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  • 99
    Bio-Rad bio rad chemidoc xrs
    Site-specific incorporation of AzF into position 160 of Uox ( a ) Crystal structure of Uox (PDB ID: 1WS2) viewed by the PyMOL program. W160 and the active site are marked in blue and red, respectively. ( b ) MALDI-TOF spectra of Lys-C-digested fragments derived from the Uox-160AzF (top) and Uox-WT (bottom). ( c ) The fluorescence image of protein gel of Uox-160AzF and Uox-WT reacted with DBCO-Rho taken by Bio-Rad <t>ChemiDoc™</t> <t>XRS+</t> (excitation: 302 nm, emission: 510–610 nm).
    Bio Rad Chemidoc Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1335 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Collaborative Drug Discovery Inc bio rad chemidoc xrs
    Site-specific incorporation of AzF into position 160 of Uox ( a ) Crystal structure of Uox (PDB ID: 1WS2) viewed by the PyMOL program. W160 and the active site are marked in blue and red, respectively. ( b ) MALDI-TOF spectra of Lys-C-digested fragments derived from the Uox-160AzF (top) and Uox-WT (bottom). ( c ) The fluorescence image of protein gel of Uox-160AzF and Uox-WT reacted with DBCO-Rho taken by Bio-Rad <t>ChemiDoc™</t> <t>XRS+</t> (excitation: 302 nm, emission: 510–610 nm).
    Bio Rad Chemidoc Xrs, supplied by Collaborative Drug Discovery Inc, used in various techniques. Bioz Stars score: 87/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Bio-Rad bio rad chemidox xrs
    Site-specific incorporation of AzF into position 160 of Uox ( a ) Crystal structure of Uox (PDB ID: 1WS2) viewed by the PyMOL program. W160 and the active site are marked in blue and red, respectively. ( b ) MALDI-TOF spectra of Lys-C-digested fragments derived from the Uox-160AzF (top) and Uox-WT (bottom). ( c ) The fluorescence image of protein gel of Uox-160AzF and Uox-WT reacted with DBCO-Rho taken by Bio-Rad <t>ChemiDoc™</t> <t>XRS+</t> (excitation: 302 nm, emission: 510–610 nm).
    Bio Rad Chemidox Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Bio-Rad bio rad chemdoc xrs
    Site-specific incorporation of AzF into position 160 of Uox ( a ) Crystal structure of Uox (PDB ID: 1WS2) viewed by the PyMOL program. W160 and the active site are marked in blue and red, respectively. ( b ) MALDI-TOF spectra of Lys-C-digested fragments derived from the Uox-160AzF (top) and Uox-WT (bottom). ( c ) The fluorescence image of protein gel of Uox-160AzF and Uox-WT reacted with DBCO-Rho taken by Bio-Rad <t>ChemiDoc™</t> <t>XRS+</t> (excitation: 302 nm, emission: 510–610 nm).
    Bio Rad Chemdoc Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 86/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Bio-Rad chemidoc xrs imager bio rad
    Half-life of CrcZ produced from plasmid p424-Z in cells with CrcZ-null, Hfq-null, or Crc-null genetic backgrounds. ( A − C ) P. putida strains KT2440-Z (Δ crcZ ), KT2440Δ hfq (Δ hfq ), and KTCRC (Δ crc ) were cultured in LB medium with streptomycin and 1 mM IPTG. At a turbidity of 0.6 (A 600 ), rifampicin was added to stop transcription. Aliquots were withdrawn at 0, 2, 4, 8, 16, and 32 min post-rifampicin addition, total RNA was isolated, resolved on a 6% polyacrylamide/7 M urea gel, and CrcZ and 5S rRNA detected by Northern blot with specific probes. Band intensities were quantified using a <t>ChemiDoc</t> <t>XRS</t> imager and Image Lab software (Bio-Rad). Values obtained for the larger (primary CrcZ transcript) or shorter bands (processed CrcZ transcript) detected with the CrcZ probe were normalized to those of the 5S rRNA of the corresponding sample. ( D , E ) Plots show the values for each time point expressed relative to that at time 0. Processed CrcZ was not detected in the Δ hfq strain. Data shown as mean ± SD for three independent assays.
    Chemidoc Xrs Imager Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 86/100, based on 24 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Bio-Rad chemidoc xrs system bio rad
    Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a <t>ChemiDoc</t> <t>XRS</t> system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.
    Chemidoc Xrs System Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 82/100, based on 347 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bio-Rad chemidoc xrs imaging system bio rad
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Chemidoc Xrs Imaging System Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 85/100, based on 1120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Bio-Rad bio rad chemidoc xr
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Bio Rad Chemidoc Xr, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 78/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Bio-Rad image analysis system chemidoc xrs bio rad
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Image Analysis System Chemidoc Xrs Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Bio-Rad microscope bio rad chemidoc xrs
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Microscope Bio Rad Chemidoc Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad chemidoc xrs plus luminescent image analyser bio rad
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Chemidoc Xrs Plus Luminescent Image Analyser Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 78/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Bio-Rad molecular imager chemidoc xrs imaging system bio rad
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Molecular Imager Chemidoc Xrs Imaging System Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 80 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Bio-Rad bio rad chemidoc xrs s tatistics
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Bio Rad Chemidoc Xrs S Tatistics, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 82/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Bio-Rad chemidoc xrs gene genius bio imaging system
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Chemidoc Xrs Gene Genius Bio Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Bio-Rad bio rad chemdoc xrs imaging system
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    Bio Rad Chemdoc Xrs Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 77/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad system gel doc xr chemidoc xrs bio rad
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
    System Gel Doc Xr Chemidoc Xrs Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 82/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Bio-Rad chemidoc xrs platform
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Bio-Rad chemidoc xrs system illuminator
    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using <t>ChemiDoc</t> ™ <t>XRS</t> Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p
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    Image Search Results


