chemidoc xrs + Bio Rad Search Results


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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 1330 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 99 stars, based on 1330 article reviews
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    bio rad chemidoc xrs - by Bioz Stars, 2020-02
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    93
    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: 93/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bio rad chemidoc xrs - by Bioz Stars, 2020-02
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    99
    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: 99/100, based on 30 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    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: 99/100, based on 53 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    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: 99/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Bio-Rad chemidoc xrs system bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Chemidoc Xrs System Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 345 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad chemidoc xrs imaging system bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Chemidoc Xrs Imaging System Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Bio-Rad bio rad chemidoc xr
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Bio Rad Chemidoc Xr, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 87/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Bio-Rad image analysis system chemidoc xrs bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Image Analysis System Chemidoc Xrs Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 78/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Bio-Rad microscope bio rad chemidoc xrs
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Microscope Bio Rad Chemidoc Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Bio-Rad chemidoc xrs plus luminescent image analyser bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Chemidoc Xrs Plus Luminescent Image Analyser Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 80/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad molecular imager chemidoc xrs imaging system bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Molecular Imager Chemidoc Xrs Imaging System Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 80 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Bio-Rad bio rad chemidoc xrs s tatistics
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Bio Rad Chemidoc Xrs S Tatistics, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad chemidoc xrs gene genius bio imaging system
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Chemidoc Xrs Gene Genius Bio Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, 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
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    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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    91
    Bio-Rad system gel doc xr chemidoc xrs bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    System Gel Doc Xr Chemidoc Xrs Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 56 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    84
    Bio-Rad equivalent rocking platform bio rad chemidoc xrs
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Equivalent Rocking Platform Bio Rad Chemidoc Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 84/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Bio-Rad densitometry bio rad chemidoc xrs system
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Densitometry Bio Rad Chemidoc Xrs System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 95/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Bio-Rad microwave rocker bio rad chemidoc xrs
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Microwave Rocker Bio Rad Chemidoc Xrs, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Bio-Rad gel imaging system chemidox xrs bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Gel Imaging System Chemidox Xrs Bio Rad, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 80/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Bio-Rad molecular imager chemidoc xrs system bio rad station
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
    Molecular Imager Chemidoc Xrs System Bio Rad Station, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 80/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad chemidoc xrs plus luminescent image analyzer bio rad
    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the <t>ChemiDoc</t> <t>XRS+</t> System (BioRad).
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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

    Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

    Journal: PLoS Neglected Tropical Diseases

    Article Title: Muscle Tissue Damage Induced by the Venom of Bothrops asper: Identification of Early and Late Pathological Events through Proteomic Analysis

    doi: 10.1371/journal.pntd.0004599

    Figure Lengend Snippet: Western blot analysis of extracellular matrix components in wound exudates collected from mice after injection of B . asper venom. Groups of five mice were injected in the gastrocnemius with 50 μg of B . asper venom. After 1, 6 and 24 h of injection mice were sacrificed and samples of exudates were collected, pooled and lyophilized. Afterwards, 100 μg of protein of each sample were separated under reducing conditions on 4–15% Tris–HCl SDS-PAGE, and transferred to nitrocellulose membranes. Immunodetection was performed with (A) anti-type IV collagen (Col IV), (B) anti-laminin, (C) anti-nidogen 1, (D) anti-type I collagen (Col I), (E) anti-type VI collagen (Col VI), and (F) anti-fibronectin. The reaction was detected using an anti-rabbit peroxidase antibody and a chemiluminescent substrate. Images were obtained with the ChemiDoc XRS+ System (BioRad).

    Article Snippet: Images were captured with the ChemiDoc XRS+ System (BioRad) and the analysis was performed with the ImageLab software (BioRad).

    Techniques: Western Blot, Mouse Assay, Injection, SDS Page, Immunodetection