abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc abcg2
    Primer sequences.
    Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/abcg2/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    abcg2 - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway"

    Article Title: Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2022/3032407

    Primer sequences.
    Figure Legend Snippet: Primer sequences.

    Techniques Used: Sequencing

    Effect of ZJW on the expression of the drug resistance-related proteins MDR1/ABCB1, MRP4/ABCC4, and ABCG2 in HCT116/L-OHP cells. (a and b) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 proteins in HCT116 cells and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. (c) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in HCT116 and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001 compared to HCT116/L.
    Figure Legend Snippet: Effect of ZJW on the expression of the drug resistance-related proteins MDR1/ABCB1, MRP4/ABCC4, and ABCG2 in HCT116/L-OHP cells. (a and b) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 proteins in HCT116 cells and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. (c) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in HCT116 and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001 compared to HCT116/L.

    Techniques Used: Expressing, Western Blot, Real-time Polymerase Chain Reaction

    Effect of ZJW on the expression of drug resistance-related proteins in vivo. (a and b) Immunofluorescence detection of MDR1/ABCB1 and ABCG2 proteins in vivo. (c and d) Immunohistochemistry detection of MRP4/ABCC4 protein in vivo. (e and f) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. (g) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001; ∗∗∗∗ , P < 0.0001; ns, no significance compared to MODEL.
    Figure Legend Snippet: Effect of ZJW on the expression of drug resistance-related proteins in vivo. (a and b) Immunofluorescence detection of MDR1/ABCB1 and ABCG2 proteins in vivo. (c and d) Immunohistochemistry detection of MRP4/ABCC4 protein in vivo. (e and f) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. (g) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001; ∗∗∗∗ , P < 0.0001; ns, no significance compared to MODEL.

    Techniques Used: Expressing, In Vivo, Immunofluorescence, Immunohistochemistry, Western Blot, Real-time Polymerase Chain Reaction

    abcg2  (Cell Signaling Technology Inc)


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  • 95

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    Cell Signaling Technology Inc abcg2
    Primer sequences.
    Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/abcg2/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    abcg2 - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway"

    Article Title: Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2022/3032407

    Primer sequences.
    Figure Legend Snippet: Primer sequences.

    Techniques Used: Sequencing

    Effect of ZJW on the expression of the drug resistance-related proteins MDR1/ABCB1, MRP4/ABCC4, and ABCG2 in HCT116/L-OHP cells. (a and b) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 proteins in HCT116 cells and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. (c) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in HCT116 and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001 compared to HCT116/L.
    Figure Legend Snippet: Effect of ZJW on the expression of the drug resistance-related proteins MDR1/ABCB1, MRP4/ABCC4, and ABCG2 in HCT116/L-OHP cells. (a and b) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 proteins in HCT116 cells and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. (c) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in HCT116 and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001 compared to HCT116/L.

    Techniques Used: Expressing, Western Blot, Real-time Polymerase Chain Reaction

    Effect of ZJW on the expression of drug resistance-related proteins in vivo. (a and b) Immunofluorescence detection of MDR1/ABCB1 and ABCG2 proteins in vivo. (c and d) Immunohistochemistry detection of MRP4/ABCC4 protein in vivo. (e and f) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. (g) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001; ∗∗∗∗ , P < 0.0001; ns, no significance compared to MODEL.
    Figure Legend Snippet: Effect of ZJW on the expression of drug resistance-related proteins in vivo. (a and b) Immunofluorescence detection of MDR1/ABCB1 and ABCG2 proteins in vivo. (c and d) Immunohistochemistry detection of MRP4/ABCC4 protein in vivo. (e and f) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. (g) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001; ∗∗∗∗ , P < 0.0001; ns, no significance compared to MODEL.

    Techniques Used: Expressing, In Vivo, Immunofluorescence, Immunohistochemistry, Western Blot, Real-time Polymerase Chain Reaction

    bcrp  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc bcrp
    Bcrp, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 1 article reviews
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    95/100 stars

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    rabbit anti abcg2 polyclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti abcg2 polyclonal antibody
    Expression of <t>ABCG2</t> in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.
    Rabbit Anti Abcg2 Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti abcg2 polyclonal antibody/product/Cell Signaling Technology Inc
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    1) Product Images from "Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma"

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    Journal: Gastroenterology Research and Practice

    doi: 10.1155/2013/782581

    Expression of ABCG2 in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.
    Figure Legend Snippet: Expression of ABCG2 in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.

    Techniques Used: Expressing, Positive Control, Negative Control

     ABCG2  expression and characteristics of patients.
    Figure Legend Snippet: ABCG2 expression and characteristics of patients.

    Techniques Used: Expressing

    ABCG2 was expressed in a minor population of SMMC-7721 cells. (a) The positive rate of ABCG2 in SMMC-7721 cells determined by flow cytometry was about 8.8% before cell sorting. P2 gate represents ABCG2 positive cells. Mouse IgG2b was used as isotype control. (b) Positive rate of ABCG2 in sorted ABCG2+/ABCG2− cells after 3 passages of culture. (c) Detection of ABCG2 protein level in freshly sorted cells by western blot. β -Actin was used as loading control. The optical density of specific bands was quantified and normalized to β -Actin. ** P < 0.01.
    Figure Legend Snippet: ABCG2 was expressed in a minor population of SMMC-7721 cells. (a) The positive rate of ABCG2 in SMMC-7721 cells determined by flow cytometry was about 8.8% before cell sorting. P2 gate represents ABCG2 positive cells. Mouse IgG2b was used as isotype control. (b) Positive rate of ABCG2 in sorted ABCG2+/ABCG2− cells after 3 passages of culture. (c) Detection of ABCG2 protein level in freshly sorted cells by western blot. β -Actin was used as loading control. The optical density of specific bands was quantified and normalized to β -Actin. ** P < 0.01.

    Techniques Used: Flow Cytometry, FACS, Western Blot

    Difference of tumorigenic ability between  ABCG2+  and ABCG2− cells.
    Figure Legend Snippet: Difference of tumorigenic ability between ABCG2+ and ABCG2− cells.

    Techniques Used:

    Expression level of ABCG2 correlated with cell proliferation and chemoresistance. (a), (b) Freshly sorted ABCG2+ cells were transfected with ABCG2-specific siRNA. ABCG2− cells were transfected with ABCG2-overexpression plasmid. The proliferation of cells after transfection was compared with untransfected cells and negative control (scrambled siRNA or empty plasmid) using MTT assay after indicated time. (c), (d) The expression level of ABCG2 was manipulated as described above. Survival rates after exposure to indicated dose of doxorubicin for 24 h were determined by MTT assay. (e), (f) IC50 value to doxorubicin was calculated for different groups. ** P < 0.01.
    Figure Legend Snippet: Expression level of ABCG2 correlated with cell proliferation and chemoresistance. (a), (b) Freshly sorted ABCG2+ cells were transfected with ABCG2-specific siRNA. ABCG2− cells were transfected with ABCG2-overexpression plasmid. The proliferation of cells after transfection was compared with untransfected cells and negative control (scrambled siRNA or empty plasmid) using MTT assay after indicated time. (c), (d) The expression level of ABCG2 was manipulated as described above. Survival rates after exposure to indicated dose of doxorubicin for 24 h were determined by MTT assay. (e), (f) IC50 value to doxorubicin was calculated for different groups. ** P < 0.01.

    Techniques Used: Expressing, Transfection, Over Expression, Plasmid Preparation, Negative Control, MTT Assay

    RNA interference and plasmid-mediated overexpression of ABCG2 in SMMC-7721 cells. (a) RT-PCR analysis of ABCG2 mRNA in SMCC-7721 cells after transfection with siRNA or plasmid for 48 h. Normal SMMC-7721 cells were used as blank control. Scrambled siRNA was set as negative control. For overexpression, empty plasmid was transfected as negative control. (b), (c) Western blot analysis confirmed the efficiency of downregulation of ABCG2 by siRNA and upregulation by overexpression, respectively. β -Actin served as loading control. The optical density was quantified and normalized to β -Actin. ** P < 0.01, *** P < 0.001.
    Figure Legend Snippet: RNA interference and plasmid-mediated overexpression of ABCG2 in SMMC-7721 cells. (a) RT-PCR analysis of ABCG2 mRNA in SMCC-7721 cells after transfection with siRNA or plasmid for 48 h. Normal SMMC-7721 cells were used as blank control. Scrambled siRNA was set as negative control. For overexpression, empty plasmid was transfected as negative control. (b), (c) Western blot analysis confirmed the efficiency of downregulation of ABCG2 by siRNA and upregulation by overexpression, respectively. β -Actin served as loading control. The optical density was quantified and normalized to β -Actin. ** P < 0.01, *** P < 0.001.

    Techniques Used: Plasmid Preparation, Over Expression, Reverse Transcription Polymerase Chain Reaction, Transfection, Negative Control, Western Blot

    Downregulation or upregulation of ABCG2 had effect on migration and invasion potential in HCC cells. (a), (b) Wound healing assay evaluated the potential of migration of HCC cells. Untreated cells served as normal control. ABCG2+ cells were transfected with ABCG2 siRNA while ABCG2− cells were transfected with ABCG2-expressing plasmid. Scrambled siRNA and empty plasmid were used as negative control. The pictures above represent the wound right after tip scratch. Pictures below showed wound-healing status after 48 h. (c), (d) Results of transwell invasion assay. After 48 h of invasion, cells invaded to the lower chamber were stained and photographed. Invaded cells were counted in three random visions and the average numbers were presented. *** P < 0.001.
    Figure Legend Snippet: Downregulation or upregulation of ABCG2 had effect on migration and invasion potential in HCC cells. (a), (b) Wound healing assay evaluated the potential of migration of HCC cells. Untreated cells served as normal control. ABCG2+ cells were transfected with ABCG2 siRNA while ABCG2− cells were transfected with ABCG2-expressing plasmid. Scrambled siRNA and empty plasmid were used as negative control. The pictures above represent the wound right after tip scratch. Pictures below showed wound-healing status after 48 h. (c), (d) Results of transwell invasion assay. After 48 h of invasion, cells invaded to the lower chamber were stained and photographed. Invaded cells were counted in three random visions and the average numbers were presented. *** P < 0.001.