    Site-specific incorporation of AzF into position 160 of Uox ( a ) Crystal structure of Uox (PDB ID: 1WS2) viewed by the PyMOL program. W160 and the active site are marked in blue and red, respectively. ( b ) MALDI-TOF spectra of Lys-C-digested fragments derived from the Uox-160AzF (top) and Uox-WT (bottom). ( c ) The fluorescence image of protein gel of Uox-160AzF and Uox-WT reacted with DBCO-Rho taken by Bio-Rad ChemiDoc™ XRS+ (excitation: 302 nm, emission: 510–610 nm).

    Journal: Scientific Reports

    Article Title: Generation of therapeutic protein variants with the human serum albumin binding capacity via site-specific fatty acid conjugation

    doi: 10.1038/s41598-017-18029-y

    Figure Lengend Snippet: Site-specific incorporation of AzF into position 160 of Uox ( a ) Crystal structure of Uox (PDB ID: 1WS2) viewed by the PyMOL program. W160 and the active site are marked in blue and red, respectively. ( b ) MALDI-TOF spectra of Lys-C-digested fragments derived from the Uox-160AzF (top) and Uox-WT (bottom). ( c ) The fluorescence image of protein gel of Uox-160AzF and Uox-WT reacted with DBCO-Rho taken by Bio-Rad ChemiDoc™ XRS+ (excitation: 302 nm, emission: 510–610 nm).

    Article Snippet: Fluorescence image of the protein gel was taken by Bio-Rad ChemiDoc™ XRS+ (Hercules, CA) followed by Coomassie staining of the gel.

    Techniques: Derivative Assay, Fluorescence

    Construction scheme and characterization of palmitic acid-conjugated Uox-160AzF ( a ) Conjugation of Uox-160AzF and the palmitic acid analog containing an azide group (azide-Pal) via SPACC using a homo-bifunctional linker (DBCO-PEG4-DBCO) ( b ) The reaction mixture of Uox-160AzF and azide-Pal was further incubated with DBCO-Rho for fluorescence analysis. Fluorescence (Fluorescence Panel; excitation: 302 nm, emission: 510–610 nm) and Coomassie-stained image (Coomassie Panel) of protein gel of Uox-160AzF (lane 1) and Uox-160AzF reacted with DBCO-PEG4-DBCO linker (lane 2) taken by Bio-Rad ChemiDoc™ XRS+. M indicates a lane for molecular weight standards. ( c ) Enzymatic activity of Uox-160Pal relative to that of Uox-WT. Error bars represent standard deviations (n = 3). Enzymatic activity of Uox-160Pal was significantly reduced when compared to Uox-WT (two-tailed student’s t-test; *Indicates p

