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  • 99
    Shimadzu Corporation hplc system
    Hplc System, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hplc system/product/Shimadzu Corporation
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hplc system - by Bioz Stars, 2021-03
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    86
    Agilent technologies 1100 hplc system
    ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography <t>(HPLC)</t> on an Agilent <t>1100</t> HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.
    1100 Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/1100 hplc system/product/Agilent technologies
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    1100 hplc system - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    99
    Agilent technologies hplc
    ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography <t>(HPLC)</t> on an Agilent <t>1100</t> HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.
    Hplc, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hplc/product/Agilent technologies
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hplc - by Bioz Stars, 2021-03
    99/100 stars
      Buy from Supplier

    86
    Agilent technologies hplc system
    Purification and analysis of aFGF. a The overall purification steps. b SDS-PAGE analysis of samples from each purification step. c <t>C18</t> <t>RP-HPLC</t> trace. d LC–MS (Q-TOF) analysis. M: marker; Lys: supernatant after sonication; 1: HisTrap purification; 2: after TEV protease treatment (the band at 28 kDa is TEVp); 3: HisTrap purification; 4: HiTrap CM purification (final product). The data are representative of three replicated experiments
    Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hplc system/product/Agilent technologies
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    hplc system - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    Image Search Results


    ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography (HPLC) on an Agilent 1100 HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.

    Journal: International Journal of Molecular Sciences

    Article Title: Non-Native Conformational Isomers of the Catalytic Domain of PCSK9 Induce an Immune Response, Reduce Lipids and Increase LDL Receptor Levels

    doi: 10.3390/ijms19020640

    Figure Lengend Snippet: ( A ) Coomassie blue staining of the purified region-1 and region-2 of mPCSK9 proteins. Region-1 (residues 152–351) and region-2 (residues 249–452) of mouse catalytic domain were cloned and expressed by pET-3a plasmids. The proteins were reduced and purified by a reverse-phase high-performance liquid chromatography (HPLC) on an Agilent 1100 HPLC system. The purified proteins were analyzed by SDS/PAGE and stained with Coomassie blue. The positions of expressed proteins are shown; ( B ) MALDI mass spectrometry on Region-1. The molecular mass of purified PCSK9 region-1 in fully reduced form (PCSK9-1R). The molecular mass of PCSK9 region-1 as determined by MALDI was 21,201 Da; ( C ) MALDI mass spectrometry on Region-2. The molecular mass of purified PCSK9 region-2 in fully reduced form (PCSK9-2R). The molecular mass of PCSK9 region-2 as determined by MALDI was 21,355 Da.

    Article Snippet: The authors used a reverse-phase high-performance liquid chromatography (HPLC) on an Agilent 1100 HPLC system (Column ZORBAX 3000 SB-C18, 9.4 mm × 25 cm) to purify the proteins.

    Techniques: Staining, Purification, Clone Assay, Positron Emission Tomography, High Performance Liquid Chromatography, SDS Page, Mass Spectrometry

    Purification and analysis of aFGF. a The overall purification steps. b SDS-PAGE analysis of samples from each purification step. c C18 RP-HPLC trace. d LC–MS (Q-TOF) analysis. M: marker; Lys: supernatant after sonication; 1: HisTrap purification; 2: after TEV protease treatment (the band at 28 kDa is TEVp); 3: HisTrap purification; 4: HiTrap CM purification (final product). The data are representative of three replicated experiments

    Journal: Microbial Cell Factories

    Article Title: Effective production of human growth factors in Escherichia coli by fusing with small protein 6HFh8

    doi: 10.1186/s12934-020-01502-1

    Figure Lengend Snippet: Purification and analysis of aFGF. a The overall purification steps. b SDS-PAGE analysis of samples from each purification step. c C18 RP-HPLC trace. d LC–MS (Q-TOF) analysis. M: marker; Lys: supernatant after sonication; 1: HisTrap purification; 2: after TEV protease treatment (the band at 28 kDa is TEVp); 3: HisTrap purification; 4: HiTrap CM purification (final product). The data are representative of three replicated experiments

    Article Snippet: The C18 RP column (Zorbax Eclipse XDB, 80 Å C18, 4.6 × 150 mm, 5 μm; Agilent Technologies) connected to an HPLC system was maintained at 40 °C.

    Techniques: Purification, SDS Page, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Marker, Sonication

    Purification and analysis of VEGF165. a The overall purification steps. b SDS-PAGE analysis of samples from each purification step. c C18 RP-HPLC trace. d LC–MS (Q-TOF) analysis. M: marker; Lys: supernatant after sonication; 1: HisTrap purification; 2: after TEV protease treatment (the band at 28 kDa is TEVp); 3: HiTrap SP purification; 4: HisTrap purification; 5: HiTrap SP purification (final product). The data are representative of three replicated experiments

    Journal: Microbial Cell Factories

    Article Title: Effective production of human growth factors in Escherichia coli by fusing with small protein 6HFh8

    doi: 10.1186/s12934-020-01502-1

    Figure Lengend Snippet: Purification and analysis of VEGF165. a The overall purification steps. b SDS-PAGE analysis of samples from each purification step. c C18 RP-HPLC trace. d LC–MS (Q-TOF) analysis. M: marker; Lys: supernatant after sonication; 1: HisTrap purification; 2: after TEV protease treatment (the band at 28 kDa is TEVp); 3: HiTrap SP purification; 4: HisTrap purification; 5: HiTrap SP purification (final product). The data are representative of three replicated experiments

    Article Snippet: The C18 RP column (Zorbax Eclipse XDB, 80 Å C18, 4.6 × 150 mm, 5 μm; Agilent Technologies) connected to an HPLC system was maintained at 40 °C.

    Techniques: Purification, SDS Page, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Marker, Sonication