recombinant g6pd protein  (OriGene)


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    Structured Review

    OriGene recombinant g6pd protein
    Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase <t>(G6PD)</t> is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.
    Recombinant G6pd Protein, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant g6pd protein/product/OriGene
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant g6pd protein - by Bioz Stars, 2024-07
    90/100 stars

    Images

    1) Product Images from "Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites"

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2016.5449

    Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase (G6PD) is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.
    Figure Legend Snippet: Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase (G6PD) is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.

    Techniques Used: Immunoprecipitation

    Effects of aspirin on glucose-6-phosphate dehydrogenase (G6PD) activity in HCT 116 and HT-29 cells. Cells were cultured and left untreated or were treated with aspirin for 24 h. Protein (100 µ g) was used to conduct a G6PD assay. The reaction mixture was incubated at 37°C for 30 min, and absorbance was measured at 450 nm. G6PD activity was expressed as a percentage of control. The experiments were repeated three times. Data are represented as mean ± standard deviation. * P<0.05, ** P<0.01, *** P<0.001 vs. the control.
    Figure Legend Snippet: Effects of aspirin on glucose-6-phosphate dehydrogenase (G6PD) activity in HCT 116 and HT-29 cells. Cells were cultured and left untreated or were treated with aspirin for 24 h. Protein (100 µ g) was used to conduct a G6PD assay. The reaction mixture was incubated at 37°C for 30 min, and absorbance was measured at 450 nm. G6PD activity was expressed as a percentage of control. The experiments were repeated three times. Data are represented as mean ± standard deviation. * P<0.05, ** P<0.01, *** P<0.001 vs. the control.

    Techniques Used: Activity Assay, Cell Culture, G6PD Assay, Incubation, Standard Deviation

    Mass spectrometry (MS) analysis of recombinant glucose-6-phosphate dehydrogenase (G6PD) isoform a . In vitro acetylation of recombinant G6PD by aspirin. (A) A total of 5 ng in vitro acetylated recombinant G6PD was immunoblotted with anti-acetyl lysine antibody and the protein band was detected by enhanced chemiluminescence. (B-D) MS/MS fragmentation spectra showing acetyl modification of (B) K77, (C) K201 and (D) K235.
    Figure Legend Snippet: Mass spectrometry (MS) analysis of recombinant glucose-6-phosphate dehydrogenase (G6PD) isoform a . In vitro acetylation of recombinant G6PD by aspirin. (A) A total of 5 ng in vitro acetylated recombinant G6PD was immunoblotted with anti-acetyl lysine antibody and the protein band was detected by enhanced chemiluminescence. (B-D) MS/MS fragmentation spectra showing acetyl modification of (B) K77, (C) K201 and (D) K235.

    Techniques Used: Mass Spectrometry, Recombinant, In Vitro, Tandem Mass Spectroscopy, Modification


    Figure Legend Snippet: Aspirin-acetylated peptides identified from glucose-6-phosphate dehydrogenase after trypsin and chymotrypsin digestion.

    Techniques Used:

    Location of aspirin-acetylated lysine residues identified in the present study and the naturally acetylated lysines on  G6PD  ( <xref ref-type= 25 )." title="... present study and the naturally acetylated lysines on G6PD ( 25 ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Location of aspirin-acetylated lysine residues identified in the present study and the naturally acetylated lysines on G6PD ( 25 ).

    Techniques Used:

    3-Dimension space-filling model of recombinant glucose-6-phosphate dehydrogenase (G6PD; NP_000393), is shown. The location of aspirin-acetylated lysine residues are highlighted in blue (K77, K112, K119, K201, K235, K390, K396, K416, K438, K459, K462, K527, K538, K544).
    Figure Legend Snippet: 3-Dimension space-filling model of recombinant glucose-6-phosphate dehydrogenase (G6PD; NP_000393), is shown. The location of aspirin-acetylated lysine residues are highlighted in blue (K77, K112, K119, K201, K235, K390, K396, K416, K438, K459, K462, K527, K538, K544).

    Techniques Used: Recombinant

    recombinant g6pd protein  (OriGene)


    Bioz Verified Symbol OriGene is a verified supplier
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  • 86

    Structured Review

    OriGene recombinant g6pd protein
    Recombinant G6pd Protein, supplied by OriGene, 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/recombinant g6pd protein/product/OriGene
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant g6pd protein - by Bioz Stars, 2024-07
    86/100 stars

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    recombinant g6pd protein  (OriGene)


    Bioz Verified Symbol OriGene is a verified supplier
    Bioz Manufacturer Symbol OriGene manufactures this product  
  • Logo
  • About
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  • 90

    Structured Review

    OriGene recombinant g6pd protein
    Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase <t>(G6PD)</t> is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.
    Recombinant G6pd Protein, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant g6pd protein/product/OriGene
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant g6pd protein - by Bioz Stars, 2024-07
    90/100 stars

    Images

    1) Product Images from "Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites"

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    Journal: Molecular Medicine Reports

    doi: 10.3892/mmr.2016.5449

    Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase (G6PD) is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.
    Figure Legend Snippet: Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase (G6PD) is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.