    Techniques Used: Migration, Wound Healing Assay, Transfection, Expressing, Plasmid Preparation, Negative Control, Transwell Invasion Assay, Staining

    anti abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti abcg2
    Anti Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti abcg2/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti abcg2 - by Bioz Stars, 2023-01
    95/100 stars

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    abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc abcg2
    Increased cellular antioxidant activity decreases ROS level to sustain the SP cell fraction in CRC cells. (A) The percentages of SP cells in LoVo and SW620 cells were compared using Hoechst 33342 staining followed by flow cytometry. (B) Images and quantification of colony or sphere formation by SP, non-SP or unsorted cells. (C) The stem cell markers CD44, CD133, Oct4, <t>ABCG2</t> and Sox2 were analyzed using immunoblotting in both SP and non-SP cells. (D) Representative histograms of significant decreases in the ROS contents of SP, non-SP or unsorted cells as detected by the fluorescent probe DCF-DA. (E) Cellular GSH levels in SP, non-SP or unsorted cells were measured via spectrophotometric analysis. (F) Reversion of H 2 O 2 -induced decreases in SP cells following NAC treatment. LoVo or SW620 cells were treated with 3 mM NAC for 2 h, followed by 100 μM H 2 O 2 for 24 h. Representative dot plots of three separate experiments are shown. Data in B and E are presented as the mean ± SD (n=3). * P < 0.05 versus control cells.
    Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/abcg2/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
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    abcg2 - by Bioz Stars, 2023-01
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    1) Product Images from "Redox Regulation of Stem-like Cells Though the CD44v-xCT Axis in Colorectal Cancer: Mechanisms and Therapeutic Implications"

    Article Title: Redox Regulation of Stem-like Cells Though the CD44v-xCT Axis in Colorectal Cancer: Mechanisms and Therapeutic Implications

    Journal: Theranostics

    doi: 10.7150/thno.14848

    Increased cellular antioxidant activity decreases ROS level to sustain the SP cell fraction in CRC cells. (A) The percentages of SP cells in LoVo and SW620 cells were compared using Hoechst 33342 staining followed by flow cytometry. (B) Images and quantification of colony or sphere formation by SP, non-SP or unsorted cells. (C) The stem cell markers CD44, CD133, Oct4, ABCG2 and Sox2 were analyzed using immunoblotting in both SP and non-SP cells. (D) Representative histograms of significant decreases in the ROS contents of SP, non-SP or unsorted cells as detected by the fluorescent probe DCF-DA. (E) Cellular GSH levels in SP, non-SP or unsorted cells were measured via spectrophotometric analysis. (F) Reversion of H 2 O 2 -induced decreases in SP cells following NAC treatment. LoVo or SW620 cells were treated with 3 mM NAC for 2 h, followed by 100 μM H 2 O 2 for 24 h. Representative dot plots of three separate experiments are shown. Data in B and E are presented as the mean ± SD (n=3). * P < 0.05 versus control cells.
    Figure Legend Snippet: Increased cellular antioxidant activity decreases ROS level to sustain the SP cell fraction in CRC cells. (A) The percentages of SP cells in LoVo and SW620 cells were compared using Hoechst 33342 staining followed by flow cytometry. (B) Images and quantification of colony or sphere formation by SP, non-SP or unsorted cells. (C) The stem cell markers CD44, CD133, Oct4, ABCG2 and Sox2 were analyzed using immunoblotting in both SP and non-SP cells. (D) Representative histograms of significant decreases in the ROS contents of SP, non-SP or unsorted cells as detected by the fluorescent probe DCF-DA. (E) Cellular GSH levels in SP, non-SP or unsorted cells were measured via spectrophotometric analysis. (F) Reversion of H 2 O 2 -induced decreases in SP cells following NAC treatment. LoVo or SW620 cells were treated with 3 mM NAC for 2 h, followed by 100 μM H 2 O 2 for 24 h. Representative dot plots of three separate experiments are shown. Data in B and E are presented as the mean ± SD (n=3). * P < 0.05 versus control cells.

    Techniques Used: Antioxidant Activity Assay, Staining, Flow Cytometry, Western Blot

    Pre-treatment of CRC cells with PEITC in vitro caused inhibition of tumor formation in vivo. (A) Depletion of cellular GSH and increased ROS levels in response to PEITC in both LoVo and SW620 cells as measured by spectrophotometric and flow cytometric analysis, respectively. (B) CRC cells were pretreated with the IC50 concentrations of PEITC and 5FU for 48 h. They were then washed and cultured in fresh medium without either drug for 48 h to allow cell death to occur. Viable cells were harvested and then stained with Hoechst 33342 to identify SP cells. (C) CD44, CD133, Oct4, ABCG2 and SOX2 expression levels were analyzed via qPCR in the indicated cells. (D) Experimental design as described in B . Equal numbers of control and drug-treated cells were inoculated subcutaneously into the flanks of athymic mice using 1.0x10 5 cells/injection site (Group 1) or 2.0x10 5 cells/injection site (Group 2). (E) Images of tumors from representative mice in each group on day 14. Measurement of tumor volumes was carried out on the indicated days. The right panel shows the mean tumor weights in each group on day 50. Data in A and C are presented as the mean±SD (n=3). * P < 0.05 versus control cells.
    Figure Legend Snippet: Pre-treatment of CRC cells with PEITC in vitro caused inhibition of tumor formation in vivo. (A) Depletion of cellular GSH and increased ROS levels in response to PEITC in both LoVo and SW620 cells as measured by spectrophotometric and flow cytometric analysis, respectively. (B) CRC cells were pretreated with the IC50 concentrations of PEITC and 5FU for 48 h. They were then washed and cultured in fresh medium without either drug for 48 h to allow cell death to occur. Viable cells were harvested and then stained with Hoechst 33342 to identify SP cells. (C) CD44, CD133, Oct4, ABCG2 and SOX2 expression levels were analyzed via qPCR in the indicated cells. (D) Experimental design as described in B . Equal numbers of control and drug-treated cells were inoculated subcutaneously into the flanks of athymic mice using 1.0x10 5 cells/injection site (Group 1) or 2.0x10 5 cells/injection site (Group 2). (E) Images of tumors from representative mice in each group on day 14. Measurement of tumor volumes was carried out on the indicated days. The right panel shows the mean tumor weights in each group on day 50. Data in A and C are presented as the mean±SD (n=3). * P < 0.05 versus control cells.

    Techniques Used: In Vitro, Inhibition, In Vivo, Cell Culture, Staining, Expressing, Injection

    anti abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti abcg2
    COX-2 and Drp1 were upregulated in the CSCs of NPC cells and NPC tissues. (A) Sorting SP and MP cells from CNE1 and CNE2 following Hoechst 33342 staining. A representative sample is displayed. The R2 gate shows the SP cells and R3 shows the MP cells. The percentages of SP cells in CNE 1 and CNE2 were 1.72% and 3.03 %. (B) In vitro extreme limiting dilution assays to demonstrate the frequency of CSCs in SP and MP cells. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs. (C) SP and MP cells were sorted by flow cytometry (FCM) and seeded on coverslips overnight. Mitochondria were stained by MitoTracker and imaged by confocal microscopy. Mitochondrial fragmentation counts were measured in 10 cells in each cell line of 3 independent experiments with IPP 6.0 (×630 magnification; scale bar, 10 μm) and shown in lower bar graph. * P < 0.05 as compared with MP cells. (D) SP and MP cell lysates were analyzed by WB. Expressions of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , total Drp1 (t-Drp1), Mfn2, <t>ABCG2,</t> and Oct4 were measured. *P < 0.05 as compared with MP cells. (E) PTGS2 and DNM1L expression levels in one cohort of NPC patients are shown by scatter plots. The relative expression values were obtained from NCBI, GEO database (Accession No. GDS3341). The horizontal lines represent the median values ( * P < 0.05). (F) The correlation between the expression of PTGS2 and DNM1L was calculated by Pearson's correlation analysis.
    Anti Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti abcg2/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti abcg2 - by Bioz Stars, 2023-01
    95/100 stars

    Images

    1) Product Images from "Downregulation of mitochondrial cyclooxygenase-2 inhibits the stemness of nasopharyngeal carcinoma by decreasing the activity of dynamin-related protein 1"

    Article Title: Downregulation of mitochondrial cyclooxygenase-2 inhibits the stemness of nasopharyngeal carcinoma by decreasing the activity of dynamin-related protein 1

