upah gene Search Results


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  • 99
    Millipore upa
    Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by <t>uPA</t> (30 IU) was then determined by incubation with the <t>Spectrozyme-PL</t> plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P
    Upa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 194 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp plau hs00170182 m1
    Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by <t>uPA</t> (30 IU) was then determined by incubation with the <t>Spectrozyme-PL</t> plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P
    Gene Exp Plau Hs00170182 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 64 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher upar gene
    Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by <t>uPA</t> (30 IU) was then determined by incubation with the <t>Spectrozyme-PL</t> plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P
    Upar Gene, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene length upar gene
    Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by <t>uPA</t> (30 IU) was then determined by incubation with the <t>Spectrozyme-PL</t> plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P
    Length Upar Gene, supplied by OriGene, used in various techniques. Bioz Stars score: 86/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad gene pulser
    Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by <t>uPA</t> (30 IU) was then determined by incubation with the <t>Spectrozyme-PL</t> plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P
    Gene Pulser, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 368 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc upar
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Upar, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 93 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp plau hs01547051 g1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Plau Hs01547051 G1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp mmp7 hs01042796 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Mmp7 Hs01042796 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 52 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp rna45s5 hs03928985 g1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Rna45s5 Hs03928985 G1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 335 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Thermo Fisher gene exp plau hs01547054 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Plau Hs01547054 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp serpine1 hs00167155 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Serpine1 Hs00167155 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp pih1d1 hs00215579 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Pih1d1 Hs00215579 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp serpinf1 hs00171467 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Serpinf1 Hs00171467 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp plat hs00263492 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Plat Hs00263492 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 34 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp mmp14 hs00237119 m1
    <t>uPAR</t> overexpression is sufficient to induce <t>EMT</t> under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.
    Gene Exp Mmp14 Hs00237119 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 95 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp mmp2 hs01548724 m1
    Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of <t>MMP2</t> and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p
    Gene Exp Mmp2 Hs01548724 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp ifna21 hs00353738 s1
    Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of <t>MMP2</t> and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p
    Gene Exp Ifna21 Hs00353738 S1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp mapt hs00902193 m1
    Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of <t>MMP2</t> and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p
    Gene Exp Mapt Hs00902193 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp 18s hs99999901 s1
    Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of <t>MMP2</t> and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p
    Gene Exp 18s Hs99999901 S1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 4768 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp timp1 hs99999139 m1
    Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of <t>MMP2</t> and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p
    Gene Exp Timp1 Hs99999139 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp cav1 hs00971716 m1
    Expression of uPA and Caveolin-1 in endocrine-resistant versus sensitive cell lines. Assessment of mRNA relative expression of uPA and Caveolin-1 using qPCR in wt-MCF7, MCF7-LTED, 1%MCF7 and MCF7-TAMR cell lines. Bars represent ± SEM. *p
    Gene Exp Cav1 Hs00971716 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 131 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp vwf hs00169795 m1
    Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, <t>VWF,</t> vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and
    Gene Exp Vwf Hs00169795 M1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gene exp serpine1 hs01126606 m1
    Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, <t>VWF,</t> vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and
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    Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, <t>VWF,</t> vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and
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    Thermo Fisher gene exp fkbp15 hs00391480 m1
    Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, <t>VWF,</t> vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and
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    Thermo Fisher gene exp rpap3 hs00226298 m1
    Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, <t>VWF,</t> vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and
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    Thermo Fisher gene exp mmp2 hs00234422 m1
    MMP13 and PAI-1 mRNA was upregulated under overexpressing ING1b and 2. (A) Results of real-time RT-PCR analyses of mRNA levels of MMP13 and <t>MMP2</t> mRNA in ING1b, 2, 3, 4 or 5 overexpressed HEK293 cells. Each ING gene (pcDNA3.1 vector 8 µg) was transfected into HEK293 cells using the Lipofectamine ® 2000 following manufacturer's protocol. Empty vector (8 µg) was used for a control. Cells were harvested at 48 h post-transfection. GAPDH mRNA level was used as the internal control. Columns, average of three independent experiments; Bars, SD. (B) Real-time RT-PCR was performed for detecting PAI-1 and uPA mRNA transcripts using the same samples as above. PAI-1 and uPA mRNA levels were normalized by GAPHD mRNA transcripts. Columns, average of three independent experiments; Bars, SD. MMP, matrix metalloproteinase; PAI-1, plasminogen activator inhibitor-1; ING, inhibitor of growth.
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    Thermo Fisher gene exp igf1r hs00609566 m1
    Co-RNAi of uPAS components and of <t>IGF1R</t> significantly reduces malignancy of BT549 and MDA-MB-231 cells. a Representative immunoblottings of uPAR, uPA (supernatant), IGF1R, GAPDH, (phospho) c-Met, MMP2, (phospho) 44/42 MAPK and p27 Kip1 are shown. Tubulin was used as loading control. b WST-1 assay was conducted 48 h ( n = 5), c Scratch wound assays 24 h and 48 h ( n = 3), d Matrigel invasion assays were conducted 48 h after starting the experiment ( n = 3). The quantifications were determined relative to mock
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    Thermo Fisher gene exp serpine1 rn01481341 m1
    Co-RNAi of uPAS components and of <t>IGF1R</t> significantly reduces malignancy of BT549 and MDA-MB-231 cells. a Representative immunoblottings of uPAR, uPA (supernatant), IGF1R, GAPDH, (phospho) c-Met, MMP2, (phospho) 44/42 MAPK and p27 Kip1 are shown. Tubulin was used as loading control. b WST-1 assay was conducted 48 h ( n = 5), c Scratch wound assays 24 h and 48 h ( n = 3), d Matrigel invasion assays were conducted 48 h after starting the experiment ( n = 3). The quantifications were determined relative to mock
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    Thermo Fisher gene optimization algorithm
    Co-RNAi of uPAS components and of <t>IGF1R</t> significantly reduces malignancy of BT549 and MDA-MB-231 cells. a Representative immunoblottings of uPAR, uPA (supernatant), IGF1R, GAPDH, (phospho) c-Met, MMP2, (phospho) 44/42 MAPK and p27 Kip1 are shown. Tubulin was used as loading control. b WST-1 assay was conducted 48 h ( n = 5), c Scratch wound assays 24 h and 48 h ( n = 3), d Matrigel invasion assays were conducted 48 h after starting the experiment ( n = 3). The quantifications were determined relative to mock
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    Thermo Fisher gene exp jun hs00277190 s1
    Effects of GdA on <t>c-Jun</t> expression. A , real time qPCR analysis ( n = 5) of the mRNA expression level of ETS-1, p53, and c-Jun in TEV-1 cells ( left ) and JEG-3 cells ( right ) under GdA treatment. B , Western blot analysis of c-Jun protein expression after GdA treatment. The c-Jun protein bands were quantified by densitometry ( n = 3). All values are presented as the percentage of changes relative to the no treatment control. *, p
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    Image Search Results


    Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by uPA (30 IU) was then determined by incubation with the Spectrozyme-PL plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P

    Journal: Infection and Immunity

    Article Title: Cell Surface Antigens of Mycoplasma Species Bovine Group 7 Bind to and Activate Plasminogen.

    doi: 10.1128/IAI.71.8.4823-4827.2003

    Figure Lengend Snippet: Cell surface plasmin activity. Fixed mycoplasma strains PG50 and 4 were incubated with 100 μg of human glu-plasminogen per ml. Plasminogen activation by uPA (30 IU) was then determined by incubation with the Spectrozyme-PL plasmin substrate for 30 min. Bars indicate means ± standard errors of the means ( n = 3). *, statistically significant difference between strain PG50 and strain 4 ( P

    Article Snippet: The optimal concentration of uPA was determined by construction of a kinetic concentration curve of plasmin activity resulting from the incubation of various concentrations of human uPA (Calbiochem) with plasminogen (100 μg/ml) and Spectrozyme-PL (250 μmol/liter).

    Techniques: Activity Assay, Incubation, Activation Assay

    uPAR overexpression is sufficient to induce EMT under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: uPAR overexpression is sufficient to induce EMT under normoxia. (A) MDA-MB-468 cells were cotransfected to transiently express GFP and uPAR (uPAR) or empty vector (pcDNA). Cells were allowed to migrate in Transwell chambers (cell migration; n = 9) or invade Matrigel (cell invasion; n = 8) for 24 h. Results are expressed as a percentage of that observed with normoxic GFP-expressing control cells (mean ± SEM). (B) Extracts from cells transfected with empty vector, uPAR-overexpressing C14 cells, and uPAR-overexpressing C18 cells were subjected to immunoblot analysis to detect uPAR and total ERK/MAPK, as a loading control. Equivalent cell extracts were probed to detect E-cadherin, vimentin, and total ERK/MAPK. All lanes are from the same immunoblot (same exposure). (C) pcDNA, C14, and C18 cells were cultured in 21% O 2 . Representative images were captured by phase-contrast microscopy. (D) pcDNA, C14, and C18 cells were immunostained to detect E-cadherin (green channel). The same cells also were stained with phalloidin (red channel) and DAPI. Bars, 50 μm.

