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rabbit polyclonal anti p62  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology rabbit polyclonal anti p62
    Fn14-positive vesicles accumulate in a TWEAK-dependent manner upon Atg8s inactivation by dominant-negative ATG4B. a – f WT or ATG4B DN stable expression HeLa cells were assayed as follows: a treated with TWK for indicated times, immunostained for Fn14 and TRAF2, and analyzed by confocal microscopy (scale bar, 20 µm); b treated with TWK and subjected to membrane floatation assay as detailed under Methods; c transfected with luciferase expression constructs as detailed under Methods, treated with TWK as indicated, and further subjected to luciferase assay as detailed to assess NF-kB activity (* P < 0.05, n = 3 biological repeats; comparisons by T test; mean ± s.e.m.). The vertical line represents control in the absence of TWK; d subjected to Proteinase protection assay (upper panel) as detailed under Methods and schematically depicted (lower panel). e , f transfected with si NT or siRNA against <t>p62</t> (si p62 ) and treated with TWK, extracted proteins were immunoblotted ( e ) or cells were immunostained for Fn14 and analyzed by confocal microscopy (scale bar, 20 µm) ( f )
    Rabbit Polyclonal Anti P62, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 136 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Autophagy differentially regulates TNF receptor Fn14 by distinct mammalian Atg8 proteins"

    Article Title: Autophagy differentially regulates TNF receptor Fn14 by distinct mammalian Atg8 proteins

    Journal: Nature Communications

    doi: 10.1038/s41467-018-06275-1

    Fn14-positive vesicles accumulate in a TWEAK-dependent manner upon Atg8s inactivation by dominant-negative ATG4B. a – f WT or ATG4B DN stable expression HeLa cells were assayed as follows: a treated with TWK for indicated times, immunostained for Fn14 and TRAF2, and analyzed by confocal microscopy (scale bar, 20 µm); b treated with TWK and subjected to membrane floatation assay as detailed under Methods; c transfected with luciferase expression constructs as detailed under Methods, treated with TWK as indicated, and further subjected to luciferase assay as detailed to assess NF-kB activity (* P < 0.05, n = 3 biological repeats; comparisons by T test; mean ± s.e.m.). The vertical line represents control in the absence of TWK; d subjected to Proteinase protection assay (upper panel) as detailed under Methods and schematically depicted (lower panel). e , f transfected with si NT or siRNA against p62 (si p62 ) and treated with TWK, extracted proteins were immunoblotted ( e ) or cells were immunostained for Fn14 and analyzed by confocal microscopy (scale bar, 20 µm) ( f )
    Figure Legend Snippet: Fn14-positive vesicles accumulate in a TWEAK-dependent manner upon Atg8s inactivation by dominant-negative ATG4B. a – f WT or ATG4B DN stable expression HeLa cells were assayed as follows: a treated with TWK for indicated times, immunostained for Fn14 and TRAF2, and analyzed by confocal microscopy (scale bar, 20 µm); b treated with TWK and subjected to membrane floatation assay as detailed under Methods; c transfected with luciferase expression constructs as detailed under Methods, treated with TWK as indicated, and further subjected to luciferase assay as detailed to assess NF-kB activity (* P < 0.05, n = 3 biological repeats; comparisons by T test; mean ± s.e.m.). The vertical line represents control in the absence of TWK; d subjected to Proteinase protection assay (upper panel) as detailed under Methods and schematically depicted (lower panel). e , f transfected with si NT or siRNA against p62 (si p62 ) and treated with TWK, extracted proteins were immunoblotted ( e ) or cells were immunostained for Fn14 and analyzed by confocal microscopy (scale bar, 20 µm) ( f )

    Techniques Used: Dominant Negative Mutation, Expressing, Confocal Microscopy, Membrane, Transfection, Luciferase, Construct, Activity Assay, Control