    Journal: Theranostics

    doi: 10.7150/thno.17647

    COX-2 and Drp1 were upregulated in the CSCs of NPC cells and NPC tissues. (A) Sorting SP and MP cells from CNE1 and CNE2 following Hoechst 33342 staining. A representative sample is displayed. The R2 gate shows the SP cells and R3 shows the MP cells. The percentages of SP cells in CNE 1 and CNE2 were 1.72% and 3.03 %. (B) In vitro extreme limiting dilution assays to demonstrate the frequency of CSCs in SP and MP cells. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs. (C) SP and MP cells were sorted by flow cytometry (FCM) and seeded on coverslips overnight. Mitochondria were stained by MitoTracker and imaged by confocal microscopy. Mitochondrial fragmentation counts were measured in 10 cells in each cell line of 3 independent experiments with IPP 6.0 (×630 magnification; scale bar, 10 μm) and shown in lower bar graph. * P < 0.05 as compared with MP cells. (D) SP and MP cell lysates were analyzed by WB. Expressions of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , total Drp1 (t-Drp1), Mfn2, ABCG2, and Oct4 were measured. *P < 0.05 as compared with MP cells. (E) PTGS2 and DNM1L expression levels in one cohort of NPC patients are shown by scatter plots. The relative expression values were obtained from NCBI, GEO database (Accession No. GDS3341). The horizontal lines represent the median values ( * P < 0.05). (F) The correlation between the expression of PTGS2 and DNM1L was calculated by Pearson's correlation analysis.
    Figure Legend Snippet: COX-2 and Drp1 were upregulated in the CSCs of NPC cells and NPC tissues. (A) Sorting SP and MP cells from CNE1 and CNE2 following Hoechst 33342 staining. A representative sample is displayed. The R2 gate shows the SP cells and R3 shows the MP cells. The percentages of SP cells in CNE 1 and CNE2 were 1.72% and 3.03 %. (B) In vitro extreme limiting dilution assays to demonstrate the frequency of CSCs in SP and MP cells. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs. (C) SP and MP cells were sorted by flow cytometry (FCM) and seeded on coverslips overnight. Mitochondria were stained by MitoTracker and imaged by confocal microscopy. Mitochondrial fragmentation counts were measured in 10 cells in each cell line of 3 independent experiments with IPP 6.0 (×630 magnification; scale bar, 10 μm) and shown in lower bar graph. * P < 0.05 as compared with MP cells. (D) SP and MP cell lysates were analyzed by WB. Expressions of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , total Drp1 (t-Drp1), Mfn2, ABCG2, and Oct4 were measured. *P < 0.05 as compared with MP cells. (E) PTGS2 and DNM1L expression levels in one cohort of NPC patients are shown by scatter plots. The relative expression values were obtained from NCBI, GEO database (Accession No. GDS3341). The horizontal lines represent the median values ( * P < 0.05). (F) The correlation between the expression of PTGS2 and DNM1L was calculated by Pearson's correlation analysis.

    Techniques Used: Staining, In Vitro, Flow Cytometry, Confocal Microscopy, Expressing

    Upregulation of COX-2 leads to the activation of Drp1 and increases the cancer stemness of NPC. (A) Confocal microscopy images of CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cell lines stained for COX-2 (green), mitochondria (red) and nuclei (blue). Manders' overlap coefficients for the co-localization of COX-2 with mitochondria and the mitochondrial fragmentation counts were calculated by IPP 6.0 and shown in right bar graphs. (B) The in situ proximity ligation assay (PLA) was used to detect interaction between COX-2 and p-Drp1 Ser616 in CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cells. Interaction events are shown as red dots (×630 magnification; scale bar, 20 μm). Quantification of COX-2/p-Drp1 Ser616 interaction events are shown by bar charts (lower). (C) WBs showing the expression of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, Mfn2, ABCG2, and Oct4 in the CNE1 or CNE2 stable cell lines either overexpressing PTGS2 or transfected with control vector (pBabe). (D) The proportion of SP cells in the CNE1 or CNE2 stable cell lines overexpressing PTGS2 was analyzed by FCM. The R2 gate shows the SP cells. Representative examples are displayed. * P < 0.05 as compared with pBabe cells. (E) In vitro extreme limiting dilution assays to demonstrate the frequency of CSCs in CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cell lines. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs.
    Figure Legend Snippet: Upregulation of COX-2 leads to the activation of Drp1 and increases the cancer stemness of NPC. (A) Confocal microscopy images of CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cell lines stained for COX-2 (green), mitochondria (red) and nuclei (blue). Manders' overlap coefficients for the co-localization of COX-2 with mitochondria and the mitochondrial fragmentation counts were calculated by IPP 6.0 and shown in right bar graphs. (B) The in situ proximity ligation assay (PLA) was used to detect interaction between COX-2 and p-Drp1 Ser616 in CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cells. Interaction events are shown as red dots (×630 magnification; scale bar, 20 μm). Quantification of COX-2/p-Drp1 Ser616 interaction events are shown by bar charts (lower). (C) WBs showing the expression of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, Mfn2, ABCG2, and Oct4 in the CNE1 or CNE2 stable cell lines either overexpressing PTGS2 or transfected with control vector (pBabe). (D) The proportion of SP cells in the CNE1 or CNE2 stable cell lines overexpressing PTGS2 was analyzed by FCM. The R2 gate shows the SP cells. Representative examples are displayed. * P < 0.05 as compared with pBabe cells. (E) In vitro extreme limiting dilution assays to demonstrate the frequency of CSCs in CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cell lines. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs.

    Techniques Used: Activation Assay, Confocal Microscopy, Staining, In Situ, Proximity Ligation Assay, Expressing, Stable Transfection, Transfection, Plasmid Preparation, In Vitro

    Inhibition of p-Drp1 Ser616 by Mdivi-1 can downregulate cancer stemness but has no effect on COX-2. (A) CNE1 and CNE2 cells were treated with 20 μM Mdivi-1 for 24 h. The co-localization of COX-2 (green) and mitochondria (red) was examined by confocal microscopy, when nuclei are stained blue. Quantification of the mitochondrial fragmentation counts is shown in right bar graphs. Manders' overlap coefficients for the co-localization of COX-2 with mitochondria are shown in Fig. . (B) CNE1 and CNE2 cells were treated with or without various concentrations of Mdivi-1 (0, 10, or 20 μM) for 24 h and the level of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, Mfn2, ABCG2, and Oct4 in CNE1 and CNE2 cells were measured by WB assay. (C) SP cells were treated as in (B) and analyzed by FCM. Quantification are shown by bar graphs. * P < 0.05, compared with the Ctrl group.
    Figure Legend Snippet: Inhibition of p-Drp1 Ser616 by Mdivi-1 can downregulate cancer stemness but has no effect on COX-2. (A) CNE1 and CNE2 cells were treated with 20 μM Mdivi-1 for 24 h. The co-localization of COX-2 (green) and mitochondria (red) was examined by confocal microscopy, when nuclei are stained blue. Quantification of the mitochondrial fragmentation counts is shown in right bar graphs. Manders' overlap coefficients for the co-localization of COX-2 with mitochondria are shown in Fig. . (B) CNE1 and CNE2 cells were treated with or without various concentrations of Mdivi-1 (0, 10, or 20 μM) for 24 h and the level of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, Mfn2, ABCG2, and Oct4 in CNE1 and CNE2 cells were measured by WB assay. (C) SP cells were treated as in (B) and analyzed by FCM. Quantification are shown by bar graphs. * P < 0.05, compared with the Ctrl group.

    Techniques Used: Inhibition, Confocal Microscopy, Staining

    Knockdown of Drp1 by si DNM1L downregulates the increase of mitochondrial fission and NPC stemness induced by COX-2 overexpression. CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cells were transfected with siNC or si DNM1L (50 nM) for 12 h. (A) The co-localization of COX-2 (green) and mitochondria (red) was determined by confocal microscopy. Quantification of the mitochondrial fragmentation counts is shown in bar graphs. (B) The expression level of COX-2, p-Drp1 Ser616 , t-Drp1, ABCG2, and Oct4 was detected by WB assay. (C) SP cells were analyzed by FCM. (D) Quantification of SP cells in CNE1 and CNE2 are shown in bar graphs. * P < 0.05, compared with the CNE1-pBabe (siNC) or CNE2-pBabe (siNC) group. # P < 0.05, compared with the CNE1- PTGS2 (siNC) or CNE2- PTGS2 (siNC) group, & P <0.05 compared with the CNE1-pBabe (si DNM1L ) or CNE2-pBabe (si DNM1L ) group.
    Figure Legend Snippet: Knockdown of Drp1 by si DNM1L downregulates the increase of mitochondrial fission and NPC stemness induced by COX-2 overexpression. CNE1-pBabe, CNE1- PTGS2 , CNE2-pBabe, and CNE2- PTGS2 cells were transfected with siNC or si DNM1L (50 nM) for 12 h. (A) The co-localization of COX-2 (green) and mitochondria (red) was determined by confocal microscopy. Quantification of the mitochondrial fragmentation counts is shown in bar graphs. (B) The expression level of COX-2, p-Drp1 Ser616 , t-Drp1, ABCG2, and Oct4 was detected by WB assay. (C) SP cells were analyzed by FCM. (D) Quantification of SP cells in CNE1 and CNE2 are shown in bar graphs. * P < 0.05, compared with the CNE1-pBabe (siNC) or CNE2-pBabe (siNC) group. # P < 0.05, compared with the CNE1- PTGS2 (siNC) or CNE2- PTGS2 (siNC) group, & P <0.05 compared with the CNE1-pBabe (si DNM1L ) or CNE2-pBabe (si DNM1L ) group.

