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prs shepha2 plasmids expressing shrnas against human epha2  (OriGene)


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    OriGene prs shepha2 plasmids expressing shrnas against human epha2
    Progranulin, Ephrin-A1, and <t>EphA2</t> expression in bladder cancer. (A) mRNA levels of GRN and EFNA1 in normal or urothelial carcinomas of low and high grade (Oncomine). (B) Steady state levels of progranulin (GRN) and ephrin-A1 (EFNA1) in T24 and UMUC-3 cells; mean ±SEM, n = 3. (C) Micrographs from the human protein Atlas depicting representative images of normal bladder and low or high-grade urothelial carcinomas. (D) EphA2 expression levels in bladder cancer tissues using IHC on a bladder cancer TMA. (E) Quantification of EphA2 expression in tissues using ImageJ; bladder, n = 27; T1-T4 urothelial carcinomas, n = 123; ***p<0.001. (F) EphA2 expression in various urothelial cancer cells by immunoblot using anti-EphA2 and anti-β-actin antibodies.
    Prs Shepha2 Plasmids Expressing Shrnas Against Human Epha2, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/prs+shepha2+plasmids+expressing+shrnas+against+human+epha2/Eph+receptor+A2+(EPHA2)+Human+shRNA+Plasmid+Kit/pmc08162889-282-23-30
    Average 90 stars, based on 1 article reviews
    prs shepha2 plasmids expressing shrnas against human epha2 - by Bioz Stars, 2026-09
    90/100 stars

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    1) Product Images from "Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer"

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    doi: 10.1016/j.matbio.2020.03.009

    Progranulin, Ephrin-A1, and EphA2 expression in bladder cancer. (A) mRNA levels of GRN and EFNA1 in normal or urothelial carcinomas of low and high grade (Oncomine). (B) Steady state levels of progranulin (GRN) and ephrin-A1 (EFNA1) in T24 and UMUC-3 cells; mean ±SEM, n = 3. (C) Micrographs from the human protein Atlas depicting representative images of normal bladder and low or high-grade urothelial carcinomas. (D) EphA2 expression levels in bladder cancer tissues using IHC on a bladder cancer TMA. (E) Quantification of EphA2 expression in tissues using ImageJ; bladder, n = 27; T1-T4 urothelial carcinomas, n = 123; ***p<0.001. (F) EphA2 expression in various urothelial cancer cells by immunoblot using anti-EphA2 and anti-β-actin antibodies.
    Figure Legend Snippet: Progranulin, Ephrin-A1, and EphA2 expression in bladder cancer. (A) mRNA levels of GRN and EFNA1 in normal or urothelial carcinomas of low and high grade (Oncomine). (B) Steady state levels of progranulin (GRN) and ephrin-A1 (EFNA1) in T24 and UMUC-3 cells; mean ±SEM, n = 3. (C) Micrographs from the human protein Atlas depicting representative images of normal bladder and low or high-grade urothelial carcinomas. (D) EphA2 expression levels in bladder cancer tissues using IHC on a bladder cancer TMA. (E) Quantification of EphA2 expression in tissues using ImageJ; bladder, n = 27; T1-T4 urothelial carcinomas, n = 123; ***p<0.001. (F) EphA2 expression in various urothelial cancer cells by immunoblot using anti-EphA2 and anti-β-actin antibodies.