    Autophagy and MVBs both contribute to Fn14 trafficking. a – d WT or ATG4B DN stable expression HeLa cells were treated as follows and analyzed by confocal microscopy (scale bar, 20 µm): a treated with wortmannin as indicated and immunostained for Fn14 and p62; b transfected with si NT or siRNA against TRAF2 (si TRAF2 ), treated with TWK as indicated, and immunostained for Fn14. Arrows and arrowheads point at Fn14 at vesicles and plasma membrane, respectively; c , d transfected with si NT or siRNA against BECN1 (si BECN1 ) ( c ) or TSG101 (si TSG101 ) ( d ), treated with TWK, and immunostained for Fn14 and EEA1
    Figure Legend Snippet: Autophagy and MVBs both contribute to Fn14 trafficking. a – d WT or ATG4B DN stable expression HeLa cells were treated as follows and analyzed by confocal microscopy (scale bar, 20 µm): a treated with wortmannin as indicated and immunostained for Fn14 and p62; b transfected with si NT or siRNA against TRAF2 (si TRAF2 ), treated with TWK as indicated, and immunostained for Fn14. Arrows and arrowheads point at Fn14 at vesicles and plasma membrane, respectively; c , d transfected with si NT or siRNA against BECN1 (si BECN1 ) ( c ) or TSG101 (si TSG101 ) ( d ), treated with TWK, and immunostained for Fn14 and EEA1

    Techniques Used: Expressing, Confocal Microscopy, Transfection, Clinical Proteomics, Membrane

    Regulation of Fn14 by the autophagic machinery. GABARAP-mediated autophagy is responsible for the main pool of the cellular Fn14 and in its absence the receptor accumulates in ERGIC. GATE-16-mediated autophagy and the canonical MVB pathway are responsible in parallel for degradation of Fn14 in endocytic compartments. In absence of GATE-16, Fn14-positive endosomes accumulate at the vicinity of open phagophores. Recruitment of Fn14 to either GABARAP- or GATE-16-dependent autophagosomes is mediated by the cargo receptor p62. Recruitment of internalized Fn14 through the GATE-16-dependent pathway requires TRAF2. The mechanism responsible for recruitment Fn14 to GABARAP-dependent autophagy is still unknown
    Figure Legend Snippet: Regulation of Fn14 by the autophagic machinery. GABARAP-mediated autophagy is responsible for the main pool of the cellular Fn14 and in its absence the receptor accumulates in ERGIC. GATE-16-mediated autophagy and the canonical MVB pathway are responsible in parallel for degradation of Fn14 in endocytic compartments. In absence of GATE-16, Fn14-positive endosomes accumulate at the vicinity of open phagophores. Recruitment of Fn14 to either GABARAP- or GATE-16-dependent autophagosomes is mediated by the cargo receptor p62. Recruitment of internalized Fn14 through the GATE-16-dependent pathway requires TRAF2. The mechanism responsible for recruitment Fn14 to GABARAP-dependent autophagy is still unknown

    Techniques Used:



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    Santa Cruz Biotechnology rabbit polyclonal anti p62
    Fn14-positive vesicles accumulate in a TWEAK-dependent manner upon Atg8s inactivation by dominant-negative ATG4B. a – f WT or ATG4B DN stable expression HeLa cells were assayed as follows: a treated with TWK for indicated times, immunostained for Fn14 and TRAF2, and analyzed by confocal microscopy (scale bar, 20 µm); b treated with TWK and subjected to membrane floatation assay as detailed under Methods; c transfected with luciferase expression constructs as detailed under Methods, treated with TWK as indicated, and further subjected to luciferase assay as detailed to assess NF-kB activity (* P < 0.05, n = 3 biological repeats; comparisons by T test; mean ± s.e.m.). The vertical line represents control in the absence of TWK; d subjected to Proteinase protection assay (upper panel) as detailed under Methods and schematically depicted (lower panel). e , f transfected with si NT or siRNA against <t>p62</t> (si p62 ) and treated with TWK, extracted proteins were immunoblotted ( e ) or cells were immunostained for Fn14 and analyzed by confocal microscopy (scale bar, 20 µm) ( f )
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    Image Search Results