    Techniques Used: Immunoprecipitation

    Effects of aspirin on glucose-6-phosphate dehydrogenase (G6PD) activity in HCT 116 and HT-29 cells. Cells were cultured and left untreated or were treated with aspirin for 24 h. Protein (100 µ g) was used to conduct a G6PD assay. The reaction mixture was incubated at 37°C for 30 min, and absorbance was measured at 450 nm. G6PD activity was expressed as a percentage of control. The experiments were repeated three times. Data are represented as mean ± standard deviation. * P<0.05, ** P<0.01, *** P<0.001 vs. the control.
    Figure Legend Snippet: Effects of aspirin on glucose-6-phosphate dehydrogenase (G6PD) activity in HCT 116 and HT-29 cells. Cells were cultured and left untreated or were treated with aspirin for 24 h. Protein (100 µ g) was used to conduct a G6PD assay. The reaction mixture was incubated at 37°C for 30 min, and absorbance was measured at 450 nm. G6PD activity was expressed as a percentage of control. The experiments were repeated three times. Data are represented as mean ± standard deviation. * P<0.05, ** P<0.01, *** P<0.001 vs. the control.

    Techniques Used: Activity Assay, Cell Culture, G6PD Assay, Incubation, Standard Deviation

    Mass spectrometry (MS) analysis of recombinant glucose-6-phosphate dehydrogenase (G6PD) isoform a . In vitro acetylation of recombinant G6PD by aspirin. (A) A total of 5 ng in vitro acetylated recombinant G6PD was immunoblotted with anti-acetyl lysine antibody and the protein band was detected by enhanced chemiluminescence. (B-D) MS/MS fragmentation spectra showing acetyl modification of (B) K77, (C) K201 and (D) K235.
    Figure Legend Snippet: Mass spectrometry (MS) analysis of recombinant glucose-6-phosphate dehydrogenase (G6PD) isoform a . In vitro acetylation of recombinant G6PD by aspirin. (A) A total of 5 ng in vitro acetylated recombinant G6PD was immunoblotted with anti-acetyl lysine antibody and the protein band was detected by enhanced chemiluminescence. (B-D) MS/MS fragmentation spectra showing acetyl modification of (B) K77, (C) K201 and (D) K235.

    Techniques Used: Mass Spectrometry, Recombinant, In Vitro, Tandem Mass Spectroscopy, Modification


    Figure Legend Snippet: Aspirin-acetylated peptides identified from glucose-6-phosphate dehydrogenase after trypsin and chymotrypsin digestion.

    Techniques Used:

    Location of aspirin-acetylated lysine residues identified in the present study and the naturally acetylated lysines on  G6PD  ( <xref ref-type= 25 )." title="... present study and the naturally acetylated lysines on G6PD ( 25 ..." property="contentUrl" width="100%" height="100%"/>
    Figure Legend Snippet: Location of aspirin-acetylated lysine residues identified in the present study and the naturally acetylated lysines on G6PD ( 25 ).

    Techniques Used:

    3-Dimension space-filling model of recombinant glucose-6-phosphate dehydrogenase (G6PD; NP_000393), is shown. The location of aspirin-acetylated lysine residues are highlighted in blue (K77, K112, K119, K201, K235, K390, K396, K416, K438, K459, K462, K527, K538, K544).
    Figure Legend Snippet: 3-Dimension space-filling model of recombinant glucose-6-phosphate dehydrogenase (G6PD; NP_000393), is shown. The location of aspirin-acetylated lysine residues are highlighted in blue (K77, K112, K119, K201, K235, K390, K396, K416, K438, K459, K462, K527, K538, K544).

    Techniques Used: Recombinant

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    OriGene recombinant g6pd protein
    Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase <t>(G6PD)</t> is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.
    Recombinant G6pd Protein, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant g6pd protein/product/OriGene
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    recombinant g6pd protein - by Bioz Stars, 2024-07
    90/100 stars
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    Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase (G6PD) is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.

    Journal: Molecular Medicine Reports

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    doi: 10.3892/mmr.2016.5449

    Figure Lengend Snippet: Aspirin-mediated acetylation of glucose-6-phosphate dehydrogenase (G6PD) is greater in (A) HCT 116 cells compared with in (B) HT-29 cells. Subconfluent cells were left untreated or were treated with aspirin for 24 h, lysates were prepared, and equal amounts of protein were immunoprecipitated with rabbit agarose-conjugated anti-acetyl lysine antibody. Agarose-bound proteins were eluted and immunoblotted with anti-G6PD antibody. (C) HCT-116 and (D) HT-29 samples were immunoblotted with anti-G6PD antibody. The experiments were repeated three times.

    Article Snippet: The recombinant G6PD protein (isoform a ) was obtained from Origene Technologies, Inc. (Rockville, MD, USA).