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Over Expression, Multiple Displacement Amplification, Plasmid Preparation, Migration, Expressing, Transfection, Cell Culture, Microscopy, Staining

    uPAR-dependent activation of the PI3K–Akt pathway is necessary to induce EMT in hypoxia. (A and B) MDA-MB-468 cells were cultured for 15 h in 21% O 2 (N) or 1.0% O 2 (H). (A) Cell extracts were subjected to immunoblot analysis to detect phosphorylated Akt (p-Akt), phosphorylated GSK-3β (p-GSK-3β), Snail, and tubulin. (B) Snail mRNA was determined by qPCR (mean ± SEM; n = 4). (C) MDA-MB-468 cells were treated with 50 μM synthetic peptide (α325) or 50 μM scrambled peptide (scα325) for 15 h in 21% O 2 (N) or 1.0% O 2 (H). Cell extracts were subjected to immunoblot analysis to detect phosphorylated Akt and tubulin. (D) MDA-MB-468 cells were treated with10 μM of the PI3K inhibitor LY294002 or with vehicle for 15 h in 21% O 2 (normoxia) or 1.0% O 2 (hypoxia). Cell extracts were subjected to immunoblot analysis to detect Snail and tubulin (representative of three studies). All lanes are from the same immunoblot (same exposure). (E–G) MDA-MB-468 cells were treated with 10 μM LY294002 or vehicle (control) and cultured for 50 h in 21% O 2 (normoxia; N) or 1.0% O 2 (hypoxia; H). (E) Cell images were captured using phase-contrast microscopy. (F) Cells were immunostained to detect E-cadherin (green). The same cells were stained with phalloidin (red) and DAPI. (G) Snail mRNA was determined by qPCR. Results are compared with the level observed in control cells in normoxia (mean ± SEM; n = 3). Bar, 50 μm.

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: uPAR-dependent activation of the PI3K–Akt pathway is necessary to induce EMT in hypoxia. (A and B) MDA-MB-468 cells were cultured for 15 h in 21% O 2 (N) or 1.0% O 2 (H). (A) Cell extracts were subjected to immunoblot analysis to detect phosphorylated Akt (p-Akt), phosphorylated GSK-3β (p-GSK-3β), Snail, and tubulin. (B) Snail mRNA was determined by qPCR (mean ± SEM; n = 4). (C) MDA-MB-468 cells were treated with 50 μM synthetic peptide (α325) or 50 μM scrambled peptide (scα325) for 15 h in 21% O 2 (N) or 1.0% O 2 (H). Cell extracts were subjected to immunoblot analysis to detect phosphorylated Akt and tubulin. (D) MDA-MB-468 cells were treated with10 μM of the PI3K inhibitor LY294002 or with vehicle for 15 h in 21% O 2 (normoxia) or 1.0% O 2 (hypoxia). Cell extracts were subjected to immunoblot analysis to detect Snail and tubulin (representative of three studies). All lanes are from the same immunoblot (same exposure). (E–G) MDA-MB-468 cells were treated with 10 μM LY294002 or vehicle (control) and cultured for 50 h in 21% O 2 (normoxia; N) or 1.0% O 2 (hypoxia; H). (E) Cell images were captured using phase-contrast microscopy. (F) Cells were immunostained to detect E-cadherin (green). The same cells were stained with phalloidin (red) and DAPI. (G) Snail mRNA was determined by qPCR. Results are compared with the level observed in control cells in normoxia (mean ± SEM; n = 3). Bar, 50 μm.

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Activation Assay, Multiple Displacement Amplification, Cell Culture, Real-time Polymerase Chain Reaction, Microscopy, Staining

    uPAR is necessary for hypoxia-induced EMT and collagen remodeling. (A) pSUPER, sh-uPAR6, and sh-uPAR12 cells were cultured for 50 h in 21% O 2 (N) or 1.0% O 2 (H). The preparations were immunostained for E-cadherin (green channel), phalloidin (red channel), and DAPI. (B) pSUPER, sh-uPAR6, and sh-uPAR12 cells were cultured for 18 h on coverslips precoated with fluorescein-labeled type I collagen in 21% O 2 (N) or 1.0% O 2 (H). Cell nuclei are stained with DAPI. Bars, 50 μm.

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: uPAR is necessary for hypoxia-induced EMT and collagen remodeling. (A) pSUPER, sh-uPAR6, and sh-uPAR12 cells were cultured for 50 h in 21% O 2 (N) or 1.0% O 2 (H). The preparations were immunostained for E-cadherin (green channel), phalloidin (red channel), and DAPI. (B) pSUPER, sh-uPAR6, and sh-uPAR12 cells were cultured for 18 h on coverslips precoated with fluorescein-labeled type I collagen in 21% O 2 (N) or 1.0% O 2 (H). Cell nuclei are stained with DAPI. Bars, 50 μm.

