amino acid farnesylation signal Search Results


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  • 92
    Thermo Fisher human keratin 18
    Human Keratin 18, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore amlexanox
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    OriGene bamhi
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    Thermo Fisher ecori
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    nhei  (TaKaRa)
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    TaKaRa nhei
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    TaKaRa bglii
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
    Bglii, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 2051 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore signal peptide
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    OriGene bglii
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
    Bglii, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 124 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene bspei
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    GenScript competent e coli bl21
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
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    Millipore dna fragment
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
    Dna Fragment, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4583 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene human pyruvate dehydrogenase
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
    Human Pyruvate Dehydrogenase, supplied by OriGene, used in various techniques. Bioz Stars score: 85/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    OriGene human calnexin
    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of <t>Amlexanox.</t> (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P
    Human Calnexin, supplied by OriGene, used in various techniques. Bioz Stars score: 88/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher mkate2 f sequence
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    Mkate2 F Sequence, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore n ethyl n isopropyl amiloride eipa
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    N Ethyl N Isopropyl Amiloride Eipa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Schiff Nutrition International responsive copolymer
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    Responsive Copolymer, supplied by Schiff Nutrition International, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore 3 4 5 dimethylthiazol 2 yl 2 5 diphenyl tetrazolium bromide
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    3 4 5 Dimethylthiazol 2 Yl 2 5 Diphenyl Tetrazolium Bromide, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3473 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Arroyo BioSciences ab1 n 1 h 4 isopropyl 1 allyl 3 methylpyrazolo 3 4 b pyridine 6 yl amino n 2 6 dichloropyridine 4 yl urea
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    Ab1 N 1 H 4 Isopropyl 1 Allyl 3 Methylpyrazolo 3 4 B Pyridine 6 Yl Amino N 2 6 Dichloropyridine 4 Yl Urea, supplied by Arroyo BioSciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher alexa fluor 488
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    Alexa Fluor 488, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 71255 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore bsa
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
    Bsa, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 42788 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore methyl β cyclodextrin mβcd
    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with <t>mKate2-F,</t> which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.
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    Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2, anti-ERK1/2, <t>anti-p-c-Fos,</t> or <t>anti-c-Fos</t> antibody. The expression levels were represented relative to the values in veh. n = 4. ** p
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    Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2, anti-ERK1/2, <t>anti-p-c-Fos,</t> or <t>anti-c-Fos</t> antibody. The expression levels were represented relative to the values in veh. n = 4. ** p
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    Activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and epidermal growth factor receptor (EGFR) by SC. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM diphenyleneiodonium (DPI), or 10 μM 5-( N -ethyl- N -isopropyl) amiloride (EIPA) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. ( B ) Cells were incubated with vehicle (vih), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. ( C ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or pH 7.6 for 15 min. ROS production was assessed by 2′,7′-dichlorofluorescin diacetate (DCFDA) fluorescence measurement and represented as a percentage of vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC or pH 7.6 for 15 min. Cytoplasmic extracts were immunoprecipitated with anti-NADPH oxidase (NOX) 4 antibody. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the membrane was blotted with <t>anti-p22phox</t> or anti-NOX4 antibody. ( E , F ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, 10 μM EIPA, or 10 μM erlotinib (ERL) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-EGFR, anti-EGFR, anti-p-ERK1/2, or anti-ERK1/2 antibody. The expression levels were represented relative to the values in vehicle. n = 3–4. ** p
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    Santa Cruz Biotechnology anti phosphorylated erk1 2
    Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with <t>anti-p-ERK1/2,</t> anti-ERK1/2, anti-p-c-Fos, or anti-c-Fos antibody. The expression levels were represented relative to the values in veh. n = 4. ** p
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    Image Search Results


    Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of Amlexanox. (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P

    Journal: The Journal of Experimental Medicine

    Article Title: Targeting IRF3 as a YAP agonist therapy against gastric cancer

    doi: 10.1084/jem.20171116

    Figure Lengend Snippet: Pharmacological inhibition of IRF3 suppresses GC growth. (A) Chemical structures of Amlexanox. (B) Cell proliferation of HGC27, BGC-823, and MKN45 cells after treatment with different doses of Amlexanox. (C) Colony formation of Amlexanox-treated cells. (D) Cell proliferation of YAP(S127)-overexpressing cells after treatment with Amlexanox. (E) Colony formation of YAP(S127A)-overexpressing cells after treatment with Amlexanox. (F) Cell viability of various cancer cells after treatment with different doses of Amlexanox. (G) Xenograft tumor growth of GC cell lines after treatment with Amlexanox. (H) Tumor volumes for the mice from G. (I) mRNA levels of YAP target genes in samples from G. (J) Tumor numbers in MNNG/HP-induced GC model after treatment with different doses of Amlexanox. (K) Ki67 staining of adenomas from J. Bar, 50 µm. At least two independent experiments were performed for all data. For curve figures and bar figures, data are presented as means ± SD. Unpaired Student’s t tests were used for comparing two variables. One-way ANOVA was used for multiple variables comparison. *, P