    Fn14-positive vesicles accumulate in a TWEAK-dependent manner upon Atg8s inactivation by dominant-negative ATG4B. a – f WT or ATG4B DN stable expression HeLa cells were assayed as follows: a treated with TWK for indicated times, immunostained for Fn14 and TRAF2, and analyzed by confocal microscopy (scale bar, 20 µm); b treated with TWK and subjected to membrane floatation assay as detailed under Methods; c transfected with luciferase expression constructs as detailed under Methods, treated with TWK as indicated, and further subjected to luciferase assay as detailed to assess NF-kB activity (* P < 0.05, n = 3 biological repeats; comparisons by T test; mean ± s.e.m.). The vertical line represents control in the absence of TWK; d subjected to Proteinase protection assay (upper panel) as detailed under Methods and schematically depicted (lower panel). e , f transfected with si NT or siRNA against p62 (si p62 ) and treated with TWK, extracted proteins were immunoblotted ( e ) or cells were immunostained for Fn14 and analyzed by confocal microscopy (scale bar, 20 µm) ( f )

    Journal: Nature Communications

    Article Title: Autophagy differentially regulates TNF receptor Fn14 by distinct mammalian Atg8 proteins

    doi: 10.1038/s41467-018-06275-1

    Figure Lengend Snippet: Fn14-positive vesicles accumulate in a TWEAK-dependent manner upon Atg8s inactivation by dominant-negative ATG4B. a – f WT or ATG4B DN stable expression HeLa cells were assayed as follows: a treated with TWK for indicated times, immunostained for Fn14 and TRAF2, and analyzed by confocal microscopy (scale bar, 20 µm); b treated with TWK and subjected to membrane floatation assay as detailed under Methods; c transfected with luciferase expression constructs as detailed under Methods, treated with TWK as indicated, and further subjected to luciferase assay as detailed to assess NF-kB activity (* P < 0.05, n = 3 biological repeats; comparisons by T test; mean ± s.e.m.). The vertical line represents control in the absence of TWK; d subjected to Proteinase protection assay (upper panel) as detailed under Methods and schematically depicted (lower panel). e , f transfected with si NT or siRNA against p62 (si p62 ) and treated with TWK, extracted proteins were immunoblotted ( e ) or cells were immunostained for Fn14 and analyzed by confocal microscopy (scale bar, 20 µm) ( f )

    Article Snippet: Mouse monoclonal anti-Fn14 (sc56250), mouse monoclonal anti-TBC1D5 (sc376296), rabbit polyclonal anti-TRAF2 (sc7187), rabbit polyclonal anti-TNFR1 (sc7895), rabbit polyclonal anti-p62 (sc25575), and mouse monoclonal anti-p62 (sc28359) were purchased from Santa-Cruz Biotechnology; mouse monoclonal anti-p62 was purchased from Abnova (H00008878, 1:3000 dilution for WB); rabbit polyclonal anti-Calnexin (ab22595), rabbit polyclonal anti-LAMP1 (ab24170), rabbit monoclonal anti-Rab7 (ab137029), and mouse monoclonal anti-Rab5 (ab66746) were purchased from Abcam; rabbit polyclonal anti-EEA1 (2411) and rabbit anti-EGFR (4267) were purchased from Cell Signaling; rabbit polyclonal anti-GATE-16 (PM038) and rabbit polyclonal anti-GABARAP (PM037) were purchased from MBL; rabbit polyclonal anti-ERGIC-53 (E1031), rabbit polyclonal anti-ATG3 (A3231), and rabbit polyclonal anti-ATG7 (A2856) were purchased from Sigma; mouse monoclonal anti-TSG101 (GTX70255) was purchased from Genetex; mouse monoclonal anti-Actin (69100, 1:5000 dilution) was purchased from Millipore; donkey anti-mouse Alexa488 (711545152), donkey anti-rabbit Cy5 (711175152), and donkey anti-rabbit Cy3 (711165152) were purchased from Jackson ImmunoResearch; rabbit polyclonal anti-GRASP65 kindly provided by Sima Lev; rabbit polyclonal anti-WIPI1 was a gift from Tassula Proikas-Cezanne; rabbit polyclonal anti-p53 was a gift from Moshe Oren; rabbit polyclonal anti-LC3 antibody was produced by immunization of a rabbit with a peptide of the first 14 amino acids (excluding Met1) of human LC3B with an additional cysteine (PSEKTFKQRRTFEQC).