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Cell Culture, Labeling, Staining

    uPAR expression and EMT in hypoxic cancer cell lines. (A) MDA-MB-468 (468), MCF-7, MDA-MB-231 (231), MDA-MB-435 (435), SK-BR3, A431, ZR-75-1 (ZR75), and SCC15 (SCC) cells were cultured in 21% O 2 (gray bars) or 1.0% O 2 (black bars). uPAR mRNA was determined by qPCR and standardized against the level present in MDA-MB-468 cells under normoxia (mean ± SEM; n ≥ 3). *, P

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: uPAR expression and EMT in hypoxic cancer cell lines. (A) MDA-MB-468 (468), MCF-7, MDA-MB-231 (231), MDA-MB-435 (435), SK-BR3, A431, ZR-75-1 (ZR75), and SCC15 (SCC) cells were cultured in 21% O 2 (gray bars) or 1.0% O 2 (black bars). uPAR mRNA was determined by qPCR and standardized against the level present in MDA-MB-468 cells under normoxia (mean ± SEM; n ≥ 3). *, P

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Expressing, Multiple Displacement Amplification, Cell Culture, Real-time Polymerase Chain Reaction

    CoCl 2 treatment promotes MDA-MB-468 cancer cell dissemination from CAMs. GFP-expressing MDA-MB-468 cells were inoculated onto CAMs at 9 d. Tumors were allowed to develop for 11 d. The cells on the CAMs were treated daily with 25 μl of 100 μM CoCl 2 (black bars) or vehicle (gray bars). (A) Primary tumors were photographed on a stereomicroscope. (B) GFP-expressing cells were imaged by fluorescence microscopy. (C) Tumors from some eggs were harvested 4 d after inoculation. RNA was isolated and analyzed by qPCR to determine levels of VEGF and uPAR mRNA. mRNA levels were standardized against the levels present in vehicle-treated tumors (mean ± SEM; n = 3). (D) Chick embryos were harvested 11 d after inoculation of tumor cells on the CAMs. The number of GFP- expressing cells/cell clusters in the heart–lung block was determined by fluorescent microscopy (mean ± SEM; n = 9).

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: CoCl 2 treatment promotes MDA-MB-468 cancer cell dissemination from CAMs. GFP-expressing MDA-MB-468 cells were inoculated onto CAMs at 9 d. Tumors were allowed to develop for 11 d. The cells on the CAMs were treated daily with 25 μl of 100 μM CoCl 2 (black bars) or vehicle (gray bars). (A) Primary tumors were photographed on a stereomicroscope. (B) GFP-expressing cells were imaged by fluorescence microscopy. (C) Tumors from some eggs were harvested 4 d after inoculation. RNA was isolated and analyzed by qPCR to determine levels of VEGF and uPAR mRNA. mRNA levels were standardized against the levels present in vehicle-treated tumors (mean ± SEM; n = 3). (D) Chick embryos were harvested 11 d after inoculation of tumor cells on the CAMs. The number of GFP- expressing cells/cell clusters in the heart–lung block was determined by fluorescent microscopy (mean ± SEM; n = 9).

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Multiple Displacement Amplification, Expressing, Fluorescence, Microscopy, Isolation, Real-time Polymerase Chain Reaction, Blocking Assay

    Hypoxia increases uPAR levels and activates cell signaling factors known to be downstream of uPAR. (A) MDA-MB-468 cells were cultured for 24 h in 21% O 2 (N) or 1.0% O 2 (H). Cell extracts were subjected to SDS-PAGE and immunoblot analysis to detect human uPAR using antibody 3932 and tubulin. (B) MDA-MB-468 cells were cultured for 15 h in 21% O 2 (N) or 1.0% O 2 (H), treated with 100 μM CoCl 2 or with vehicle (control; C). Cell extracts were affinity precipitated with PAK-1 PBD and subjected to immunoblot analysis to detect GTP-bound Rac1. The original cell extracts were studied by immunoblot analysis to determine total Rac1. Cell extracts were also probed for phosphorylated ERK/MAPK and HIF-1α. (C) The results of three separate experiments were averaged to determine the percentage of increase in activated Rac1 in hypoxia (mean ± SEM; n = 3).

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: Hypoxia increases uPAR levels and activates cell signaling factors known to be downstream of uPAR. (A) MDA-MB-468 cells were cultured for 24 h in 21% O 2 (N) or 1.0% O 2 (H). Cell extracts were subjected to SDS-PAGE and immunoblot analysis to detect human uPAR using antibody 3932 and tubulin. (B) MDA-MB-468 cells were cultured for 15 h in 21% O 2 (N) or 1.0% O 2 (H), treated with 100 μM CoCl 2 or with vehicle (control; C). Cell extracts were affinity precipitated with PAK-1 PBD and subjected to immunoblot analysis to detect GTP-bound Rac1. The original cell extracts were studied by immunoblot analysis to determine total Rac1. Cell extracts were also probed for phosphorylated ERK/MAPK and HIF-1α. (C) The results of three separate experiments were averaged to determine the percentage of increase in activated Rac1 in hypoxia (mean ± SEM; n = 3).