    Article Snippet: Poly(I:C) (P1530), poly(dA:dT) (P0883), Amlexanox (SML0517), 5-FU (F6627), and antibodies specific for Flag (M3165), α-tubulin (T6199), and β-actin (A2228) were from Sigma-Aldrich.

    Techniques: Inhibition, Mouse Assay, Staining

    Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with mKate2-F, which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.

    Journal: PLoS ONE

    Article Title: Tyrosine 416 Is Phosphorylated in the Closed, Repressed Conformation of c-Src

    doi: 10.1371/journal.pone.0071035

    Figure Lengend Snippet: Phosphorylation of Y416 in the closed, repressed conformation is driven by core kinase domains. A. Confocal micrographs of c-Src expressed as fusions to Emerald in AD293 cells in either full length or truncated form lacking the first 63 residues (Δ1–63), which contains the unique domain and myristoylation sequences. Cells were co-transfected with mKate2-F, which is a fluorescent protein containing a farnesylation signal to localize it to membranes. Turquoise shows c-Src-Em, red shows mKate2-F. Scale bar, 10 µm. Images are representative of three independent experiments. B. Western Blots of AD293 cells transfected with the indicated constructs for 24 h with 10 µg total protein lysate. Phospho-Y416 was detected with two different antibodies: #1, cat. PK1109 from Calbiochem; #2, cat. 2101 from Cell Signaling. Key: Em, Emerald fluorescent protein; closed, Q528E, P529E, G530I mutant of c-Src; open, Y527F mutant of c-Src; β-gal, β -galactosidase in same vector as c-Src constructs. Experiments were performed at least twice, which showed consistent results.

    Article Snippet: The mKate2-F sequence was commercially synthesized (GeneArt) with human optimized codons and appended at the C-terminus with the sequence SGLRTKLNPPDESGPGCMSCKCVLS, which includes C-terminal 20 amino acid farnesylation signal sequence from the c-HA-Ras protein , .

    Techniques: Transfection, Western Blot, Construct, Mutagenesis, Plasmid Preparation

    Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2, anti-ERK1/2, anti-p-c-Fos, or anti-c-Fos antibody. The expression levels were represented relative to the values in veh. n = 4. ** p

    Journal: Nutrients

    Article Title: Sodium Citrate Increases Expression and Flux of Mg2+ Transport Carriers Mediated by Activation of MEK/ERK/c-Fos Pathway in Renal Tubular Epithelial Cells

    doi: 10.3390/nu10101345

    Figure Lengend Snippet: Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2, anti-ERK1/2, anti-p-c-Fos, or anti-c-Fos antibody. The expression levels were represented relative to the values in veh. n = 4. ** p

    Article Snippet: Anti-actin, anti-phosphorylated ERK1/2 (p-ERK1/2), anti-c-Fos, and anti-p22phox antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Inhibition, Expressing, Incubation, Real-time Polymerase Chain Reaction

    Association of c-Fos with AP-1 binding site in the TRPM6 promoter. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 24 h. Nuclear extracts were immunoblotted with anti-acetyl-histone H3 or anti-histone H3 antibody. ( B ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 2 h. Genomic DNA was immunoprecipitated with an anti-c-Fos antibody. After immunoprecipitation, the 5′-flanking region of TNRP6 was amplified by semi-quantitative (upper gel photos) and quantitative PCR (lower graphs) using primer pairs amplifying AP-1 binding site. Input was amplified by the primer without immunoprecipitation. ChIP data are represented as % of input. n = 3. ** p

    Journal: Nutrients

    Article Title: Sodium Citrate Increases Expression and Flux of Mg2+ Transport Carriers Mediated by Activation of MEK/ERK/c-Fos Pathway in Renal Tubular Epithelial Cells

    doi: 10.3390/nu10101345

    Figure Lengend Snippet: Association of c-Fos with AP-1 binding site in the TRPM6 promoter. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 24 h. Nuclear extracts were immunoblotted with anti-acetyl-histone H3 or anti-histone H3 antibody. ( B ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 2 h. Genomic DNA was immunoprecipitated with an anti-c-Fos antibody. After immunoprecipitation, the 5′-flanking region of TNRP6 was amplified by semi-quantitative (upper gel photos) and quantitative PCR (lower graphs) using primer pairs amplifying AP-1 binding site. Input was amplified by the primer without immunoprecipitation. ChIP data are represented as % of input. n = 3. ** p