    Techniques Used: Expressing, Western Blot

    Progranulin evokes EphA2 phosphorylation. Serum-starved T24 cells were exposed to progranulin (150 nM, 15 min) and immunoprecipitated with anti-EphA2 antibodies. Coomassie-stained bands of interest were trypsin-digested and analyzed by LC-MS/MS on a Q Exactive™ Plus mass spec. The mass spec data were probed against the UniProt human database for STY phosphorylation. False discovery rate for peptides/site identifications was set at 1%. (A) Modifications of various residues shown as the sum of MS peptides intensities. (B) EphA2 schematic showing the location of phosphorylated residues. (C-D) Western immunoblots of serum-starved T24 cells exposed to 150 nM progranulin using several Phospho-specific and total antibodies. (E) Western immunoblots of serum-starved 5637 cells after progranulin stimulation ±specific inhibitors for PI3K pathway (LY294002, 20 μM) or Erk1/2 (U0126, 10 μM). (F) Phospho-EphA2 (Ser897) assessed by immunoblot in UMUC-3/shScr (control) and UMUC-3/shPGRN cells. (G) Inhibition of EphA2 kinase activity blocks progranulin-induced phosphorylation. Western immunoblots of serum-starved T24 cells exposed to Ephrin-A1-Fc (2.1 nM) or progranulin (150 nM) for 15 min ±ALW-II-41–27 (1 μM), and probed with Phospho-EphA2 (Ser897) and EphA2 antibodies.
    Figure Legend Snippet: Progranulin evokes EphA2 phosphorylation. Serum-starved T24 cells were exposed to progranulin (150 nM, 15 min) and immunoprecipitated with anti-EphA2 antibodies. Coomassie-stained bands of interest were trypsin-digested and analyzed by LC-MS/MS on a Q Exactive™ Plus mass spec. The mass spec data were probed against the UniProt human database for STY phosphorylation. False discovery rate for peptides/site identifications was set at 1%. (A) Modifications of various residues shown as the sum of MS peptides intensities. (B) EphA2 schematic showing the location of phosphorylated residues. (C-D) Western immunoblots of serum-starved T24 cells exposed to 150 nM progranulin using several Phospho-specific and total antibodies. (E) Western immunoblots of serum-starved 5637 cells after progranulin stimulation ±specific inhibitors for PI3K pathway (LY294002, 20 μM) or Erk1/2 (U0126, 10 μM). (F) Phospho-EphA2 (Ser897) assessed by immunoblot in UMUC-3/shScr (control) and UMUC-3/shPGRN cells. (G) Inhibition of EphA2 kinase activity blocks progranulin-induced phosphorylation. Western immunoblots of serum-starved T24 cells exposed to Ephrin-A1-Fc (2.1 nM) or progranulin (150 nM) for 15 min ±ALW-II-41–27 (1 μM), and probed with Phospho-EphA2 (Ser897) and EphA2 antibodies.

    Techniques Used: Phospho-proteomics, Immunoprecipitation, Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Western Blot, Control, Inhibition, Activity Assay

    EphA2 is required for progranulin-evoked activity and cisplatin sensitivity. (A) EphA2 was depleted in UMUC-3 cells by siRNA approaches and EphA2 expression levels were assessed by immunoblot with anti-EphA2 polyclonal antibodies and normalized over β-actin content. Densitometric analysis was performed using ImageJ (National Institutes of Health) and expressed as arbitrary units. (B) Motility assays in Boyden chambers ±progranulin, ***p<0.001. (C) Anchorage-independent growth in soft-agar was performed as described in Materials and Methods ***p<0.001. (D) Cell survival as assessed by a Colorimetric Cell Cytotoxicity Assay Kit at various cisplatin concentrations. Mean ±SD; n = 3 biological replicates run in duplicates. **p<0.005; ***p<0.001.
    Figure Legend Snippet: EphA2 is required for progranulin-evoked activity and cisplatin sensitivity. (A) EphA2 was depleted in UMUC-3 cells by siRNA approaches and EphA2 expression levels were assessed by immunoblot with anti-EphA2 polyclonal antibodies and normalized over β-actin content. Densitometric analysis was performed using ImageJ (National Institutes of Health) and expressed as arbitrary units. (B) Motility assays in Boyden chambers ±progranulin, ***p<0.001. (C) Anchorage-independent growth in soft-agar was performed as described in Materials and Methods ***p<0.001. (D) Cell survival as assessed by a Colorimetric Cell Cytotoxicity Assay Kit at various cisplatin concentrations. Mean ±SD; n = 3 biological replicates run in duplicates. **p<0.005; ***p<0.001.

    Techniques Used: Activity Assay, Expressing, Western Blot, Cytotoxicity Assay

    EphA2 interacts with liprinα–1 and vinculin. (A) EphA2 interactome involved in cell motility as identified by proteomics. (B) Co-immunoprecipitation and western immunoblot of serum-starved T24 cells ±progranulin (150 nM) with the indicated antibodies. (C) Immunoblot of Liprinα–1 and vinculin in various urothelial carcinoma cells. (D) Co-localization of EphA2/liprinα–1 assessed by confocal microscopy. Insets = higher magnification of the relative areas within the white boxes. Bar = 10 μm. (E) Western immunoblot of liprinα–1- depleted T24 cells. (F) Quantification of T24 cell lateral motility determined by wound healing assays as previously described [18,19,26]. p = 0.000666.
    Figure Legend Snippet: EphA2 interacts with liprinα–1 and vinculin. (A) EphA2 interactome involved in cell motility as identified by proteomics. (B) Co-immunoprecipitation and western immunoblot of serum-starved T24 cells ±progranulin (150 nM) with the indicated antibodies. (C) Immunoblot of Liprinα–1 and vinculin in various urothelial carcinoma cells. (D) Co-localization of EphA2/liprinα–1 assessed by confocal microscopy. Insets = higher magnification of the relative areas within the white boxes. Bar = 10 μm. (E) Western immunoblot of liprinα–1- depleted T24 cells. (F) Quantification of T24 cell lateral motility determined by wound healing assays as previously described [18,19,26]. p = 0.000666.