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Multiple Displacement Amplification, Cell Culture, SDS Page

    uPAR is necessary for hypoxia-promoted cell migration, invasion, and Rac1 activation. (A) MDA-MB-468 cells were pretreated with 25 μg/ml uPA-specific antibody 3471 and 25 μg/ml uPAR-specific antibody 399R or with 50 μg/ml control IgG. Cells were allowed to migrate in Transwell chambers for 24 h in 21% O 2 (gray bars) or 1.0% O 2 (black bars). Cell migration is expressed as a percentage of that observed with control IgG in normoxia (mean ± SEM; n = 6). (B) MDA-MB-468 cells expressing empty vector (pSUPER), sh-uPAR6 cells, and sh-uPAR12 cells were cultured for 24 h in 21% O 2 (gray bars) or 1.0% O 2 (black bars). uPAR mRNA was determined by qPCR. Results are normalized against HPRT-1 and compared with the level observed in the pSUPER cells in normoxia (mean ± SEM; n = 3). (C) pSUPER, sh-uPAR6, and sh-uPAR12 cells were allowed to migrate in Transwell chamber (cell migration) or to invade Matrigel (cell invasion) for 24 h in 21% O 2 (gray bars) or 1.0% O 2 (black bars). Results are expressed as a percentage of that observed with pSUPER cells in normoxia (mean ± SEM; n = 7 and n = 6, respectively). (D) pSUPER, sh-uPAR6, and sh-uPAR12 cells were cultured for 15 h in 21% O 2 (N) or in 1.0% O 2 (H). Cell extracts were affinity precipitated with PAK-1 PBD and subjected to immunoblot analysis to determine GTP-bound Rac1. The original extracts were subjected to immunoblot analysis for tubulin, as a loading control.

    Journal: The Journal of Cell Biology

    Article Title: uPAR induces epithelial-mesenchymal transition in hypoxic breast cancer cells

    doi: 10.1083/jcb.200701092

    Figure Lengend Snippet: uPAR is necessary for hypoxia-promoted cell migration, invasion, and Rac1 activation. (A) MDA-MB-468 cells were pretreated with 25 μg/ml uPA-specific antibody 3471 and 25 μg/ml uPAR-specific antibody 399R or with 50 μg/ml control IgG. Cells were allowed to migrate in Transwell chambers for 24 h in 21% O 2 (gray bars) or 1.0% O 2 (black bars). Cell migration is expressed as a percentage of that observed with control IgG in normoxia (mean ± SEM; n = 6). (B) MDA-MB-468 cells expressing empty vector (pSUPER), sh-uPAR6 cells, and sh-uPAR12 cells were cultured for 24 h in 21% O 2 (gray bars) or 1.0% O 2 (black bars). uPAR mRNA was determined by qPCR. Results are normalized against HPRT-1 and compared with the level observed in the pSUPER cells in normoxia (mean ± SEM; n = 3). (C) pSUPER, sh-uPAR6, and sh-uPAR12 cells were allowed to migrate in Transwell chamber (cell migration) or to invade Matrigel (cell invasion) for 24 h in 21% O 2 (gray bars) or 1.0% O 2 (black bars). Results are expressed as a percentage of that observed with pSUPER cells in normoxia (mean ± SEM; n = 7 and n = 6, respectively). (D) pSUPER, sh-uPAR6, and sh-uPAR12 cells were cultured for 15 h in 21% O 2 (N) or in 1.0% O 2 (H). Cell extracts were affinity precipitated with PAK-1 PBD and subjected to immunoblot analysis to determine GTP-bound Rac1. The original extracts were subjected to immunoblot analysis for tubulin, as a loading control.

    Article Snippet: uPAR is required for hypoxia-induced EMT To test whether uPAR is responsible for the increase in cell migration observed in hypoxia, we treated MDA-MB-468 cells with antibodies that block uPA binding to uPAR and inhibit uPAR-initiated cell signaling ( ). shows that the antibodies inhibited the increase in cell migration observed in hypoxia by 90 ± 7% (P < 0.005; n = 6) without affecting cell migration in 21% O2 .