    Article Snippet: Anti-actin, anti-phosphorylated ERK1/2 (p-ERK1/2), anti-c-Fos, and anti-p22phox antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Binding Assay, Incubation, Immunoprecipitation, Amplification, Real-time Polymerase Chain Reaction, Chromatin Immunoprecipitation

    Activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and epidermal growth factor receptor (EGFR) by SC. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM diphenyleneiodonium (DPI), or 10 μM 5-( N -ethyl- N -isopropyl) amiloride (EIPA) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. ( B ) Cells were incubated with vehicle (vih), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. ( C ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or pH 7.6 for 15 min. ROS production was assessed by 2′,7′-dichlorofluorescin diacetate (DCFDA) fluorescence measurement and represented as a percentage of vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC or pH 7.6 for 15 min. Cytoplasmic extracts were immunoprecipitated with anti-NADPH oxidase (NOX) 4 antibody. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the membrane was blotted with anti-p22phox or anti-NOX4 antibody. ( E , F ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, 10 μM EIPA, or 10 μM erlotinib (ERL) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-EGFR, anti-EGFR, anti-p-ERK1/2, or anti-ERK1/2 antibody. The expression levels were represented relative to the values in vehicle. n = 3–4. ** p

    Journal: Nutrients

    Article Title: Sodium Citrate Increases Expression and Flux of Mg2+ Transport Carriers Mediated by Activation of MEK/ERK/c-Fos Pathway in Renal Tubular Epithelial Cells

    doi: 10.3390/nu10101345

    Figure Lengend Snippet: Activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and epidermal growth factor receptor (EGFR) by SC. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM diphenyleneiodonium (DPI), or 10 μM 5-( N -ethyl- N -isopropyl) amiloride (EIPA) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. ( B ) Cells were incubated with vehicle (vih), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. ( C ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or pH 7.6 for 15 min. ROS production was assessed by 2′,7′-dichlorofluorescin diacetate (DCFDA) fluorescence measurement and represented as a percentage of vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC or pH 7.6 for 15 min. Cytoplasmic extracts were immunoprecipitated with anti-NADPH oxidase (NOX) 4 antibody. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the membrane was blotted with anti-p22phox or anti-NOX4 antibody. ( E , F ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, 10 μM EIPA, or 10 μM erlotinib (ERL) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-EGFR, anti-EGFR, anti-p-ERK1/2, or anti-ERK1/2 antibody. The expression levels were represented relative to the values in vehicle. n = 3–4. ** p

    Article Snippet: Anti-actin, anti-phosphorylated ERK1/2 (p-ERK1/2), anti-c-Fos, and anti-p22phox antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Activation Assay, Incubation, Real-time Polymerase Chain Reaction, Fluorescence, Immunoprecipitation, Polyacrylamide Gel Electrophoresis, SDS Page, Expressing

    Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2, anti-ERK1/2, anti-p-c-Fos, or anti-c-Fos antibody. The expression levels were represented relative to the values in veh. n = 4. ** p

    Journal: Nutrients

    Article Title: Sodium Citrate Increases Expression and Flux of Mg2+ Transport Carriers Mediated by Activation of MEK/ERK/c-Fos Pathway in Renal Tubular Epithelial Cells

    doi: 10.3390/nu10101345

    Figure Lengend Snippet: Inhibition of SC-induced TRPM6 expression by U0126. ( A – C ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6, CNNM2, TRPM7, and β-actin. The contents of TRPM6, CNNM2, and TRPM7 mRNAs were represented as fold-increase over vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 24 h. Cytoplasmic extracts were immunoblotted with anti-TRPM6, anti-CNNM2, anti-TRPM7, or anti-β-actin antibody. The expression levels were represented relative to the values in vehicle. ( E ) Cells were incubated with vehicle (veh), 10 μM SC, or 10 μM U0126 (U) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2, anti-ERK1/2, anti-p-c-Fos, or anti-c-Fos antibody. The expression levels were represented relative to the values in veh. n = 4. ** p

    Article Snippet: Anti-actin, anti-phosphorylated ERK1/2 (p-ERK1/2), anti-c-Fos, and anti-p22phox antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Inhibition, Expressing, Incubation, Real-time Polymerase Chain Reaction

    Activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and epidermal growth factor receptor (EGFR) by SC. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM diphenyleneiodonium (DPI), or 10 μM 5-( N -ethyl- N -isopropyl) amiloride (EIPA) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. ( B ) Cells were incubated with vehicle (vih), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. ( C ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or pH 7.6 for 15 min. ROS production was assessed by 2′,7′-dichlorofluorescin diacetate (DCFDA) fluorescence measurement and represented as a percentage of vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC or pH 7.6 for 15 min. Cytoplasmic extracts were immunoprecipitated with anti-NADPH oxidase (NOX) 4 antibody. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the membrane was blotted with anti-p22phox or anti-NOX4 antibody. ( E , F ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, 10 μM EIPA, or 10 μM erlotinib (ERL) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-EGFR, anti-EGFR, anti-p-ERK1/2, or anti-ERK1/2 antibody. The expression levels were represented relative to the values in vehicle. n = 3–4. ** p

    Journal: Nutrients

    Article Title: Sodium Citrate Increases Expression and Flux of Mg2+ Transport Carriers Mediated by Activation of MEK/ERK/c-Fos Pathway in Renal Tubular Epithelial Cells

    doi: 10.3390/nu10101345

    Figure Lengend Snippet: Activation of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and epidermal growth factor receptor (EGFR) by SC. ( A ) NRK-52E cells were incubated with vehicle (veh), 10 μM SC, 10 μM diphenyleneiodonium (DPI), or 10 μM 5-( N -ethyl- N -isopropyl) amiloride (EIPA) for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. ( B ) Cells were incubated with vehicle (vih), 10 μM SC, 10 μM DPI, or 10 μM EIPA for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. ( C ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, or pH 7.6 for 15 min. ROS production was assessed by 2′,7′-dichlorofluorescin diacetate (DCFDA) fluorescence measurement and represented as a percentage of vehicle. ( D ) Cells were incubated with vehicle (veh), 10 μM SC or pH 7.6 for 15 min. Cytoplasmic extracts were immunoprecipitated with anti-NADPH oxidase (NOX) 4 antibody. After sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the membrane was blotted with anti-p22phox or anti-NOX4 antibody. ( E , F ) Cells were incubated with vehicle (veh), 10 μM SC, 10 μM DPI, 10 μM EIPA, or 10 μM erlotinib (ERL) for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-EGFR, anti-EGFR, anti-p-ERK1/2, or anti-ERK1/2 antibody. The expression levels were represented relative to the values in vehicle. n = 3–4. ** p

    Article Snippet: Anti-actin, anti-phosphorylated ERK1/2 (p-ERK1/2), anti-c-Fos, and anti-p22phox antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Activation Assay, Incubation, Real-time Polymerase Chain Reaction, Fluorescence, Immunoprecipitation, Polyacrylamide Gel Electrophoresis, SDS Page, Expressing

    Increase in TRPM6 and p-ERK1/2 expression by SC. ( A ) The pH of culture medium was measured using a pH meter. ( B ) NRK-52E cells were incubated in the medium of indicated pH for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. The expression levels were represented relative to the values at pH 7.4. ( C ) Cells were incubated in the medium of indicated pH for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. The contents of TRPM6 mRNA were represented as fold-increase over vehicle. ( D ) Cells were incubated in the medium of indicated pH for 15 min in the absence (veh) or presence of 10 μM U0126 (U). Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. The expression levels were represented relative to the values at pH 7.4. n = 4. ** p

    Journal: Nutrients

    Article Title: Sodium Citrate Increases Expression and Flux of Mg2+ Transport Carriers Mediated by Activation of MEK/ERK/c-Fos Pathway in Renal Tubular Epithelial Cells

    doi: 10.3390/nu10101345

    Figure Lengend Snippet: Increase in TRPM6 and p-ERK1/2 expression by SC. ( A ) The pH of culture medium was measured using a pH meter. ( B ) NRK-52E cells were incubated in the medium of indicated pH for 15 min. Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. The expression levels were represented relative to the values at pH 7.4. ( C ) Cells were incubated in the medium of indicated pH for 24 h. Quantitative real-time PCR was performed using primer pairs of TRPM6 and β-actin. The contents of TRPM6 mRNA were represented as fold-increase over vehicle. ( D ) Cells were incubated in the medium of indicated pH for 15 min in the absence (veh) or presence of 10 μM U0126 (U). Cytoplasmic extracts were immunoblotted with anti-p-ERK1/2 or anti-ERK1/2 antibody. The expression levels were represented relative to the values at pH 7.4. n = 4. ** p

    Article Snippet: Anti-actin, anti-phosphorylated ERK1/2 (p-ERK1/2), anti-c-Fos, and anti-p22phox antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Expressing, Incubation, Real-time Polymerase Chain Reaction