    Techniques Used: Immunoprecipitation, Western Blot, Confocal Microscopy

    Mechanism of progranulin-dependent EphA2 activation. Scheme depicting progranulin-induced EphA2 activation at Tyr588 and resultant Akt/MAPK feedback loop to phosphorylate Ser897.
    Figure Legend Snippet: Mechanism of progranulin-dependent EphA2 activation. Scheme depicting progranulin-induced EphA2 activation at Tyr588 and resultant Akt/MAPK feedback loop to phosphorylate Ser897.

    Techniques Used: Activation Assay

    Related Articles

    Stable Transfection:

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer
    Article Snippet: The specific EphA2 inhibitor ALW-II-41–27 (1 μM) was from Cayman Chemical and was resuspended and utilized according to the manufacturer’s instructions. .. Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus). ..

    Generated:

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer
    Article Snippet: The specific EphA2 inhibitor ALW-II-41–27 (1 μM) was from Cayman Chemical and was resuspended and utilized according to the manufacturer’s instructions. .. Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus). ..

    Expressing:

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer
    Article Snippet: The specific EphA2 inhibitor ALW-II-41–27 (1 μM) was from Cayman Chemical and was resuspended and utilized according to the manufacturer’s instructions. .. Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus). ..

    Transfection:

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer
    Article Snippet: The specific EphA2 inhibitor ALW-II-41–27 (1 μM) was from Cayman Chemical and was resuspended and utilized according to the manufacturer’s instructions. .. Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus). ..



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    prs shepha2 plasmids expressing shrnas against human epha2  (OriGene)
    90
    OriGene prs shepha2 plasmids expressing shrnas against human epha2
    Progranulin, Ephrin-A1, and <t>EphA2</t> expression in bladder cancer. (A) mRNA levels of GRN and EFNA1 in normal or urothelial carcinomas of low and high grade (Oncomine). (B) Steady state levels of progranulin (GRN) and ephrin-A1 (EFNA1) in T24 and UMUC-3 cells; mean ±SEM, n = 3. (C) Micrographs from the human protein Atlas depicting representative images of normal bladder and low or high-grade urothelial carcinomas. (D) EphA2 expression levels in bladder cancer tissues using IHC on a bladder cancer TMA. (E) Quantification of EphA2 expression in tissues using ImageJ; bladder, n = 27; T1-T4 urothelial carcinomas, n = 123; ***p<0.001. (F) EphA2 expression in various urothelial cancer cells by immunoblot using anti-EphA2 and anti-β-actin antibodies.
    Prs Shepha2 Plasmids Expressing Shrnas Against Human Epha2, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/prs+shepha2+plasmids+expressing+shrnas+against+human+epha2/Eph+receptor+A2+(EPHA2)+Human+shRNA+Plasmid+Kit/pmc08162889-282-23-30
    Average 90 stars, based on 1 article reviews
    prs shepha2 plasmids expressing shrnas against human epha2 - by Bioz Stars, 2026-09
    90/100 stars
    		  Buy from Supplier

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    Progranulin, Ephrin-A1, and EphA2 expression in bladder cancer. (A) mRNA levels of GRN and EFNA1 in normal or urothelial carcinomas of low and high grade (Oncomine). (B) Steady state levels of progranulin (GRN) and ephrin-A1 (EFNA1) in T24 and UMUC-3 cells; mean ±SEM, n = 3. (C) Micrographs from the human protein Atlas depicting representative images of normal bladder and low or high-grade urothelial carcinomas. (D) EphA2 expression levels in bladder cancer tissues using IHC on a bladder cancer TMA. (E) Quantification of EphA2 expression in tissues using ImageJ; bladder, n = 27; T1-T4 urothelial carcinomas, n = 123; ***p<0.001. (F) EphA2 expression in various urothelial cancer cells by immunoblot using anti-EphA2 and anti-β-actin antibodies.