    Journal: Scientific Reports

    Article Title: Generation of therapeutic protein variants with the human serum albumin binding capacity via site-specific fatty acid conjugation

    doi: 10.1038/s41598-017-18029-y

    Figure Lengend Snippet: Construction scheme and characterization of palmitic acid-conjugated Uox-160AzF ( a ) Conjugation of Uox-160AzF and the palmitic acid analog containing an azide group (azide-Pal) via SPACC using a homo-bifunctional linker (DBCO-PEG4-DBCO) ( b ) The reaction mixture of Uox-160AzF and azide-Pal was further incubated with DBCO-Rho for fluorescence analysis. Fluorescence (Fluorescence Panel; excitation: 302 nm, emission: 510–610 nm) and Coomassie-stained image (Coomassie Panel) of protein gel of Uox-160AzF (lane 1) and Uox-160AzF reacted with DBCO-PEG4-DBCO linker (lane 2) taken by Bio-Rad ChemiDoc™ XRS+. M indicates a lane for molecular weight standards. ( c ) Enzymatic activity of Uox-160Pal relative to that of Uox-WT. Error bars represent standard deviations (n = 3). Enzymatic activity of Uox-160Pal was significantly reduced when compared to Uox-WT (two-tailed student’s t-test; *Indicates p

    Article Snippet: Fluorescence image of the protein gel was taken by Bio-Rad ChemiDoc™ XRS+ (Hercules, CA) followed by Coomassie staining of the gel.

    Techniques: Conjugation Assay, Incubation, Fluorescence, Staining, Molecular Weight, Activity Assay, Two Tailed Test

    Comparison of fluorescence dye-conjugation yields of Uox variants. ( a ) Fluorescence (Fluorescence Panel; excitation: 302 nm, emission: 510–610 nm) and Coomassie-stained (Coomassie Panel) images of protein gels of Uox variant samples reacted with DBCO-Rho (Uox-22AzF (lane 1), Uox-23AzF (lane 3), Uox-112AzF (lane 5), Uox-138AzF (lane 7), Uox-160AzF (lane 9), and Uox-243AzF (lane 11)) and reacted with DBCO-amine followed by reaction with DBCO-Rho (Uox-22AzF (lane 2), Uox-23AzF (lane 4), Uox-112AzF (lane 6), Uox-138AzF (lane 8), Uox-160AzF (lane 10), and Uox-243AzF (lane 12)). ( b ) Fluorescence (Fluorescence Panel) and Coomassie-stained (Coomassie Panel) images of the protein gel of unreacted Uox variant (Uox-112AzF (lane 1) and Uox-160AzF (lane 4)), Uox variant reacted with DBCO-Rho (Uox-112AzF (lane 2) and Uox-160AzF (lane 5), and Uox variant reacted with DBCO-amine followed by reaction with DBCO-Rho (Uox-112AzF (lane 3) and Uox-160AzF (lane 6)). M indicates a lane for molecular weight standards. The images were taken by Bio-Rad ChemiDoc™ XRS+. The band intensities were analyzed by Image Lab software provided by Bio-Rad. Relative intensity values indicate the band intensities of Uox-112AzF samples relative to those of Uox-160AzF samples.

    Journal: Scientific Reports

    Article Title: Generation of therapeutic protein variants with the human serum albumin binding capacity via site-specific fatty acid conjugation

    doi: 10.1038/s41598-017-18029-y

    Figure Lengend Snippet: Comparison of fluorescence dye-conjugation yields of Uox variants. ( a ) Fluorescence (Fluorescence Panel; excitation: 302 nm, emission: 510–610 nm) and Coomassie-stained (Coomassie Panel) images of protein gels of Uox variant samples reacted with DBCO-Rho (Uox-22AzF (lane 1), Uox-23AzF (lane 3), Uox-112AzF (lane 5), Uox-138AzF (lane 7), Uox-160AzF (lane 9), and Uox-243AzF (lane 11)) and reacted with DBCO-amine followed by reaction with DBCO-Rho (Uox-22AzF (lane 2), Uox-23AzF (lane 4), Uox-112AzF (lane 6), Uox-138AzF (lane 8), Uox-160AzF (lane 10), and Uox-243AzF (lane 12)). ( b ) Fluorescence (Fluorescence Panel) and Coomassie-stained (Coomassie Panel) images of the protein gel of unreacted Uox variant (Uox-112AzF (lane 1) and Uox-160AzF (lane 4)), Uox variant reacted with DBCO-Rho (Uox-112AzF (lane 2) and Uox-160AzF (lane 5), and Uox variant reacted with DBCO-amine followed by reaction with DBCO-Rho (Uox-112AzF (lane 3) and Uox-160AzF (lane 6)). M indicates a lane for molecular weight standards. The images were taken by Bio-Rad ChemiDoc™ XRS+. The band intensities were analyzed by Image Lab software provided by Bio-Rad. Relative intensity values indicate the band intensities of Uox-112AzF samples relative to those of Uox-160AzF samples.