    Techniques: Migration, Activation Assay, Multiple Displacement Amplification, Expressing, Plasmid Preparation, Cell Culture, Real-time Polymerase Chain Reaction

    Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of MMP2 and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Glycodelin-A Protein Interacts with Siglec-6 Protein to Suppress Trophoblast Invasiveness by Down-regulating Extracellular Signal-regulated Kinase (ERK)/c-Jun Signaling Pathway *

    doi: 10.1074/jbc.M111.233841

    Figure Lengend Snippet: Effects of GdA on ERK and trophoblast invasiveness. A , effects of GdA treatment on activation of JNK and ERK in TEV-1 and JEG-3 cells. Left , representative Western blots for protein expression from five individual experiments. Right , the phosphorylated ERK ( pERK ) protein bands were quantified by densitometry ( n = 5). pJNK , phosphorylated JNK. B , quantitative determination of TEV-1 cell invasion under PD98059 or U0126 treatment ( n = 5). Representative photographs showing the invasion of TEV-1 cells after GdA treatment are shown. C , real time qPCR analysis of the mRNA expression of MMP2 and uPA after PD98059 ( upper ) or U0126 ( lower ) treatment in TEV-1 cells. All values are presented as the percentage of changes relative to the no treatment control ( A ) or DMSO control ( B and C ). *, p

    Article Snippet: The resulting cDNA was subjected to qPCR analysis (TaqMan gene expression assays; Applied Biosystems) of MMP2 (Hs01548724_m1), uPA (Hs00170182_m1), ETS-1 (Hs00901425_m1), c-Jun (Hs00277190_s1), and p53 (Hs99999147_m1) using an ABI 7500 sequence detector (Applied Biosystems) as described ( ).

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

    Expression of uPA and Caveolin-1 in endocrine-resistant versus sensitive cell lines. Assessment of mRNA relative expression of uPA and Caveolin-1 using qPCR in wt-MCF7, MCF7-LTED, 1%MCF7 and MCF7-TAMR cell lines. Bars represent ± SEM. *p

    Journal: PLoS ONE

    Article Title: Src Is a Potential Therapeutic Target in Endocrine-Resistant Breast Cancer Exhibiting Low Estrogen Receptor-Mediated Transactivation

    doi: 10.1371/journal.pone.0157397

    Figure Lengend Snippet: Expression of uPA and Caveolin-1 in endocrine-resistant versus sensitive cell lines. Assessment of mRNA relative expression of uPA and Caveolin-1 using qPCR in wt-MCF7, MCF7-LTED, 1%MCF7 and MCF7-TAMR cell lines. Bars represent ± SEM. *p

    Article Snippet: Taqman gene expression assays (Applied Biosystems) were used to detect expression of uPA (Hs01547051_m1) and Caveolin-1 (Hs00971716_m1), together with FKBP15 (Hs00391480_m1), as a housekeeping gene, to normalise the data.

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, VWF, vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and

    Journal: Blood

    Article Title: Increased expression of urokinase plasminogen activator in Quebec platelet disorder is linked to megakaryocyte differentiation

    doi: 10.1182/blood-2008-08-172338

    Figure Lengend Snippet: Expression of uPA, α-granule proteins, vinculin, and CAMK2G in QPD (Q) and control (C) CD34 + cells, cultured megakaryocytes, and platelets. (A) RT-qPCR analysis of uPA, VWF, vinculin, and CAMK2G mRNA levels in platelets and/or CD34 + cells, and

    Article Snippet: The gene-specific sets of oligonucleotide primers and fluorescent probes for qPCR (from predeveloped TaqMan Gene Expression Assays) were as follows: uPA: Hs00170182_m1; VWF: Hs00169795_m1; vinculin: Hs00243320_m1; CAMK2G: Hs00538454_m1; and GAPDH: 4333764T.

    Techniques: Expressing, Cell Culture, Quantitative RT-PCR

    MMP13 and PAI-1 mRNA was upregulated under overexpressing ING1b and 2. (A) Results of real-time RT-PCR analyses of mRNA levels of MMP13 and MMP2 mRNA in ING1b, 2, 3, 4 or 5 overexpressed HEK293 cells. Each ING gene (pcDNA3.1 vector 8 µg) was transfected into HEK293 cells using the Lipofectamine ® 2000 following manufacturer's protocol. Empty vector (8 µg) was used for a control. Cells were harvested at 48 h post-transfection. GAPDH mRNA level was used as the internal control. Columns, average of three independent experiments; Bars, SD. (B) Real-time RT-PCR was performed for detecting PAI-1 and uPA mRNA transcripts using the same samples as above. PAI-1 and uPA mRNA levels were normalized by GAPHD mRNA transcripts. Columns, average of three independent experiments; Bars, SD. MMP, matrix metalloproteinase; PAI-1, plasminogen activator inhibitor-1; ING, inhibitor of growth.