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer

    doi: 10.1016/j.matbio.2020.03.009

    Figure Lengend Snippet: Progranulin, Ephrin-A1, and EphA2 expression in bladder cancer. (A) mRNA levels of GRN and EFNA1 in normal or urothelial carcinomas of low and high grade (Oncomine). (B) Steady state levels of progranulin (GRN) and ephrin-A1 (EFNA1) in T24 and UMUC-3 cells; mean ±SEM, n = 3. (C) Micrographs from the human protein Atlas depicting representative images of normal bladder and low or high-grade urothelial carcinomas. (D) EphA2 expression levels in bladder cancer tissues using IHC on a bladder cancer TMA. (E) Quantification of EphA2 expression in tissues using ImageJ; bladder, n = 27; T1-T4 urothelial carcinomas, n = 123; ***p<0.001. (F) EphA2 expression in various urothelial cancer cells by immunoblot using anti-EphA2 and anti-β-actin antibodies.

    Article Snippet: Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus).

    Techniques: Expressing, Western Blot

    Progranulin evokes EphA2 phosphorylation. Serum-starved T24 cells were exposed to progranulin (150 nM, 15 min) and immunoprecipitated with anti-EphA2 antibodies. Coomassie-stained bands of interest were trypsin-digested and analyzed by LC-MS/MS on a Q Exactive™ Plus mass spec. The mass spec data were probed against the UniProt human database for STY phosphorylation. False discovery rate for peptides/site identifications was set at 1%. (A) Modifications of various residues shown as the sum of MS peptides intensities. (B) EphA2 schematic showing the location of phosphorylated residues. (C-D) Western immunoblots of serum-starved T24 cells exposed to 150 nM progranulin using several Phospho-specific and total antibodies. (E) Western immunoblots of serum-starved 5637 cells after progranulin stimulation ±specific inhibitors for PI3K pathway (LY294002, 20 μM) or Erk1/2 (U0126, 10 μM). (F) Phospho-EphA2 (Ser897) assessed by immunoblot in UMUC-3/shScr (control) and UMUC-3/shPGRN cells. (G) Inhibition of EphA2 kinase activity blocks progranulin-induced phosphorylation. Western immunoblots of serum-starved T24 cells exposed to Ephrin-A1-Fc (2.1 nM) or progranulin (150 nM) for 15 min ±ALW-II-41–27 (1 μM), and probed with Phospho-EphA2 (Ser897) and EphA2 antibodies.

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer

    doi: 10.1016/j.matbio.2020.03.009

    Figure Lengend Snippet: Progranulin evokes EphA2 phosphorylation. Serum-starved T24 cells were exposed to progranulin (150 nM, 15 min) and immunoprecipitated with anti-EphA2 antibodies. Coomassie-stained bands of interest were trypsin-digested and analyzed by LC-MS/MS on a Q Exactive™ Plus mass spec. The mass spec data were probed against the UniProt human database for STY phosphorylation. False discovery rate for peptides/site identifications was set at 1%. (A) Modifications of various residues shown as the sum of MS peptides intensities. (B) EphA2 schematic showing the location of phosphorylated residues. (C-D) Western immunoblots of serum-starved T24 cells exposed to 150 nM progranulin using several Phospho-specific and total antibodies. (E) Western immunoblots of serum-starved 5637 cells after progranulin stimulation ±specific inhibitors for PI3K pathway (LY294002, 20 μM) or Erk1/2 (U0126, 10 μM). (F) Phospho-EphA2 (Ser897) assessed by immunoblot in UMUC-3/shScr (control) and UMUC-3/shPGRN cells. (G) Inhibition of EphA2 kinase activity blocks progranulin-induced phosphorylation. Western immunoblots of serum-starved T24 cells exposed to Ephrin-A1-Fc (2.1 nM) or progranulin (150 nM) for 15 min ±ALW-II-41–27 (1 μM), and probed with Phospho-EphA2 (Ser897) and EphA2 antibodies.

    Article Snippet: Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus).