    Techniques Used: Over Expression, Transfection, Confocal Microscopy, Expressing

    Inhibiting COX-2 expression decreases p-Drp1 Ser616 and cancer stemness by lessening the mitochondrial translocation of p53. COX-2 knockdown cells, CNE1-shCtrl, CNE1-sh PTGS2 CNE2-shCtrl, and CNE2-sh PTGS2 cells were used. (A) The four cell lines stained for COX-2 (green), mitochondria (red) and nucleus (blue) were imaged by confocal microscopy. Manders' overlap coefficients for the co-localization of COX-2 with mitochondria and the mitochondrial fragmentation counts calculated by IPP 6.0 are shown in right bar graphs. (B) The in situ proximity ligation assay (PLA) shows the interactions of COX-2 with p-Drp1 Ser616 and p53 with p-Drp1 Ser616 in the four cell lines. Interaction events are shown as red dots (Scale bar: 20 μm). Quantification of p53/p-Drp1 Ser616 and COX-2/p-Drp1 Ser616 interaction events are shown in bar charts (lower). * P < 0.05 as compared with the shCtrl cells. (C) SP and MP cells were sorted from CNE1 and CNE2 cells and transfected with siNC or si PTGS2 (50 nM) for 12 h and the interaction between COX-2 and p-Drp1 Ser616 was then detected with the PLA. Interaction events are shown as red dots (×630 magnification; scale bar, 20 μm). Quantifications of COX-2/p-Drp1 Ser616 interaction events are shown by bar charts (right). * P < 0.05 as compared with CNE1-SP (siNC) or CNE2-SP (siNC), # P < 0.05 as compared with CNE1-MP (siNC) or CNE2-MP (siNC). (D-E) Whole cell lysates (WCL) and mitochondrial (Mito) and cytosolic (Cyto) fractions of in the four cell lines were subjected to WB assay. Expressions of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, and Mfn2 are shown for WCL, and COX-2, p53, and p-Drp1 Ser616 are shown for the Mito and Cyto fractions. (F) Cell lysates of PTGS2 -knockdown cell lines were subjected to WB for measurement of ABCG2 and Oct4. (G-H) SP cells in the four cell lines were analyzed by FCM and quantification is shown in the bar graphs. * P < 0.05 as compared with the shCtrl cells. (I) The frequencies of CSCs in PTGS2 -knockdown cell lines were measured by in vitro extreme limiting dilution assays. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs.
    Figure Legend Snippet: Inhibiting COX-2 expression decreases p-Drp1 Ser616 and cancer stemness by lessening the mitochondrial translocation of p53. COX-2 knockdown cells, CNE1-shCtrl, CNE1-sh PTGS2 CNE2-shCtrl, and CNE2-sh PTGS2 cells were used. (A) The four cell lines stained for COX-2 (green), mitochondria (red) and nucleus (blue) were imaged by confocal microscopy. Manders' overlap coefficients for the co-localization of COX-2 with mitochondria and the mitochondrial fragmentation counts calculated by IPP 6.0 are shown in right bar graphs. (B) The in situ proximity ligation assay (PLA) shows the interactions of COX-2 with p-Drp1 Ser616 and p53 with p-Drp1 Ser616 in the four cell lines. Interaction events are shown as red dots (Scale bar: 20 μm). Quantification of p53/p-Drp1 Ser616 and COX-2/p-Drp1 Ser616 interaction events are shown in bar charts (lower). * P < 0.05 as compared with the shCtrl cells. (C) SP and MP cells were sorted from CNE1 and CNE2 cells and transfected with siNC or si PTGS2 (50 nM) for 12 h and the interaction between COX-2 and p-Drp1 Ser616 was then detected with the PLA. Interaction events are shown as red dots (×630 magnification; scale bar, 20 μm). Quantifications of COX-2/p-Drp1 Ser616 interaction events are shown by bar charts (right). * P < 0.05 as compared with CNE1-SP (siNC) or CNE2-SP (siNC), # P < 0.05 as compared with CNE1-MP (siNC) or CNE2-MP (siNC). (D-E) Whole cell lysates (WCL) and mitochondrial (Mito) and cytosolic (Cyto) fractions of in the four cell lines were subjected to WB assay. Expressions of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, and Mfn2 are shown for WCL, and COX-2, p53, and p-Drp1 Ser616 are shown for the Mito and Cyto fractions. (F) Cell lysates of PTGS2 -knockdown cell lines were subjected to WB for measurement of ABCG2 and Oct4. (G-H) SP cells in the four cell lines were analyzed by FCM and quantification is shown in the bar graphs. * P < 0.05 as compared with the shCtrl cells. (I) The frequencies of CSCs in PTGS2 -knockdown cell lines were measured by in vitro extreme limiting dilution assays. The dashed lines show 95% confidence interval (CI) of the frequency of CSCs.

    Techniques Used: Expressing, Translocation Assay, Staining, Confocal Microscopy, In Situ, Proximity Ligation Assay, Transfection, In Vitro

    Resveratrol inhibits mitochondrial fission and induces the suppression of NPC stemness by reducing the mitochondrial localization of COX-2 and p53. (A-B) CNE1 and CNE2 cells were treated with or without 100 μM resveratrol (RSV) for 24 h. (A) Confocal microscopy images of CNE1 and CNE2 cells immunostained with anti-COX-2 (green), anti-p53 (blue) antibodies, and MitoTracker (red). Manders' overlap coefficients for the co-localization of COX-2-mitochondria, p53-mitochondria, and COX-2-p53 are shown. Mitochondrial fragmentation counts were calculated by IPP6.0 and shown in bar graphs. (B) Whole cell lysates (WCL) and mitochondrial (Mito) and cytosolic (Cyto) fractions of CNE1 and CNE2 cells with or without treatment were prepared. WB assays were performed to determine the expression levels of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1 in WCL and those of COX-2, p53, p-Drp1 Ser616 in Mito and Cyto fractions. (C-D) CNE1 and CNE2 cells treated with 0, 50, 100 μM RSV for 24 h were harvested. (C) COX-2, ABCG2 and Oct4 protein level was determined by WB assays. (D) The proportion of SP cells was analyzed by FCM. (E) Quantification of SP cells in CNE1 and CNE2 was shown in bar graphs. * P < 0.05, compared with the Ctrl group.
    Figure Legend Snippet: Resveratrol inhibits mitochondrial fission and induces the suppression of NPC stemness by reducing the mitochondrial localization of COX-2 and p53. (A-B) CNE1 and CNE2 cells were treated with or without 100 μM resveratrol (RSV) for 24 h. (A) Confocal microscopy images of CNE1 and CNE2 cells immunostained with anti-COX-2 (green), anti-p53 (blue) antibodies, and MitoTracker (red). Manders' overlap coefficients for the co-localization of COX-2-mitochondria, p53-mitochondria, and COX-2-p53 are shown. Mitochondrial fragmentation counts were calculated by IPP6.0 and shown in bar graphs. (B) Whole cell lysates (WCL) and mitochondrial (Mito) and cytosolic (Cyto) fractions of CNE1 and CNE2 cells with or without treatment were prepared. WB assays were performed to determine the expression levels of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1 in WCL and those of COX-2, p53, p-Drp1 Ser616 in Mito and Cyto fractions. (C-D) CNE1 and CNE2 cells treated with 0, 50, 100 μM RSV for 24 h were harvested. (C) COX-2, ABCG2 and Oct4 protein level was determined by WB assays. (D) The proportion of SP cells was analyzed by FCM. (E) Quantification of SP cells in CNE1 and CNE2 was shown in bar graphs. * P < 0.05, compared with the Ctrl group.

    Techniques Used: Confocal Microscopy, Expressing

    Resveratrol sensitizes NPC cells to 5-FU by decreasing COX-2 and p-Drp1 Ser616 . (A-D) CNE1 and CNE2 cells were treated with 10 μM 5-FU in the presence or absence of resveratrol (RSV, 100 μM) for 24 h. (A) The co-localization of COX-2 (green), p53 (bule) and mitochondria (red) was imaged by confocal microscopy. Manders' overlap coefficients for the co-localization of COX-2 with mitochondria and the mitochondrial fragmentation counts were shown in bar graphs. (B) Expression of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, Mfn2, ABCG2 and Oct4 were detected using WB assay. (C) SP cells were measured by FCM. (D) Quantification of SP cells in CNE1 and CNE2 was shown in bar graphs. * P < 0.05, compared with the Ctrl group. # P < 0.05, compared with the 5-FU alone group. (E) CNE1 and CNE2 cells were treated with increasing concentrations of 5-FU (1.25-80 μM) with or without RSV (100 μM) for 24 h, and cell viability was measured with the MTT assay. * P < 0.05 for combination treatment vs. 5-FU alone. (F-G) CNE1 and CNE2 cells were treated with Ctrl, 5-FU (10 μM), RSV (100 μM) or a combination of 5-FU and RSV for 24 h. (F) The cell apoptosis rate detected by Annexin V-FITC assay and analyzed by FCM. * P < 0.05 as compared with Ctrl group, # P < 0.05 as compared with 5-FU alone group. (G) Expressions of BAX, Bcl-2, cleaved-caspase 3, and LC3 as detected using WB assay.
    Figure Legend Snippet: Resveratrol sensitizes NPC cells to 5-FU by decreasing COX-2 and p-Drp1 Ser616 . (A-D) CNE1 and CNE2 cells were treated with 10 μM 5-FU in the presence or absence of resveratrol (RSV, 100 μM) for 24 h. (A) The co-localization of COX-2 (green), p53 (bule) and mitochondria (red) was imaged by confocal microscopy. Manders' overlap coefficients for the co-localization of COX-2 with mitochondria and the mitochondrial fragmentation counts were shown in bar graphs. (B) Expression of COX-2, p-Drp1 Ser616 , p-Drp1 Ser637 , t-Drp1, Mfn2, ABCG2 and Oct4 were detected using WB assay. (C) SP cells were measured by FCM. (D) Quantification of SP cells in CNE1 and CNE2 was shown in bar graphs. * P < 0.05, compared with the Ctrl group. # P < 0.05, compared with the 5-FU alone group. (E) CNE1 and CNE2 cells were treated with increasing concentrations of 5-FU (1.25-80 μM) with or without RSV (100 μM) for 24 h, and cell viability was measured with the MTT assay. * P < 0.05 for combination treatment vs. 5-FU alone. (F-G) CNE1 and CNE2 cells were treated with Ctrl, 5-FU (10 μM), RSV (100 μM) or a combination of 5-FU and RSV for 24 h. (F) The cell apoptosis rate detected by Annexin V-FITC assay and analyzed by FCM. * P < 0.05 as compared with Ctrl group, # P < 0.05 as compared with 5-FU alone group. (G) Expressions of BAX, Bcl-2, cleaved-caspase 3, and LC3 as detected using WB assay.