    Article Snippet: Fluorescence image of the protein gel was taken by Bio-Rad ChemiDoc™ XRS+ (Hercules, CA) followed by Coomassie staining of the gel.

    Techniques: Fluorescence, Conjugation Assay, Staining, Variant Assay, Molecular Weight, Software

    Effects of H 2 O 2 exposure on the T. bernacchii 26S proteasome ( A ) Native-PAGE of T. bernacchii 26S proteasome complex after treatment with H 2 O 2 . Purified 26S proteasome was exposed to increasing H 2 O 2 concentrations for 24 h at 37°C and the bands were visualized by Coomassie-blue stained. The experimental conditions for H 2 O 2 treatment and native-PAGE are described in Materials and Methods section. ( B, left panel ) Unoxidized and oxidized BSA were incubated with 26S proteasome at 37°C for the indicated periods; ( B, right panel ) Unoxidized and oxidized BSA were incubated with H 2 O 2 -treated 26S proteasome at 37°C for the indicated periods. All the reaction mixtures were subjected to SDS/PAGE. ( C ) SDS/PAGE data are expressed as percentage density of BSA at the indicated incubation times compared with time 0, and were obtained by densitometric analysis with ChemiDoc XRS and Quantity One software. Oxidized BSA levels after incubation with 26S and H 2 O 2 -treated 26S are indicated by diamonds and squares respectively. Unoxidized BSA incubated with 26S and H 2 O 2 -treated 26S are indicated by triangles and circles respectively. The experiments were performed in duplicate on two different protein preparations, and the average of the relative intensities of measurements, performed in triplicate, are expressed as means ± standard deviations.

    Journal: Bioscience Reports

    Article Title: Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii

    doi: 10.1042/BSR20160022

    Figure Lengend Snippet: Effects of H 2 O 2 exposure on the T. bernacchii 26S proteasome ( A ) Native-PAGE of T. bernacchii 26S proteasome complex after treatment with H 2 O 2 . Purified 26S proteasome was exposed to increasing H 2 O 2 concentrations for 24 h at 37°C and the bands were visualized by Coomassie-blue stained. The experimental conditions for H 2 O 2 treatment and native-PAGE are described in Materials and Methods section. ( B, left panel ) Unoxidized and oxidized BSA were incubated with 26S proteasome at 37°C for the indicated periods; ( B, right panel ) Unoxidized and oxidized BSA were incubated with H 2 O 2 -treated 26S proteasome at 37°C for the indicated periods. All the reaction mixtures were subjected to SDS/PAGE. ( C ) SDS/PAGE data are expressed as percentage density of BSA at the indicated incubation times compared with time 0, and were obtained by densitometric analysis with ChemiDoc XRS and Quantity One software. Oxidized BSA levels after incubation with 26S and H 2 O 2 -treated 26S are indicated by diamonds and squares respectively. Unoxidized BSA incubated with 26S and H 2 O 2 -treated 26S are indicated by triangles and circles respectively. The experiments were performed in duplicate on two different protein preparations, and the average of the relative intensities of measurements, performed in triplicate, are expressed as means ± standard deviations.

    Article Snippet: Enhanced chemiluminescence and autoradiography (Amersham Biosciences) were used to displayed immune complexes formed and measured by densitometry analysis with ChemiDoc XRS (Bio-Rad Laboratories).

    Techniques: Clear Native PAGE, Purification, Staining, Incubation, SDS Page, Software

    Half-life of CrcZ produced from plasmid p424-Z in cells with CrcZ-null, Hfq-null, or Crc-null genetic backgrounds. ( A − C ) P. putida strains KT2440-Z (Δ crcZ ), KT2440Δ hfq (Δ hfq ), and KTCRC (Δ crc ) were cultured in LB medium with streptomycin and 1 mM IPTG. At a turbidity of 0.6 (A 600 ), rifampicin was added to stop transcription. Aliquots were withdrawn at 0, 2, 4, 8, 16, and 32 min post-rifampicin addition, total RNA was isolated, resolved on a 6% polyacrylamide/7 M urea gel, and CrcZ and 5S rRNA detected by Northern blot with specific probes. Band intensities were quantified using a ChemiDoc XRS imager and Image Lab software (Bio-Rad). Values obtained for the larger (primary CrcZ transcript) or shorter bands (processed CrcZ transcript) detected with the CrcZ probe were normalized to those of the 5S rRNA of the corresponding sample. ( D , E ) Plots show the values for each time point expressed relative to that at time 0. Processed CrcZ was not detected in the Δ hfq strain. Data shown as mean ± SD for three independent assays.