    Techniques: Phospho-proteomics, Immunoprecipitation, Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Western Blot, Control, Inhibition, Activity Assay

    EphA2 is required for progranulin-evoked activity and cisplatin sensitivity. (A) EphA2 was depleted in UMUC-3 cells by siRNA approaches and EphA2 expression levels were assessed by immunoblot with anti-EphA2 polyclonal antibodies and normalized over β-actin content. Densitometric analysis was performed using ImageJ (National Institutes of Health) and expressed as arbitrary units. (B) Motility assays in Boyden chambers ±progranulin, ***p<0.001. (C) Anchorage-independent growth in soft-agar was performed as described in Materials and Methods ***p<0.001. (D) Cell survival as assessed by a Colorimetric Cell Cytotoxicity Assay Kit at various cisplatin concentrations. Mean ±SD; n = 3 biological replicates run in duplicates. **p<0.005; ***p<0.001.

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer

    doi: 10.1016/j.matbio.2020.03.009

    Figure Lengend Snippet: EphA2 is required for progranulin-evoked activity and cisplatin sensitivity. (A) EphA2 was depleted in UMUC-3 cells by siRNA approaches and EphA2 expression levels were assessed by immunoblot with anti-EphA2 polyclonal antibodies and normalized over β-actin content. Densitometric analysis was performed using ImageJ (National Institutes of Health) and expressed as arbitrary units. (B) Motility assays in Boyden chambers ±progranulin, ***p<0.001. (C) Anchorage-independent growth in soft-agar was performed as described in Materials and Methods ***p<0.001. (D) Cell survival as assessed by a Colorimetric Cell Cytotoxicity Assay Kit at various cisplatin concentrations. Mean ±SD; n = 3 biological replicates run in duplicates. **p<0.005; ***p<0.001.

    Article Snippet: Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus).

    Techniques: Activity Assay, Expressing, Western Blot, Cytotoxicity Assay

    EphA2 interacts with liprinα–1 and vinculin. (A) EphA2 interactome involved in cell motility as identified by proteomics. (B) Co-immunoprecipitation and western immunoblot of serum-starved T24 cells ±progranulin (150 nM) with the indicated antibodies. (C) Immunoblot of Liprinα–1 and vinculin in various urothelial carcinoma cells. (D) Co-localization of EphA2/liprinα–1 assessed by confocal microscopy. Insets = higher magnification of the relative areas within the white boxes. Bar = 10 μm. (E) Western immunoblot of liprinα–1- depleted T24 cells. (F) Quantification of T24 cell lateral motility determined by wound healing assays as previously described [18,19,26]. p = 0.000666.

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer

    doi: 10.1016/j.matbio.2020.03.009

    Figure Lengend Snippet: EphA2 interacts with liprinα–1 and vinculin. (A) EphA2 interactome involved in cell motility as identified by proteomics. (B) Co-immunoprecipitation and western immunoblot of serum-starved T24 cells ±progranulin (150 nM) with the indicated antibodies. (C) Immunoblot of Liprinα–1 and vinculin in various urothelial carcinoma cells. (D) Co-localization of EphA2/liprinα–1 assessed by confocal microscopy. Insets = higher magnification of the relative areas within the white boxes. Bar = 10 μm. (E) Western immunoblot of liprinα–1- depleted T24 cells. (F) Quantification of T24 cell lateral motility determined by wound healing assays as previously described [18,19,26]. p = 0.000666.

    Article Snippet: Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus).

    Techniques: Immunoprecipitation, Western Blot, Confocal Microscopy

    Mechanism of progranulin-dependent EphA2 activation. Scheme depicting progranulin-induced EphA2 activation at Tyr588 and resultant Akt/MAPK feedback loop to phosphorylate Ser897.

    Journal: Matrix biology : journal of the International Society for Matrix Biology

    Article Title: Progranulin/EphA2 axis: A novel oncogenic mechanism in bladder cancer

    doi: 10.1016/j.matbio.2020.03.009

    Figure Lengend Snippet: Mechanism of progranulin-dependent EphA2 activation. Scheme depicting progranulin-induced EphA2 activation at Tyr588 and resultant Akt/MAPK feedback loop to phosphorylate Ser897.

    Article Snippet: Generation of EphA2-depleted bladder cancer cells Cell lines (UMUC-3) stably depleted of endogenous EphA2 were generated by transfecting the pRS-shScr (scrambled shRNAs) and pRS/shEphA2 plasmids expressing shRNAs against human EphA2 (OriGene Technologies, Inc.) using the TransIT ® -Prostate Transfection Kit (Mirus).

    Techniques: Activation Assay