    Techniques Used: Confocal Microscopy, Expressing, MTT Assay

    Resveratrol enhances the sensitivity of NPC to 5-FU in vivo. Nude mice bearing CNE2 cells as primary xenografts were randomly separated into 4 groups (n=6) and injected by tail vein with physiological saline (Ctrl), 5-FU (2 mg/kg), resveratrol (RSV, 50 mg/kg) or a combination of 5-FU and RSV every other days for five times. (A) The growth curves of the tumors in the four groups. Tumor volume=1/2 × length × width 2 . (B) Representative images of the xenograft tumors in the four groups. (C) Tumor weights in the four groups. (D) Sections of tumors were subjected IHC for evaluating the expression of COX-2, p-Drp1 Ser616 , ABCG2, and Oct4. Scale bars, 50 μm. The relative amounts of COX-2, p-Drp1 Ser616 , ABCG2 and Oct4 proteins determined by IPP 6.0 analysis are shown in the bar graphs (lower). (E) WB assays were employed to measure the expression levels of COX-2, p-Drp1 Ser616 , ABCG2, and Oct4 in representative tumor tissues (n=3). Quantification of the expression levels are shown in the bar graphs (lower photograph).* P < 0.05 for RSV, or 5-FU alone vs. control. # P < 0.05 for combination treatment vs. 5-FU alone.
    Figure Legend Snippet: Resveratrol enhances the sensitivity of NPC to 5-FU in vivo. Nude mice bearing CNE2 cells as primary xenografts were randomly separated into 4 groups (n=6) and injected by tail vein with physiological saline (Ctrl), 5-FU (2 mg/kg), resveratrol (RSV, 50 mg/kg) or a combination of 5-FU and RSV every other days for five times. (A) The growth curves of the tumors in the four groups. Tumor volume=1/2 × length × width 2 . (B) Representative images of the xenograft tumors in the four groups. (C) Tumor weights in the four groups. (D) Sections of tumors were subjected IHC for evaluating the expression of COX-2, p-Drp1 Ser616 , ABCG2, and Oct4. Scale bars, 50 μm. The relative amounts of COX-2, p-Drp1 Ser616 , ABCG2 and Oct4 proteins determined by IPP 6.0 analysis are shown in the bar graphs (lower). (E) WB assays were employed to measure the expression levels of COX-2, p-Drp1 Ser616 , ABCG2, and Oct4 in representative tumor tissues (n=3). Quantification of the expression levels are shown in the bar graphs (lower photograph).* P < 0.05 for RSV, or 5-FU alone vs. control. # P < 0.05 for combination treatment vs. 5-FU alone.

    Techniques Used: In Vivo, Injection, Expressing

    abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc abcg2
    Summary of the sequences of RT-PCR primers, the appropriate annealing temperature used in experiments, and product size.
    Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Quercetin Protects against Cadmium-Induced Renal Uric Acid Transport System Alteration and Lipid Metabolism Disorder in Rats"

    Article Title: Quercetin Protects against Cadmium-Induced Renal Uric Acid Transport System Alteration and Lipid Metabolism Disorder in Rats

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    doi: 10.1155/2012/548430

    Summary of the sequences of RT-PCR primers, the appropriate annealing temperature used in experiments, and product size.
    Figure Legend Snippet: Summary of the sequences of RT-PCR primers, the appropriate annealing temperature used in experiments, and product size.

    Techniques Used:

    Effects of a 4-week treatment of CdCl 2 and coadministration of quercetin on expression of RST (a), OAT1 (b), MRP4 (c), and ABCG2 (d) at mRNA levels and activity of Na + -K + -ATPase (e) in renal cortex of rats. The mRNA levels were normalized by GAPDH. Values are mean ± SEM of n = 4–6 in each group. P value CdCl 2 versus control at + < 0.05, ++ < 0.01, and +++ < 0.001; treatment versus CdCl 2 at *<0.05 and **<0.01 for LSD post hoc test.
    Figure Legend Snippet: Effects of a 4-week treatment of CdCl 2 and coadministration of quercetin on expression of RST (a), OAT1 (b), MRP4 (c), and ABCG2 (d) at mRNA levels and activity of Na + -K + -ATPase (e) in renal cortex of rats. The mRNA levels were normalized by GAPDH. Values are mean ± SEM of n = 4–6 in each group. P value CdCl 2 versus control at + < 0.05, ++ < 0.01, and +++ < 0.001; treatment versus CdCl 2 at *<0.05 and **<0.01 for LSD post hoc test.

    Techniques Used: Expressing, Activity Assay

    Effects of a 4-week treatment of CdCl 2 and coadministration of quercetin on expression of RST (a), OAT1 (b), MRP4 (c), and ABCG2 (d) at protein levels in renal cortex of rats. The protein levels were normalized by GAPDH. Values are mean ± SEM of n = 4–6 in each group. P value CdCl 2 versus control at + <0.05, ++ <0.01, +++ <0.001; treatment versus CdCl 2 at *<0.05, and **<0.01 for LSD post hoc test.
    Figure Legend Snippet: Effects of a 4-week treatment of CdCl 2 and coadministration of quercetin on expression of RST (a), OAT1 (b), MRP4 (c), and ABCG2 (d) at protein levels in renal cortex of rats. The protein levels were normalized by GAPDH. Values are mean ± SEM of n = 4–6 in each group. P value CdCl 2 versus control at + <0.05, ++ <0.01, +++ <0.001; treatment versus CdCl 2 at *<0.05, and **<0.01 for LSD post hoc test.

    Techniques Used: Expressing

    polyclonal antibodies against abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc polyclonal antibodies against abcg2
    Human lung adenocarcinoma cells (A549), human renal cancer cells (Caki-1),human colorectal cancer cells (DLD-1),human bladder cancer cells (T24) and human histiocytic lymphoma cells (U937) were used in this experiment. A, Western blotting analysis of whole cell lysates of various cancer cell lines. <t>ABCG2</t> was detected with a polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). Actin was used as a protein loading control. A representative blot of multiple experiments is shown. B , Relative contents of each protein were determined by densitometric scanning and were normalized using actin. C , Levels of accumulated ALA-mediated PpIX in various cancer cell lines. Bar graphs show flow cytometric analysis results of cellular PpIX content. Mean intensities of fluorescence (autofluorescence values) obtained from control experiments of each cell line were normalized to 100%. Results represent the mean ± SD of three independent experiments.
    Polyclonal Antibodies Against Abcg2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal antibodies against abcg2/product/Cell Signaling Technology Inc
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyclonal antibodies against abcg2 - by Bioz Stars, 2023-01
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    1) Product Images from "Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation"

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0050082

    Human lung adenocarcinoma cells (A549), human renal cancer cells (Caki-1),human colorectal cancer cells (DLD-1),human bladder cancer cells (T24) and human histiocytic lymphoma cells (U937) were used in this experiment. A, Western blotting analysis of whole cell lysates of various cancer cell lines. ABCG2 was detected with a polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). Actin was used as a protein loading control. A representative blot of multiple experiments is shown. B , Relative contents of each protein were determined by densitometric scanning and were normalized using actin. C , Levels of accumulated ALA-mediated PpIX in various cancer cell lines. Bar graphs show flow cytometric analysis results of cellular PpIX content. Mean intensities of fluorescence (autofluorescence values) obtained from control experiments of each cell line were normalized to 100%. Results represent the mean ± SD of three independent experiments.
    Figure Legend Snippet: Human lung adenocarcinoma cells (A549), human renal cancer cells (Caki-1),human colorectal cancer cells (DLD-1),human bladder cancer cells (T24) and human histiocytic lymphoma cells (U937) were used in this experiment. A, Western blotting analysis of whole cell lysates of various cancer cell lines. ABCG2 was detected with a polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). Actin was used as a protein loading control. A representative blot of multiple experiments is shown. B , Relative contents of each protein were determined by densitometric scanning and were normalized using actin. C , Levels of accumulated ALA-mediated PpIX in various cancer cell lines. Bar graphs show flow cytometric analysis results of cellular PpIX content. Mean intensities of fluorescence (autofluorescence values) obtained from control experiments of each cell line were normalized to 100%. Results represent the mean ± SD of three independent experiments.

    Techniques Used: Western Blot, Fluorescence

    Live cells cultured on glass coverslips were incubated with 25 nM of Mito Tracker Red CMXRos to label mitochondria ( red ); then they were fixed and processed for ABCG2 protein immunostaining ( green ). Confocal images were obtained from cells immunostained with mouse monoclonal anti-ABCG2 antibody (5D3; R&D Systems) and Alexa Fluor 488-conjugated goat anti-mouse IgG antibody. Insets show a magnified area, indicated by white arrows.
    Figure Legend Snippet: Live cells cultured on glass coverslips were incubated with 25 nM of Mito Tracker Red CMXRos to label mitochondria ( red ); then they were fixed and processed for ABCG2 protein immunostaining ( green ). Confocal images were obtained from cells immunostained with mouse monoclonal anti-ABCG2 antibody (5D3; R&D Systems) and Alexa Fluor 488-conjugated goat anti-mouse IgG antibody. Insets show a magnified area, indicated by white arrows.