    Journal: RNA

    Article Title: Effect of Crc and Hfq proteins on the transcription, processing, and stability of the Pseudomonas putida CrcZ sRNA

    doi: 10.1261/rna.058313.116

    Figure Lengend Snippet: Half-life of CrcZ produced from plasmid p424-Z in cells with CrcZ-null, Hfq-null, or Crc-null genetic backgrounds. ( A − C ) P. putida strains KT2440-Z (Δ crcZ ), KT2440Δ hfq (Δ hfq ), and KTCRC (Δ crc ) were cultured in LB medium with streptomycin and 1 mM IPTG. At a turbidity of 0.6 (A 600 ), rifampicin was added to stop transcription. Aliquots were withdrawn at 0, 2, 4, 8, 16, and 32 min post-rifampicin addition, total RNA was isolated, resolved on a 6% polyacrylamide/7 M urea gel, and CrcZ and 5S rRNA detected by Northern blot with specific probes. Band intensities were quantified using a ChemiDoc XRS imager and Image Lab software (Bio-Rad). Values obtained for the larger (primary CrcZ transcript) or shorter bands (processed CrcZ transcript) detected with the CrcZ probe were normalized to those of the 5S rRNA of the corresponding sample. ( D , E ) Plots show the values for each time point expressed relative to that at time 0. Processed CrcZ was not detected in the Δ hfq strain. Data shown as mean ± SD for three independent assays.

    Article Snippet: Band intensities were quantified using a ChemiDoc XRS imager and Image Lab software (Bio-Rad).

    Techniques: Produced, Plasmid Preparation, Cell Culture, Isolation, Northern Blot, Software

    Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.

    Journal: Scientific Reports

    Article Title: Bacterial periplasmic nitrate and trimethylamine-N-oxide respiration coupled to menaquinol-cytochrome c reductase (Qcr): Implications for electrogenic reduction of alternative electron acceptors

    doi: 10.1038/s41598-018-33857-2

    Figure Lengend Snippet: Construction and verification of a qcrABC deletion mutant. ( A ) Mutagenesis strategy. The majority of the coding regions of the qcrA-C genes were replaced with a kanamycin resistance cassette with its own promoter. The downstream cfa gene has its own promoter, but the cassette has no terminator and so should be non-polar on cfa . ( B ) RT-PCR to verify expression of cfa gene and absence of qcr gene transcription in the qcrABC mutant. Fold-change in the mutant is shown relative to the wild type strain, using gyrA gene as a control. The difference between expression of the cfa gene in mutant and wild-type was not significant by t-test. ( C ) shows a comparison of the membrane associated c -type cytochromes revealed after a total membrane preparation was subjected to SDS-PAGE and electroblotting to a nitrocellulose membrane, followed by staining for haem-associated peroxidase activity using the chemiluminescence technique described in Methods. 20 μg total protein was run per lane. The Image shown is a cropped version of the full-size blot that can viewed in Supplementary Fig. 1 , and was obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min. A band corresponding to the expected size of QcrC is missing in the qcrABC deletion mutant.

    Article Snippet: Images were obtained using a ChemiDoc XRS system (BioRad Inc) with an exposure time of 2 min.

    Techniques: Mutagenesis, Reverse Transcription Polymerase Chain Reaction, Expressing, SDS Page, Staining, Activity Assay

    Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using ChemiDoc ™ XRS Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p