    Techniques: Dominant Negative Mutation, Expressing, Confocal Microscopy, Membrane, Transfection, Luciferase, Construct, Activity Assay, Control

    Autophagy and MVBs both contribute to Fn14 trafficking. a – d WT or ATG4B DN stable expression HeLa cells were treated as follows and analyzed by confocal microscopy (scale bar, 20 µm): a treated with wortmannin as indicated and immunostained for Fn14 and p62; b transfected with si NT or siRNA against TRAF2 (si TRAF2 ), treated with TWK as indicated, and immunostained for Fn14. Arrows and arrowheads point at Fn14 at vesicles and plasma membrane, respectively; c , d transfected with si NT or siRNA against BECN1 (si BECN1 ) ( c ) or TSG101 (si TSG101 ) ( d ), treated with TWK, and immunostained for Fn14 and EEA1

    Journal: Nature Communications

    Article Title: Autophagy differentially regulates TNF receptor Fn14 by distinct mammalian Atg8 proteins

    doi: 10.1038/s41467-018-06275-1

    Figure Lengend Snippet: Autophagy and MVBs both contribute to Fn14 trafficking. a – d WT or ATG4B DN stable expression HeLa cells were treated as follows and analyzed by confocal microscopy (scale bar, 20 µm): a treated with wortmannin as indicated and immunostained for Fn14 and p62; b transfected with si NT or siRNA against TRAF2 (si TRAF2 ), treated with TWK as indicated, and immunostained for Fn14. Arrows and arrowheads point at Fn14 at vesicles and plasma membrane, respectively; c , d transfected with si NT or siRNA against BECN1 (si BECN1 ) ( c ) or TSG101 (si TSG101 ) ( d ), treated with TWK, and immunostained for Fn14 and EEA1

    Article Snippet: Mouse monoclonal anti-Fn14 (sc56250), mouse monoclonal anti-TBC1D5 (sc376296), rabbit polyclonal anti-TRAF2 (sc7187), rabbit polyclonal anti-TNFR1 (sc7895), rabbit polyclonal anti-p62 (sc25575), and mouse monoclonal anti-p62 (sc28359) were purchased from Santa-Cruz Biotechnology; mouse monoclonal anti-p62 was purchased from Abnova (H00008878, 1:3000 dilution for WB); rabbit polyclonal anti-Calnexin (ab22595), rabbit polyclonal anti-LAMP1 (ab24170), rabbit monoclonal anti-Rab7 (ab137029), and mouse monoclonal anti-Rab5 (ab66746) were purchased from Abcam; rabbit polyclonal anti-EEA1 (2411) and rabbit anti-EGFR (4267) were purchased from Cell Signaling; rabbit polyclonal anti-GATE-16 (PM038) and rabbit polyclonal anti-GABARAP (PM037) were purchased from MBL; rabbit polyclonal anti-ERGIC-53 (E1031), rabbit polyclonal anti-ATG3 (A3231), and rabbit polyclonal anti-ATG7 (A2856) were purchased from Sigma; mouse monoclonal anti-TSG101 (GTX70255) was purchased from Genetex; mouse monoclonal anti-Actin (69100, 1:5000 dilution) was purchased from Millipore; donkey anti-mouse Alexa488 (711545152), donkey anti-rabbit Cy5 (711175152), and donkey anti-rabbit Cy3 (711165152) were purchased from Jackson ImmunoResearch; rabbit polyclonal anti-GRASP65 kindly provided by Sima Lev; rabbit polyclonal anti-WIPI1 was a gift from Tassula Proikas-Cezanne; rabbit polyclonal anti-p53 was a gift from Moshe Oren; rabbit polyclonal anti-LC3 antibody was produced by immunization of a rabbit with a peptide of the first 14 amino acids (excluding Met1) of human LC3B with an additional cysteine (PSEKTFKQRRTFEQC).