    Techniques Used: Cell Culture, Incubation, Immunostaining

    A , Subcellular fractions were isolated by a centrifugation method as described in . ABCG2 was detected by western blotting analysis using polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). CoxIV, Actin, SEC23A, GM130, and Na, K-ATPase were used as organelle-specific markers of mitochondria, cytosol, endoplasmic reticulum, Golgi apparatus, and plasma membrane, respectively. A representative blot of multiple experiments is shown. B , Highly purified mitochondria were isolated by OptiPrep density gradient centrifugation as described in and the western blotting analysis was performed using antibodies as described in A. Equal volume of samples from both whole cell lysate and mitochondrial fraction of A549 cells were subjected to SDS-PAGE. A representative blot of multiple experiments is shown.
    Figure Legend Snippet: A , Subcellular fractions were isolated by a centrifugation method as described in . ABCG2 was detected by western blotting analysis using polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). CoxIV, Actin, SEC23A, GM130, and Na, K-ATPase were used as organelle-specific markers of mitochondria, cytosol, endoplasmic reticulum, Golgi apparatus, and plasma membrane, respectively. A representative blot of multiple experiments is shown. B , Highly purified mitochondria were isolated by OptiPrep density gradient centrifugation as described in and the western blotting analysis was performed using antibodies as described in A. Equal volume of samples from both whole cell lysate and mitochondrial fraction of A549 cells were subjected to SDS-PAGE. A representative blot of multiple experiments is shown.

    Techniques Used: Isolation, Centrifugation, Western Blot, Purification, Gradient Centrifugation, SDS Page

    A, Confocal immunofluorescence analysis of HEK cells and ST-HEK cells. Mitochondria, stained with Mito Tracker Red CMXRos; ABCG2, stained with monoclonal anti-FLAG IgG and Alexa Fluor 488-conjugated goat anti-mouse IgG. B, Western blotting analysis of mitochondrial fraction of HEK cells and ST-HEK cells. A representative blot of multiple experiments is shown.
    Figure Legend Snippet: A, Confocal immunofluorescence analysis of HEK cells and ST-HEK cells. Mitochondria, stained with Mito Tracker Red CMXRos; ABCG2, stained with monoclonal anti-FLAG IgG and Alexa Fluor 488-conjugated goat anti-mouse IgG. B, Western blotting analysis of mitochondrial fraction of HEK cells and ST-HEK cells. A representative blot of multiple experiments is shown.

    Techniques Used: Immunofluorescence, Staining, Western Blot

    Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with proteinase K on ice for 60 min in the presence or absence of 0.2% Triton X-100 (TX-100). Then the proteins were analyzed by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.
    Figure Legend Snippet: Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with proteinase K on ice for 60 min in the presence or absence of 0.2% Triton X-100 (TX-100). Then the proteins were analyzed by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.

    Techniques Used: Western Blot

    Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with PNGase F or Endo H, and then ABCG2 was detected by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.
    Figure Legend Snippet: Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with PNGase F or Endo H, and then ABCG2 was detected by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.

    Techniques Used: Western Blot

    abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc abcg2
    Scutellarin suppressed the expressions of multidrug-resistant proteins in glioma cells. Notes: The expressions of multidrug-resistant proteins including ABCB1 and <t>ABCG2</t> in cisplatin-resistant U87 ( A ) and U251 cells ( B ) were analyzed by Western blot. * P <0.05 vs control. ( C ) U87/DDP cells were transfected with si-control or si-ABCB1 for 24 hours, and cell apoptosis was detected. ( D ) U251/DDP cells were transfected with si-control or si-ABCB1 for 24 hours, and cell apoptosis was detected. * P <0.05 vs si-control. Data are represented as mean ± SD of three independent experiments.
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    1) Product Images from "Scutellarin inhibits the metastasis and cisplatin resistance in glioma cells"

    Article Title: Scutellarin inhibits the metastasis and cisplatin resistance in glioma cells

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S187426

    Scutellarin suppressed the expressions of multidrug-resistant proteins in glioma cells. Notes: The expressions of multidrug-resistant proteins including ABCB1 and ABCG2 in cisplatin-resistant U87 ( A ) and U251 cells ( B ) were analyzed by Western blot. * P <0.05 vs control. ( C ) U87/DDP cells were transfected with si-control or si-ABCB1 for 24 hours, and cell apoptosis was detected. ( D ) U251/DDP cells were transfected with si-control or si-ABCB1 for 24 hours, and cell apoptosis was detected. * P <0.05 vs si-control. Data are represented as mean ± SD of three independent experiments.
    Figure Legend Snippet: Scutellarin suppressed the expressions of multidrug-resistant proteins in glioma cells. Notes: The expressions of multidrug-resistant proteins including ABCB1 and ABCG2 in cisplatin-resistant U87 ( A ) and U251 cells ( B ) were analyzed by Western blot. * P <0.05 vs control. ( C ) U87/DDP cells were transfected with si-control or si-ABCB1 for 24 hours, and cell apoptosis was detected. ( D ) U251/DDP cells were transfected with si-control or si-ABCB1 for 24 hours, and cell apoptosis was detected. * P <0.05 vs si-control. Data are represented as mean ± SD of three independent experiments.

    Techniques Used: Western Blot, Transfection

    abcg2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc abcg2
    CD13 is an inducer to promote the MDR development of GC cells . (a) CD13 expression in typical tissue sections from advanced GC patients with or without chemotherapy treatment, was determined by immunohistochemistry analysis. Intuitive expression of CD13 was shown as brown or brownish-yellow particles. Normal gastric mucosa tissues were used as the normal controls. (b) Comparison of CD13 protein levels between nonchemotherapy and chemotherapy group in GC patients was carried out by western blotting analysis. The expression levels of CD13 were normalized to those of -actin, the horizontal line represents the median value, and the error bars indicate the SEM. ∗∗ P<0.01. (c) The protein expression of LRP, P-gp, MRP1, and <t>ABCG2</t> in parental cells and MDR GC cells was determined by western blotting analysis. Data are shown as representatives (left panels) and relative densities compared to β -actin from three independent experiments with means ± SD (right panels). ∗∗ P<0.01. (d) The expression of CD13 in parental cells and MDR GC cells was determined by western blotting analysis. Data are shown as representatives (upper panels) and relative gray values contrasted with β -actin from three independent experiments with means ±SD (bottom panels). ∗∗ P<0.01.
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    1) Product Images from "Ubenimex Reverses MDR in Gastric Cancer Cells by Activating Caspase-3-Mediated Apoptosis and Suppressing the Expression of Membrane Transport Proteins"

    Article Title: Ubenimex Reverses MDR in Gastric Cancer Cells by Activating Caspase-3-Mediated Apoptosis and Suppressing the Expression of Membrane Transport Proteins

    Journal: BioMed Research International

    doi: 10.1155/2019/4390839

    CD13 is an inducer to promote the MDR development of GC cells . (a) CD13 expression in typical tissue sections from advanced GC patients with or without chemotherapy treatment, was determined by immunohistochemistry analysis. Intuitive expression of CD13 was shown as brown or brownish-yellow particles. Normal gastric mucosa tissues were used as the normal controls. (b) Comparison of CD13 protein levels between nonchemotherapy and chemotherapy group in GC patients was carried out by western blotting analysis. The expression levels of CD13 were normalized to those of -actin, the horizontal line represents the median value, and the error bars indicate the SEM. ∗∗ P<0.01. (c) The protein expression of LRP, P-gp, MRP1, and ABCG2 in parental cells and MDR GC cells was determined by western blotting analysis. Data are shown as representatives (left panels) and relative densities compared to β -actin from three independent experiments with means ± SD (right panels). ∗∗ P<0.01. (d) The expression of CD13 in parental cells and MDR GC cells was determined by western blotting analysis. Data are shown as representatives (upper panels) and relative gray values contrasted with β -actin from three independent experiments with means ±SD (bottom panels). ∗∗ P<0.01.
    Figure Legend Snippet: CD13 is an inducer to promote the MDR development of GC cells . (a) CD13 expression in typical tissue sections from advanced GC patients with or without chemotherapy treatment, was determined by immunohistochemistry analysis. Intuitive expression of CD13 was shown as brown or brownish-yellow particles. Normal gastric mucosa tissues were used as the normal controls. (b) Comparison of CD13 protein levels between nonchemotherapy and chemotherapy group in GC patients was carried out by western blotting analysis. The expression levels of CD13 were normalized to those of -actin, the horizontal line represents the median value, and the error bars indicate the SEM. ∗∗ P<0.01. (c) The protein expression of LRP, P-gp, MRP1, and ABCG2 in parental cells and MDR GC cells was determined by western blotting analysis. Data are shown as representatives (left panels) and relative densities compared to β -actin from three independent experiments with means ± SD (right panels). ∗∗ P<0.01. (d) The expression of CD13 in parental cells and MDR GC cells was determined by western blotting analysis. Data are shown as representatives (upper panels) and relative gray values contrasted with β -actin from three independent experiments with means ±SD (bottom panels). ∗∗ P<0.01.

    Techniques Used: Expressing, Immunohistochemistry, Western Blot

    Ubenimex suppresses the expression of membrane transport proteins by inhibiting CD13 expression to enhance drug accumulation in GC cells . ((a) and (b)) Indicted cells were pretreated with or without pEGFP-N1-CD13 plasmid and then stimulated with Ubenimex. The expressions of P-gp, MRP1, LRP, and ABCG2 SGC7901/X (a) and MKN45/X (b) cells were determined via western blotting analysis. Representative results are shown (left panels) and the means ± SD are revealed (right panels). ∗ P < 0.05, ∗∗ P <0.01, and # P>0.05. ((c) and (d)) Effect of Ubenimex (400 μ mol/l) in the presence or absence of pEGFP-N1-CD13 plasmid on intracellular accumulation of 5-fluorouracil, oxaliplatin, and leucovorin in SGC7901/X cells (c) and MKN45/X (d) cells was evaluated via LC-MS/MS analysis. Data are expressed as means ±SD of three independent experiments. ∗∗ P < 0.01 and # P>0.05.
    Figure Legend Snippet: Ubenimex suppresses the expression of membrane transport proteins by inhibiting CD13 expression to enhance drug accumulation in GC cells . ((a) and (b)) Indicted cells were pretreated with or without pEGFP-N1-CD13 plasmid and then stimulated with Ubenimex. The expressions of P-gp, MRP1, LRP, and ABCG2 SGC7901/X (a) and MKN45/X (b) cells were determined via western blotting analysis. Representative results are shown (left panels) and the means ± SD are revealed (right panels). ∗ P < 0.05, ∗∗ P <0.01, and # P>0.05. ((c) and (d)) Effect of Ubenimex (400 μ mol/l) in the presence or absence of pEGFP-N1-CD13 plasmid on intracellular accumulation of 5-fluorouracil, oxaliplatin, and leucovorin in SGC7901/X cells (c) and MKN45/X (d) cells was evaluated via LC-MS/MS analysis. Data are expressed as means ±SD of three independent experiments. ∗∗ P < 0.01 and # P>0.05.