    Journal: Scientific Reports

    Article Title: Mitragynine, an euphoric compound inhibits hERG1a/1b channel current and upregulates the complexation of hERG1a-Hsp90 in HEK293-hERG1a/1b cells

    doi: 10.1038/s41598-019-56106-6

    Figure Lengend Snippet: Densitometric scanning analysis and representative images of Western blot analysis for the protein expression of Hsp70 and Hsp90 following treatment with arsenic trioxide and mitragynine for 24 h. The effects of arsenic trioxide and mitragynine on the expression levels of endogenous ( A ) Hsp70 and ( B ) Hsp90. Densitometric scanning analysis and representative images for the protein expression of cg-hERG1a immunoprecipitated with anti-Hsp70 (IP-Hsp70) or anti-Hsp90 (IP-Hsp90) normalized against cg-hERG1a immunoprecipitated with anti-hERG1 (IP-hERG1) and relative to untreated control. The effects of arsenic trioxide and mitragynine on the interaction between cg-hERG1a (135 kDa) with ( C ) Hsp70 and ( D ) Hsp90. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using ChemiDoc ™ XRS Imaging System (Bio-Rad Laboratories Inc, USA). Hsp70 bands were detected with exposure time of 1.5 s, whereas β-actin bands were detected with exposure time of 10 s, meanwhile both Hsp90 β-actin were detected with the exposure time of 7.6 s. For IP-hERG1, total protein lysates and proteins of interest were run on the same gel and blot with different exposure times for the proteins of interest (11 s) and total protein lysates (5 s). Data are presented as mean fold change ± SD of three independent experiments. * p

    Article Snippet: Chemiluminescence signal was detected using ChemiDoc™ XRS Imaging System (Bio-Rad Laboratories, USA).

    Techniques: Western Blot, Expressing, Immunoprecipitation, Electrophoresis, Molecular Weight, Marker, Incubation, Imaging

    The effects of ( A,B ) arsenic trioxide and ( C,D ) mitragynine on the hERG1a/1b protein expression. Representative image of Western blot analysis for the protein expression of hERG1a (155 kDa and 135 kDa), hERG1b (95 kDa and 80 kDa) and β-actin (43 kDa) following treatment with arsenic trioxide or mitragynine for 24 h. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using ChemiDoc TM XRS Imaging System (Bio-Rad Laboratories Inc, USA). For ( B ) hERG1a β-actin, the exposure time was 24 s, meanwhile for hERG1b β-actin, the exposure time was 111 s. As for ( D ) hERG1a β-actin, the exposure time was 16 s, meanwhile, for hERG1b and β-actin, the exposure time were 206 s and 32 s respectively. Densitometric scanning analyses for the protein expression of hERG1a (155 kDa and 135 kDa) and hERG1b (95 kDa and 80 kDa) are normalized against actin and relative to the untreated control. Densitometric data are presented as mean fold change ± SD of three independent experiments. *p

    Journal: Scientific Reports

    Article Title: Mitragynine, an euphoric compound inhibits hERG1a/1b channel current and upregulates the complexation of hERG1a-Hsp90 in HEK293-hERG1a/1b cells

    doi: 10.1038/s41598-019-56106-6

    Figure Lengend Snippet: The effects of ( A,B ) arsenic trioxide and ( C,D ) mitragynine on the hERG1a/1b protein expression. Representative image of Western blot analysis for the protein expression of hERG1a (155 kDa and 135 kDa), hERG1b (95 kDa and 80 kDa) and β-actin (43 kDa) following treatment with arsenic trioxide or mitragynine for 24 h. Electrophoresis was carried out at 150 V for 90 min and the protein bands were then transferred to a single PVDF membrane at 1.0 A and 25 V for 30 min. The protein of interest and the internal control of protein loading, β-actin (43 kDa), were separated by cutting the membrane at around 50 kDa using the molecular weight marker as reference. The separated membranes were then placed in different containers and incubated with respective antibodies. After immunoblotting, the separated membranes were placed together and visualized using ChemiDoc TM XRS Imaging System (Bio-Rad Laboratories Inc, USA). For ( B ) hERG1a β-actin, the exposure time was 24 s, meanwhile for hERG1b β-actin, the exposure time was 111 s. As for ( D ) hERG1a β-actin, the exposure time was 16 s, meanwhile, for hERG1b and β-actin, the exposure time were 206 s and 32 s respectively. Densitometric scanning analyses for the protein expression of hERG1a (155 kDa and 135 kDa) and hERG1b (95 kDa and 80 kDa) are normalized against actin and relative to the untreated control. Densitometric data are presented as mean fold change ± SD of three independent experiments. *p

    Article Snippet: Chemiluminescence signal was detected using ChemiDoc™ XRS Imaging System (Bio-Rad Laboratories, USA).

    Techniques: Expressing, Western Blot, Electrophoresis, Molecular Weight, Marker, Incubation, Imaging