    Techniques: Immunoprecipitation

    Effects of aspirin on glucose-6-phosphate dehydrogenase (G6PD) activity in HCT 116 and HT-29 cells. Cells were cultured and left untreated or were treated with aspirin for 24 h. Protein (100 µ g) was used to conduct a G6PD assay. The reaction mixture was incubated at 37°C for 30 min, and absorbance was measured at 450 nm. G6PD activity was expressed as a percentage of control. The experiments were repeated three times. Data are represented as mean ± standard deviation. * P<0.05, ** P<0.01, *** P<0.001 vs. the control.

    Journal: Molecular Medicine Reports

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    doi: 10.3892/mmr.2016.5449

    Figure Lengend Snippet: Effects of aspirin on glucose-6-phosphate dehydrogenase (G6PD) activity in HCT 116 and HT-29 cells. Cells were cultured and left untreated or were treated with aspirin for 24 h. Protein (100 µ g) was used to conduct a G6PD assay. The reaction mixture was incubated at 37°C for 30 min, and absorbance was measured at 450 nm. G6PD activity was expressed as a percentage of control. The experiments were repeated three times. Data are represented as mean ± standard deviation. * P<0.05, ** P<0.01, *** P<0.001 vs. the control.

    Article Snippet: The recombinant G6PD protein (isoform a ) was obtained from Origene Technologies, Inc. (Rockville, MD, USA).

    Techniques: Activity Assay, Cell Culture, G6PD Assay, Incubation, Standard Deviation

    Mass spectrometry (MS) analysis of recombinant glucose-6-phosphate dehydrogenase (G6PD) isoform a . In vitro acetylation of recombinant G6PD by aspirin. (A) A total of 5 ng in vitro acetylated recombinant G6PD was immunoblotted with anti-acetyl lysine antibody and the protein band was detected by enhanced chemiluminescence. (B-D) MS/MS fragmentation spectra showing acetyl modification of (B) K77, (C) K201 and (D) K235.

    Journal: Molecular Medicine Reports

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    doi: 10.3892/mmr.2016.5449

    Figure Lengend Snippet: Mass spectrometry (MS) analysis of recombinant glucose-6-phosphate dehydrogenase (G6PD) isoform a . In vitro acetylation of recombinant G6PD by aspirin. (A) A total of 5 ng in vitro acetylated recombinant G6PD was immunoblotted with anti-acetyl lysine antibody and the protein band was detected by enhanced chemiluminescence. (B-D) MS/MS fragmentation spectra showing acetyl modification of (B) K77, (C) K201 and (D) K235.

    Article Snippet: The recombinant G6PD protein (isoform a ) was obtained from Origene Technologies, Inc. (Rockville, MD, USA).

    Techniques: Mass Spectrometry, Recombinant, In Vitro, Tandem Mass Spectroscopy, Modification

    Journal: Molecular Medicine Reports

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    doi: 10.3892/mmr.2016.5449

    Figure Lengend Snippet: Aspirin-acetylated peptides identified from glucose-6-phosphate dehydrogenase after trypsin and chymotrypsin digestion.

    Article Snippet: The recombinant G6PD protein (isoform a ) was obtained from Origene Technologies, Inc. (Rockville, MD, USA).

    Techniques:

    Location of aspirin-acetylated lysine residues identified in the present study and the naturally acetylated lysines on  G6PD  ( <xref ref-type= 25 )." width="100%" height="100%">

    Journal: Molecular Medicine Reports

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    doi: 10.3892/mmr.2016.5449

    Figure Lengend Snippet: Location of aspirin-acetylated lysine residues identified in the present study and the naturally acetylated lysines on G6PD ( 25 ).

    Article Snippet: The recombinant G6PD protein (isoform a ) was obtained from Origene Technologies, Inc. (Rockville, MD, USA).

    Techniques:

    3-Dimension space-filling model of recombinant glucose-6-phosphate dehydrogenase (G6PD; NP_000393), is shown. The location of aspirin-acetylated lysine residues are highlighted in blue (K77, K112, K119, K201, K235, K390, K396, K416, K438, K459, K462, K527, K538, K544).

    Journal: Molecular Medicine Reports

    Article Title: Aspirin inhibits glucose-6-phosphate dehydrogenase activity in HCT 116 cells through acetylation: Identification of aspirin-acetylated sites

    doi: 10.3892/mmr.2016.5449

    Figure Lengend Snippet: 3-Dimension space-filling model of recombinant glucose-6-phosphate dehydrogenase (G6PD; NP_000393), is shown. The location of aspirin-acetylated lysine residues are highlighted in blue (K77, K112, K119, K201, K235, K390, K396, K416, K438, K459, K462, K527, K538, K544).

    Article Snippet: The recombinant G6PD protein (isoform a ) was obtained from Origene Technologies, Inc. (Rockville, MD, USA).

    Techniques: Recombinant