    Techniques Used: Expressing, Plasmid Preparation, Western Blot, Liquid Chromatography with Mass Spectroscopy

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    Cell Signaling Technology Inc abcg2
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    Cell Signaling Technology Inc rabbit anti abcg2 polyclonal antibody
    Expression of <t>ABCG2</t> in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.
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    Expression of <t>ABCG2</t> in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.
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    Human lung adenocarcinoma cells (A549), human renal cancer cells (Caki-1),human colorectal cancer cells (DLD-1),human bladder cancer cells (T24) and human histiocytic lymphoma cells (U937) were used in this experiment. A, Western blotting analysis of whole cell lysates of various cancer cell lines. <t>ABCG2</t> was detected with a polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). Actin was used as a protein loading control. A representative blot of multiple experiments is shown. B , Relative contents of each protein were determined by densitometric scanning and were normalized using actin. C , Levels of accumulated ALA-mediated PpIX in various cancer cell lines. Bar graphs show flow cytometric analysis results of cellular PpIX content. Mean intensities of fluorescence (autofluorescence values) obtained from control experiments of each cell line were normalized to 100%. Results represent the mean ± SD of three independent experiments.
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    Primer sequences.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway

    doi: 10.1155/2022/3032407

    Figure Lengend Snippet: Primer sequences.

    Article Snippet: The primary antibodies used were MDR1/ABCB1 (CST, USA), ABCG2 (CST, USA), MRP4/ABCC4 (CST, USA), JNK2 (CST, USA), phospho-SAPK/JNK (CST, USA), and GAPDH (CST, USA).

    Techniques: Sequencing

    Effect of ZJW on the expression of the drug resistance-related proteins MDR1/ABCB1, MRP4/ABCC4, and ABCG2 in HCT116/L-OHP cells. (a and b) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 proteins in HCT116 cells and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. (c) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in HCT116 and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001 compared to HCT116/L.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway

    doi: 10.1155/2022/3032407

    Figure Lengend Snippet: Effect of ZJW on the expression of the drug resistance-related proteins MDR1/ABCB1, MRP4/ABCC4, and ABCG2 in HCT116/L-OHP cells. (a and b) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 proteins in HCT116 cells and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. (c) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in HCT116 and HCT116/L-OHP cells treated with L-OHP combined with different concentrations of ZJW. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001 compared to HCT116/L.

    Article Snippet: The primary antibodies used were MDR1/ABCB1 (CST, USA), ABCG2 (CST, USA), MRP4/ABCC4 (CST, USA), JNK2 (CST, USA), phospho-SAPK/JNK (CST, USA), and GAPDH (CST, USA).

    Techniques: Expressing, Western Blot, Real-time Polymerase Chain Reaction

    Effect of ZJW on the expression of drug resistance-related proteins in vivo. (a and b) Immunofluorescence detection of MDR1/ABCB1 and ABCG2 proteins in vivo. (c and d) Immunohistochemistry detection of MRP4/ABCC4 protein in vivo. (e and f) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. (g) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001; ∗∗∗∗ , P < 0.0001; ns, no significance compared to MODEL.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: Zuo Jin Wan Reverses the Resistance of Colorectal Cancer to Oxaliplatin by Regulating the MALAT1/miR-200s/JNK Signaling Pathway

    doi: 10.1155/2022/3032407

    Figure Lengend Snippet: Effect of ZJW on the expression of drug resistance-related proteins in vivo. (a and b) Immunofluorescence detection of MDR1/ABCB1 and ABCG2 proteins in vivo. (c and d) Immunohistochemistry detection of MRP4/ABCC4 protein in vivo. (e and f) Western blot assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. (g) Real-time PCR assay of ABCG2, MDR1/ABCB1, and MRP4/ABCC4 levels in vivo. ∗ , P < 0.05; ∗∗ , P < 0.01; ∗∗∗ , P < 0.001; ∗∗∗∗ , P < 0.0001; ns, no significance compared to MODEL.

    Article Snippet: The primary antibodies used were MDR1/ABCB1 (CST, USA), ABCG2 (CST, USA), MRP4/ABCC4 (CST, USA), JNK2 (CST, USA), phospho-SAPK/JNK (CST, USA), and GAPDH (CST, USA).

    Techniques: Expressing, In Vivo, Immunofluorescence, Immunohistochemistry, Western Blot, Real-time Polymerase Chain Reaction

    Expression of ABCG2 in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: Expression of ABCG2 in human HCC tissues. (a) ABCG2 was expressed in placenta tissues (positive control). (b) Primary antibody omitted placenta tissue slide was set as negative control. (c) Positive ABCG2 expression in HCC tissue. (d) Negative ABCG2 expression in HCC tissue.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques: Expressing, Positive Control, Negative Control

     ABCG2  expression and characteristics of patients.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: ABCG2 expression and characteristics of patients.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques: Expressing

    ABCG2 was expressed in a minor population of SMMC-7721 cells. (a) The positive rate of ABCG2 in SMMC-7721 cells determined by flow cytometry was about 8.8% before cell sorting. P2 gate represents ABCG2 positive cells. Mouse IgG2b was used as isotype control. (b) Positive rate of ABCG2 in sorted ABCG2+/ABCG2− cells after 3 passages of culture. (c) Detection of ABCG2 protein level in freshly sorted cells by western blot. β -Actin was used as loading control. The optical density of specific bands was quantified and normalized to β -Actin. ** P < 0.01.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: ABCG2 was expressed in a minor population of SMMC-7721 cells. (a) The positive rate of ABCG2 in SMMC-7721 cells determined by flow cytometry was about 8.8% before cell sorting. P2 gate represents ABCG2 positive cells. Mouse IgG2b was used as isotype control. (b) Positive rate of ABCG2 in sorted ABCG2+/ABCG2− cells after 3 passages of culture. (c) Detection of ABCG2 protein level in freshly sorted cells by western blot. β -Actin was used as loading control. The optical density of specific bands was quantified and normalized to β -Actin. ** P < 0.01.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques: Flow Cytometry, FACS, Western Blot

    Difference of tumorigenic ability between  ABCG2+  and ABCG2− cells.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: Difference of tumorigenic ability between ABCG2+ and ABCG2− cells.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques:

    Expression level of ABCG2 correlated with cell proliferation and chemoresistance. (a), (b) Freshly sorted ABCG2+ cells were transfected with ABCG2-specific siRNA. ABCG2− cells were transfected with ABCG2-overexpression plasmid. The proliferation of cells after transfection was compared with untransfected cells and negative control (scrambled siRNA or empty plasmid) using MTT assay after indicated time. (c), (d) The expression level of ABCG2 was manipulated as described above. Survival rates after exposure to indicated dose of doxorubicin for 24 h were determined by MTT assay. (e), (f) IC50 value to doxorubicin was calculated for different groups. ** P < 0.01.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: Expression level of ABCG2 correlated with cell proliferation and chemoresistance. (a), (b) Freshly sorted ABCG2+ cells were transfected with ABCG2-specific siRNA. ABCG2− cells were transfected with ABCG2-overexpression plasmid. The proliferation of cells after transfection was compared with untransfected cells and negative control (scrambled siRNA or empty plasmid) using MTT assay after indicated time. (c), (d) The expression level of ABCG2 was manipulated as described above. Survival rates after exposure to indicated dose of doxorubicin for 24 h were determined by MTT assay. (e), (f) IC50 value to doxorubicin was calculated for different groups. ** P < 0.01.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques: Expressing, Transfection, Over Expression, Plasmid Preparation, Negative Control, MTT Assay

    RNA interference and plasmid-mediated overexpression of ABCG2 in SMMC-7721 cells. (a) RT-PCR analysis of ABCG2 mRNA in SMCC-7721 cells after transfection with siRNA or plasmid for 48 h. Normal SMMC-7721 cells were used as blank control. Scrambled siRNA was set as negative control. For overexpression, empty plasmid was transfected as negative control. (b), (c) Western blot analysis confirmed the efficiency of downregulation of ABCG2 by siRNA and upregulation by overexpression, respectively. β -Actin served as loading control. The optical density was quantified and normalized to β -Actin. ** P < 0.01, *** P < 0.001.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: RNA interference and plasmid-mediated overexpression of ABCG2 in SMMC-7721 cells. (a) RT-PCR analysis of ABCG2 mRNA in SMCC-7721 cells after transfection with siRNA or plasmid for 48 h. Normal SMMC-7721 cells were used as blank control. Scrambled siRNA was set as negative control. For overexpression, empty plasmid was transfected as negative control. (b), (c) Western blot analysis confirmed the efficiency of downregulation of ABCG2 by siRNA and upregulation by overexpression, respectively. β -Actin served as loading control. The optical density was quantified and normalized to β -Actin. ** P < 0.01, *** P < 0.001.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques: Plasmid Preparation, Over Expression, Reverse Transcription Polymerase Chain Reaction, Transfection, Negative Control, Western Blot

    Downregulation or upregulation of ABCG2 had effect on migration and invasion potential in HCC cells. (a), (b) Wound healing assay evaluated the potential of migration of HCC cells. Untreated cells served as normal control. ABCG2+ cells were transfected with ABCG2 siRNA while ABCG2− cells were transfected with ABCG2-expressing plasmid. Scrambled siRNA and empty plasmid were used as negative control. The pictures above represent the wound right after tip scratch. Pictures below showed wound-healing status after 48 h. (c), (d) Results of transwell invasion assay. After 48 h of invasion, cells invaded to the lower chamber were stained and photographed. Invaded cells were counted in three random visions and the average numbers were presented. *** P < 0.001.