    Journal: Molecular Medicine Reports

    Article Title: ING2, a tumor associated gene, enhances PAI-1 and HSPA1A expression with HDAC1 and mSin3A through the PHD domain and C-terminal

    doi: 10.3892/mmr.2017.7553

    Figure Lengend Snippet: MMP13 and PAI-1 mRNA was upregulated under overexpressing ING1b and 2. (A) Results of real-time RT-PCR analyses of mRNA levels of MMP13 and MMP2 mRNA in ING1b, 2, 3, 4 or 5 overexpressed HEK293 cells. Each ING gene (pcDNA3.1 vector 8 µg) was transfected into HEK293 cells using the Lipofectamine ® 2000 following manufacturer's protocol. Empty vector (8 µg) was used for a control. Cells were harvested at 48 h post-transfection. GAPDH mRNA level was used as the internal control. Columns, average of three independent experiments; Bars, SD. (B) Real-time RT-PCR was performed for detecting PAI-1 and uPA mRNA transcripts using the same samples as above. PAI-1 and uPA mRNA levels were normalized by GAPHD mRNA transcripts. Columns, average of three independent experiments; Bars, SD. MMP, matrix metalloproteinase; PAI-1, plasminogen activator inhibitor-1; ING, inhibitor of growth.

    Article Snippet: Real-time RT-PCR analysis was performed using ABI prism 7500 (Applied Biosystems; Thermo Fisher Scientific, Inc.) with a TaqMan probe provided by the manufacturer as the following; MMP13 (Id Hs00233992_m1), MMP2 (Id Hs00234422_m1), PAI-1 (Id Hs00167155_m1), uPA (Id Hs00170182_m1), HSPA1A (Id Hs00234422_m1), GADD45B (Id Hs00234422_m1), LGALS1 (Id Hs00234422_m1), and GAPDH (Id Hs99999905_m1).

    Techniques: Quantitative RT-PCR, Plasmid Preparation, Transfection

    Co-RNAi of uPAS components and of IGF1R significantly reduces malignancy of BT549 and MDA-MB-231 cells. a Representative immunoblottings of uPAR, uPA (supernatant), IGF1R, GAPDH, (phospho) c-Met, MMP2, (phospho) 44/42 MAPK and p27 Kip1 are shown. Tubulin was used as loading control. b WST-1 assay was conducted 48 h ( n = 5), c Scratch wound assays 24 h and 48 h ( n = 3), d Matrigel invasion assays were conducted 48 h after starting the experiment ( n = 3). The quantifications were determined relative to mock

    Journal: BMC Cancer

    Article Title: uPAR enhances malignant potential of triple-negative breast cancer by directly interacting with uPA and IGF1R

    doi: 10.1186/s12885-016-2663-9

    Figure Lengend Snippet: Co-RNAi of uPAS components and of IGF1R significantly reduces malignancy of BT549 and MDA-MB-231 cells. a Representative immunoblottings of uPAR, uPA (supernatant), IGF1R, GAPDH, (phospho) c-Met, MMP2, (phospho) 44/42 MAPK and p27 Kip1 are shown. Tubulin was used as loading control. b WST-1 assay was conducted 48 h ( n = 5), c Scratch wound assays 24 h and 48 h ( n = 3), d Matrigel invasion assays were conducted 48 h after starting the experiment ( n = 3). The quantifications were determined relative to mock

    Article Snippet: Quantitative PCR was conducted in triplicates using TaqMan probes: uPAR (Hs00958880_m1), uPA (Hs01547054_m1) and IGF1R (Hs00609566_m1, Thermo Fisher, Waltham, Massachusetts, USA).

    Techniques: Multiple Displacement Amplification, WST-1 Assay

    The uPAR and IGF1R complexes correlate with their co-overexpression in TNBC samples. a Immunohistochemical analyses and visualisation of uPAR and IGF1R in the same tumour sample expressing the target proteins at a high (score 3+) or ( b ) at a low (score 1+) level, bar: 100 μm

    Journal: BMC Cancer

    Article Title: uPAR enhances malignant potential of triple-negative breast cancer by directly interacting with uPA and IGF1R

    doi: 10.1186/s12885-016-2663-9

    Figure Lengend Snippet: The uPAR and IGF1R complexes correlate with their co-overexpression in TNBC samples. a Immunohistochemical analyses and visualisation of uPAR and IGF1R in the same tumour sample expressing the target proteins at a high (score 3+) or ( b ) at a low (score 1+) level, bar: 100 μm

    Article Snippet: Quantitative PCR was conducted in triplicates using TaqMan probes: uPAR (Hs00958880_m1), uPA (Hs01547054_m1) and IGF1R (Hs00609566_m1, Thermo Fisher, Waltham, Massachusetts, USA).