    Techniques: Expressing, Confocal Microscopy, Transfection, Clinical Proteomics, Membrane

    Regulation of Fn14 by the autophagic machinery. GABARAP-mediated autophagy is responsible for the main pool of the cellular Fn14 and in its absence the receptor accumulates in ERGIC. GATE-16-mediated autophagy and the canonical MVB pathway are responsible in parallel for degradation of Fn14 in endocytic compartments. In absence of GATE-16, Fn14-positive endosomes accumulate at the vicinity of open phagophores. Recruitment of Fn14 to either GABARAP- or GATE-16-dependent autophagosomes is mediated by the cargo receptor p62. Recruitment of internalized Fn14 through the GATE-16-dependent pathway requires TRAF2. The mechanism responsible for recruitment Fn14 to GABARAP-dependent autophagy is still unknown

    Journal: Nature Communications

    Article Title: Autophagy differentially regulates TNF receptor Fn14 by distinct mammalian Atg8 proteins

    doi: 10.1038/s41467-018-06275-1

    Figure Lengend Snippet: Regulation of Fn14 by the autophagic machinery. GABARAP-mediated autophagy is responsible for the main pool of the cellular Fn14 and in its absence the receptor accumulates in ERGIC. GATE-16-mediated autophagy and the canonical MVB pathway are responsible in parallel for degradation of Fn14 in endocytic compartments. In absence of GATE-16, Fn14-positive endosomes accumulate at the vicinity of open phagophores. Recruitment of Fn14 to either GABARAP- or GATE-16-dependent autophagosomes is mediated by the cargo receptor p62. Recruitment of internalized Fn14 through the GATE-16-dependent pathway requires TRAF2. The mechanism responsible for recruitment Fn14 to GABARAP-dependent autophagy is still unknown

    Article Snippet: Mouse monoclonal anti-Fn14 (sc56250), mouse monoclonal anti-TBC1D5 (sc376296), rabbit polyclonal anti-TRAF2 (sc7187), rabbit polyclonal anti-TNFR1 (sc7895), rabbit polyclonal anti-p62 (sc25575), and mouse monoclonal anti-p62 (sc28359) were purchased from Santa-Cruz Biotechnology; mouse monoclonal anti-p62 was purchased from Abnova (H00008878, 1:3000 dilution for WB); rabbit polyclonal anti-Calnexin (ab22595), rabbit polyclonal anti-LAMP1 (ab24170), rabbit monoclonal anti-Rab7 (ab137029), and mouse monoclonal anti-Rab5 (ab66746) were purchased from Abcam; rabbit polyclonal anti-EEA1 (2411) and rabbit anti-EGFR (4267) were purchased from Cell Signaling; rabbit polyclonal anti-GATE-16 (PM038) and rabbit polyclonal anti-GABARAP (PM037) were purchased from MBL; rabbit polyclonal anti-ERGIC-53 (E1031), rabbit polyclonal anti-ATG3 (A3231), and rabbit polyclonal anti-ATG7 (A2856) were purchased from Sigma; mouse monoclonal anti-TSG101 (GTX70255) was purchased from Genetex; mouse monoclonal anti-Actin (69100, 1:5000 dilution) was purchased from Millipore; donkey anti-mouse Alexa488 (711545152), donkey anti-rabbit Cy5 (711175152), and donkey anti-rabbit Cy3 (711165152) were purchased from Jackson ImmunoResearch; rabbit polyclonal anti-GRASP65 kindly provided by Sima Lev; rabbit polyclonal anti-WIPI1 was a gift from Tassula Proikas-Cezanne; rabbit polyclonal anti-p53 was a gift from Moshe Oren; rabbit polyclonal anti-LC3 antibody was produced by immunization of a rabbit with a peptide of the first 14 amino acids (excluding Met1) of human LC3B with an additional cysteine (PSEKTFKQRRTFEQC).