    Journal: Gastroenterology Research and Practice

    Article Title: Expression of Potential Cancer Stem Cell Marker ABCG2 is Associated with Malignant Behaviors of Hepatocellular Carcinoma

    doi: 10.1155/2013/782581

    Figure Lengend Snippet: Downregulation or upregulation of ABCG2 had effect on migration and invasion potential in HCC cells. (a), (b) Wound healing assay evaluated the potential of migration of HCC cells. Untreated cells served as normal control. ABCG2+ cells were transfected with ABCG2 siRNA while ABCG2− cells were transfected with ABCG2-expressing plasmid. Scrambled siRNA and empty plasmid were used as negative control. The pictures above represent the wound right after tip scratch. Pictures below showed wound-healing status after 48 h. (c), (d) Results of transwell invasion assay. After 48 h of invasion, cells invaded to the lower chamber were stained and photographed. Invaded cells were counted in three random visions and the average numbers were presented. *** P < 0.001.

    Article Snippet: Sections were incubated with rabbit anti-ABCG2 polyclonal antibody (1 : 200, 4477S, Cell Signaling Technology, Danvers, MA) and rabbit anti-Ki67 monoclonal antibody (1 : 900, ab16667, Abcam, Cambridge, MA) at 4°C overnight.

    Techniques: Migration, Wound Healing Assay, Transfection, Expressing, Plasmid Preparation, Negative Control, Transwell Invasion Assay, Staining

    Human lung adenocarcinoma cells (A549), human renal cancer cells (Caki-1),human colorectal cancer cells (DLD-1),human bladder cancer cells (T24) and human histiocytic lymphoma cells (U937) were used in this experiment. A, Western blotting analysis of whole cell lysates of various cancer cell lines. ABCG2 was detected with a polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). Actin was used as a protein loading control. A representative blot of multiple experiments is shown. B , Relative contents of each protein were determined by densitometric scanning and were normalized using actin. C , Levels of accumulated ALA-mediated PpIX in various cancer cell lines. Bar graphs show flow cytometric analysis results of cellular PpIX content. Mean intensities of fluorescence (autofluorescence values) obtained from control experiments of each cell line were normalized to 100%. Results represent the mean ± SD of three independent experiments.

    Journal: PLoS ONE

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    doi: 10.1371/journal.pone.0050082

    Figure Lengend Snippet: Human lung adenocarcinoma cells (A549), human renal cancer cells (Caki-1),human colorectal cancer cells (DLD-1),human bladder cancer cells (T24) and human histiocytic lymphoma cells (U937) were used in this experiment. A, Western blotting analysis of whole cell lysates of various cancer cell lines. ABCG2 was detected with a polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). Actin was used as a protein loading control. A representative blot of multiple experiments is shown. B , Relative contents of each protein were determined by densitometric scanning and were normalized using actin. C , Levels of accumulated ALA-mediated PpIX in various cancer cell lines. Bar graphs show flow cytometric analysis results of cellular PpIX content. Mean intensities of fluorescence (autofluorescence values) obtained from control experiments of each cell line were normalized to 100%. Results represent the mean ± SD of three independent experiments.

    Article Snippet: Polyclonal antibodies against ABCG2 (Cat. #4477), cytochrome c oxidase subunit IV (CoxIV), Na, K-ATPase, GM130, and Alexa Fluor 488-conjugated goat anti-mouse IgG were from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Western Blot, Fluorescence

    Live cells cultured on glass coverslips were incubated with 25 nM of Mito Tracker Red CMXRos to label mitochondria ( red ); then they were fixed and processed for ABCG2 protein immunostaining ( green ). Confocal images were obtained from cells immunostained with mouse monoclonal anti-ABCG2 antibody (5D3; R&D Systems) and Alexa Fluor 488-conjugated goat anti-mouse IgG antibody. Insets show a magnified area, indicated by white arrows.

    Journal: PLoS ONE

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    doi: 10.1371/journal.pone.0050082

    Figure Lengend Snippet: Live cells cultured on glass coverslips were incubated with 25 nM of Mito Tracker Red CMXRos to label mitochondria ( red ); then they were fixed and processed for ABCG2 protein immunostaining ( green ). Confocal images were obtained from cells immunostained with mouse monoclonal anti-ABCG2 antibody (5D3; R&D Systems) and Alexa Fluor 488-conjugated goat anti-mouse IgG antibody. Insets show a magnified area, indicated by white arrows.

    Article Snippet: Polyclonal antibodies against ABCG2 (Cat. #4477), cytochrome c oxidase subunit IV (CoxIV), Na, K-ATPase, GM130, and Alexa Fluor 488-conjugated goat anti-mouse IgG were from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Cell Culture, Incubation, Immunostaining

    A , Subcellular fractions were isolated by a centrifugation method as described in . ABCG2 was detected by western blotting analysis using polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). CoxIV, Actin, SEC23A, GM130, and Na, K-ATPase were used as organelle-specific markers of mitochondria, cytosol, endoplasmic reticulum, Golgi apparatus, and plasma membrane, respectively. A representative blot of multiple experiments is shown. B , Highly purified mitochondria were isolated by OptiPrep density gradient centrifugation as described in and the western blotting analysis was performed using antibodies as described in A. Equal volume of samples from both whole cell lysate and mitochondrial fraction of A549 cells were subjected to SDS-PAGE. A representative blot of multiple experiments is shown.

    Journal: PLoS ONE

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    doi: 10.1371/journal.pone.0050082

    Figure Lengend Snippet: A , Subcellular fractions were isolated by a centrifugation method as described in . ABCG2 was detected by western blotting analysis using polyclonal anti-ABCG2 (Cat. #4477; Cell Signaling Technology). CoxIV, Actin, SEC23A, GM130, and Na, K-ATPase were used as organelle-specific markers of mitochondria, cytosol, endoplasmic reticulum, Golgi apparatus, and plasma membrane, respectively. A representative blot of multiple experiments is shown. B , Highly purified mitochondria were isolated by OptiPrep density gradient centrifugation as described in and the western blotting analysis was performed using antibodies as described in A. Equal volume of samples from both whole cell lysate and mitochondrial fraction of A549 cells were subjected to SDS-PAGE. A representative blot of multiple experiments is shown.

    Article Snippet: Polyclonal antibodies against ABCG2 (Cat. #4477), cytochrome c oxidase subunit IV (CoxIV), Na, K-ATPase, GM130, and Alexa Fluor 488-conjugated goat anti-mouse IgG were from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Isolation, Centrifugation, Western Blot, Purification, Gradient Centrifugation, SDS Page

    A, Confocal immunofluorescence analysis of HEK cells and ST-HEK cells. Mitochondria, stained with Mito Tracker Red CMXRos; ABCG2, stained with monoclonal anti-FLAG IgG and Alexa Fluor 488-conjugated goat anti-mouse IgG. B, Western blotting analysis of mitochondrial fraction of HEK cells and ST-HEK cells. A representative blot of multiple experiments is shown.

    Journal: PLoS ONE

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    doi: 10.1371/journal.pone.0050082

    Figure Lengend Snippet: A, Confocal immunofluorescence analysis of HEK cells and ST-HEK cells. Mitochondria, stained with Mito Tracker Red CMXRos; ABCG2, stained with monoclonal anti-FLAG IgG and Alexa Fluor 488-conjugated goat anti-mouse IgG. B, Western blotting analysis of mitochondrial fraction of HEK cells and ST-HEK cells. A representative blot of multiple experiments is shown.

    Article Snippet: Polyclonal antibodies against ABCG2 (Cat. #4477), cytochrome c oxidase subunit IV (CoxIV), Na, K-ATPase, GM130, and Alexa Fluor 488-conjugated goat anti-mouse IgG were from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Immunofluorescence, Staining, Western Blot

    Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with proteinase K on ice for 60 min in the presence or absence of 0.2% Triton X-100 (TX-100). Then the proteins were analyzed by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.

    Journal: PLoS ONE

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    doi: 10.1371/journal.pone.0050082

    Figure Lengend Snippet: Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with proteinase K on ice for 60 min in the presence or absence of 0.2% Triton X-100 (TX-100). Then the proteins were analyzed by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.

    Article Snippet: Polyclonal antibodies against ABCG2 (Cat. #4477), cytochrome c oxidase subunit IV (CoxIV), Na, K-ATPase, GM130, and Alexa Fluor 488-conjugated goat anti-mouse IgG were from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Western Blot

    Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with PNGase F or Endo H, and then ABCG2 was detected by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.

    Journal: PLoS ONE

    Article Title: Mitochondrial Localization of ABC Transporter ABCG2 and Its Function in 5-Aminolevulinic Acid-Mediated Protoporphyrin IX Accumulation

    doi: 10.1371/journal.pone.0050082

    Figure Lengend Snippet: Mitochondrial preparations of A549 cells (A) and ST-HEK cells (B) were treated with PNGase F or Endo H, and then ABCG2 was detected by Western blotting using a polyclonal anti-ABCG2 antibody. A representative blot of three independent experiments is shown.

    Article Snippet: Polyclonal antibodies against ABCG2 (Cat. #4477), cytochrome c oxidase subunit IV (CoxIV), Na, K-ATPase, GM130, and Alexa Fluor 488-conjugated goat anti-mouse IgG were from Cell Signaling Technology (Danvers, MA, USA).

    Techniques: Western Blot