    Techniques: Over Expression, Immunohistochemistry, Expressing

    uPAR directly interacts with uPA and IGF1R. a Western blot analyses of co-immunoprecipitation replicates (co-IP 1–3) of uPAR with uPA or with IGF1R ( c ), the lysate (L) of MDA-MB-231 cells was used as positive control and a non-targeting isotype antibody was used as negative control (NK) b PLA and quantification of protein-protein complexes of uPAR with uPA or with IGF1R ( d ) on cell block sections from mock and uPAR-depleted cells (uPAR-RNAi)

    Journal: BMC Cancer

    Article Title: uPAR enhances malignant potential of triple-negative breast cancer by directly interacting with uPA and IGF1R

    doi: 10.1186/s12885-016-2663-9

    Figure Lengend Snippet: uPAR directly interacts with uPA and IGF1R. a Western blot analyses of co-immunoprecipitation replicates (co-IP 1–3) of uPAR with uPA or with IGF1R ( c ), the lysate (L) of MDA-MB-231 cells was used as positive control and a non-targeting isotype antibody was used as negative control (NK) b PLA and quantification of protein-protein complexes of uPAR with uPA or with IGF1R ( d ) on cell block sections from mock and uPAR-depleted cells (uPAR-RNAi)

    Article Snippet: Quantitative PCR was conducted in triplicates using TaqMan probes: uPAR (Hs00958880_m1), uPA (Hs01547054_m1) and IGF1R (Hs00609566_m1, Thermo Fisher, Waltham, Massachusetts, USA).

    Techniques: Western Blot, Immunoprecipitation, Co-Immunoprecipitation Assay, Multiple Displacement Amplification, Positive Control, Negative Control, Proximity Ligation Assay, Blocking Assay

    Co-overexpression of uPAS components and tumour-promoting proteins in TNBC samples and cell lines. a Immunohistochemical analysis of tumour samples showing positive expression and localisation of the proteins of interest: uPAR, uPA, PAI-1, IGF1R, IR and c-Met, bar: 50 μm and b Protein expressions of uPAR, uPA, PAI-1, IGF1R, IR and c-Met in the TNBC cohort ( n = 174). c Immunoblottings of uPAR, uPA (supernatant), PAI-1, IGF1R, (phospho) c-Met, HER2, ER, PR in two TNBC cell lines: BT549 and MDA-MB-231 and in the breast cancer cell lines: BT474, MCF7, MDA-MB-361, SKBR3 and T47D. Tubulin was used as loading control

    Journal: BMC Cancer

    Article Title: uPAR enhances malignant potential of triple-negative breast cancer by directly interacting with uPA and IGF1R

    doi: 10.1186/s12885-016-2663-9

    Figure Lengend Snippet: Co-overexpression of uPAS components and tumour-promoting proteins in TNBC samples and cell lines. a Immunohistochemical analysis of tumour samples showing positive expression and localisation of the proteins of interest: uPAR, uPA, PAI-1, IGF1R, IR and c-Met, bar: 50 μm and b Protein expressions of uPAR, uPA, PAI-1, IGF1R, IR and c-Met in the TNBC cohort ( n = 174). c Immunoblottings of uPAR, uPA (supernatant), PAI-1, IGF1R, (phospho) c-Met, HER2, ER, PR in two TNBC cell lines: BT549 and MDA-MB-231 and in the breast cancer cell lines: BT474, MCF7, MDA-MB-361, SKBR3 and T47D. Tubulin was used as loading control

    Article Snippet: Quantitative PCR was conducted in triplicates using TaqMan probes: uPAR (Hs00958880_m1), uPA (Hs01547054_m1) and IGF1R (Hs00609566_m1, Thermo Fisher, Waltham, Massachusetts, USA).

    Techniques: Over Expression, Immunohistochemistry, Expressing, Multiple Displacement Amplification

    Effects of GdA on c-Jun expression. A , real time qPCR analysis ( n = 5) of the mRNA expression level of ETS-1, p53, and c-Jun in TEV-1 cells ( left ) and JEG-3 cells ( right ) under GdA treatment. B , Western blot analysis of c-Jun protein expression after GdA treatment. The c-Jun protein bands were quantified by densitometry ( n = 3). All values are presented as the percentage of changes relative to the no treatment control. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Glycodelin-A Protein Interacts with Siglec-6 Protein to Suppress Trophoblast Invasiveness by Down-regulating Extracellular Signal-regulated Kinase (ERK)/c-Jun Signaling Pathway *

    doi: 10.1074/jbc.M111.233841

    Figure Lengend Snippet: Effects of GdA on c-Jun expression. A , real time qPCR analysis ( n = 5) of the mRNA expression level of ETS-1, p53, and c-Jun in TEV-1 cells ( left ) and JEG-3 cells ( right ) under GdA treatment. B , Western blot analysis of c-Jun protein expression after GdA treatment. The c-Jun protein bands were quantified by densitometry ( n = 3). All values are presented as the percentage of changes relative to the no treatment control. *, p

    Article Snippet: The resulting cDNA was subjected to qPCR analysis (TaqMan gene expression assays; Applied Biosystems) of MMP2 (Hs01548724_m1), uPA (Hs00170182_m1), ETS-1 (Hs00901425_m1), c-Jun (Hs00277190_s1), and p53 (Hs99999147_m1) using an ABI 7500 sequence detector (Applied Biosystems) as described ( ).

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