    Techniques:

    Expression of SPARC was evaluated by immunohistochemical analysis of resected gastric cancer specimens. Positive staining for SPARC was observed in stromal cells and cancer cells, but was markedly more intense in stromal cells than in cancer cells. (A) ×200; and (B) ×400. SPARC, secreted protein, acidic and cysteine-rich.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Expression of SPARC was evaluated by immunohistochemical analysis of resected gastric cancer specimens. Positive staining for SPARC was observed in stromal cells and cancer cells, but was markedly more intense in stromal cells than in cancer cells. (A) ×200; and (B) ×400. SPARC, secreted protein, acidic and cysteine-rich.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Expressing, Immunohistochemical staining, Staining

    SPARC and β-actin mRNA expression in (A) 7 gastric cancer cell lines and (B) clinical samples, as determined by reverse-transcription polymerase chain reaction. The product size of SPARC and β-actin was 126 and 171 base pairs, respectively. SPARC, secreted protein, acidic and cysteine-rich; p, positive control; n, negative control; T, tumor; N, adjacent normal mucosa.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: SPARC and β-actin mRNA expression in (A) 7 gastric cancer cell lines and (B) clinical samples, as determined by reverse-transcription polymerase chain reaction. The product size of SPARC and β-actin was 126 and 171 base pairs, respectively. SPARC, secreted protein, acidic and cysteine-rich; p, positive control; n, negative control; T, tumor; N, adjacent normal mucosa.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Expressing, Reverse Transcription, Polymerase Chain Reaction, Positive Control, Negative Control

    Comparison of SPARC expression levels between gastric cancer tissues and adjacent normal mucosa (P=0.0012, as determined using the Wilcoxon's signed rank test). Box indicates the interquartile range (25–75%), the horizontal line indicates the mean and the bars indicates the first and ninth decile. SPARC, secreted protein, acidic and cysteine-rich.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Comparison of SPARC expression levels between gastric cancer tissues and adjacent normal mucosa (P=0.0012, as determined using the Wilcoxon's signed rank test). Box indicates the interquartile range (25–75%), the horizontal line indicates the mean and the bars indicates the first and ninth decile. SPARC, secreted protein, acidic and cysteine-rich.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Comparison, Expressing

    Univariate analysis of potential prognostic variables for overall survival.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Univariate analysis of potential prognostic variables for overall survival.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Expressing

    Multivariate analysis of potential prognostic variables for overall survival.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Multivariate analysis of potential prognostic variables for overall survival.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Expressing

    Association between  SPARC  gene expression and potential prognostic variables.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Association between SPARC gene expression and potential prognostic variables.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Gene Expression, Expressing

    Comparison of overall survival rates between low and high SPARC expression levels in patients who had following adjuvant S-1 chemotherapy (P=0.000006, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Comparison of overall survival rates between low and high SPARC expression levels in patients who had following adjuvant S-1 chemotherapy (P=0.000006, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Comparison, Expressing, Adjuvant

    Comparison of overall survival rates between high and low SPARC expression levels in patients with stage II gastric cancer who had following adjuvant S-1 chemotherapy (P=0.036, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Comparison of overall survival rates between high and low SPARC expression levels in patients with stage II gastric cancer who had following adjuvant S-1 chemotherapy (P=0.036, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Comparison, Expressing, Adjuvant

    Comparison of overall survival rates between high and low SPARC expression levels in patients with stage III gastric cancer who had following adjuvant S-1 chemotherapy (P=0.000017, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Comparison of overall survival rates between high and low SPARC expression levels in patients with stage III gastric cancer who had following adjuvant S-1 chemotherapy (P=0.000017, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Comparison, Expressing, Adjuvant

    Comparison of overall survival rates between high and low SPARC expression levels in the patients who had not received adjuvant S-1 chemotherapy (P=0.732, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Journal: Oncology Letters

    Article Title: Clinical significance of secreted protein, acidic and cysteine-rich gene expression in patients with stage II/III gastric cancer following curative resection and adjuvant chemotherapy with S-1

    doi: 10.3892/ol.2018.8248

    Figure Lengend Snippet: Comparison of overall survival rates between high and low SPARC expression levels in the patients who had not received adjuvant S-1 chemotherapy (P=0.732, as determined using the log-rank test). SPARC, secreted protein, acidic and cysteine-rich.

    Article Snippet: Primary polyclonal antibodies against SPARC (dilution, 1:50; cat. no. sc-25574; Santa Cruz Biotechnology, Inc., Dallas, TX, USA).

    Techniques: Comparison, Expressing, Adjuvant