because of color inversion. Loading controls are provided by Coomassie staining to assess the total mitochondrial protein content per sample (only for complex V, left panel) and western blot analysis of VDAC protein levels in mitochondrial protein lysates collected prior to BN-PAGE gel loading. The position of complex I (CI), complex IV (CIV), complex V dimers (CV 2 ), complex V monomers (CV 1 ) and complex V subassembled components ( sub CV a and sub CV b ) are indicated by arrows.

    Article Snippet: For mass spectrometry analyses, samples were denatured at 95°C for 5 min followed by SDS-PAGE on 4–20% Criterion Tris-HCl precast SDS-PAGE gels (Bio-Rad).

    Techniques: Western Blot, SDS Page, Polyacrylamide Gel Electrophoresis, Activity Assay, Staining