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antibodies against phospho-p42mapk (try 202 )/p44mapk (try 204 ; erk1/2  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc antibodies against phospho-p42mapk (try 202 )/p44mapk (try 204 ; erk1/2
Gβγ mediates ANG II-induced c-Src, ERK, and EGFR receptor (EGFR) activity. β-Adrenergic receptor kinase (βARK-ct) or empty vector (mock) plasmids were transfected into rabbit proximal tubule cells 24 h before assay. Proximal tubule cells were treated with 0.1% DMSO (vol/vol), arachidonic acid (AA; 15 μmol/l), eicosatetraenoic acid (ETYA; 15 μmol/l), or ANG II (1 μmol/l) for 5 min or with plasmids encoding β1 and γ2, (5 μg each) for 24 h. Extracts from cells were analyzed by Western blotting using anti-phospho-c-Src (Tyr416), <t>anti-phospho-p42MAPK</t> (Try202)/p44MAPK (Try204) (ERK1/2), p42MAPK (Try202)/p44MAPK (Try204), and anti-EGFR antibodies. Equal protein loading was confirmed by membrane reprobing with anti-c-Src, anti-ERK, and anti-EGFR antibodies. The corresponding bands were scanned, and intensities were normalized to anti-c-Src, anti-ERK, and anti-EGFR from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). B: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). C: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ns, Not significant compared with control. **P < 0.01 for comparison with control.
Antibodies Against Phospho P42mapk (Try 202 )/P44mapk (Try 204 ; Erk1/2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p42mapk+(try+202+)/anti+p38/pmc04121571-72-11-34
Average 90 stars, based on 1 article reviews
antibodies against phospho-p42mapk (try 202 )/p44mapk (try 204 ; erk1/2 - by Bioz Stars, 2026-09
90/100 stars
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p42mapk (try 202 )/p44mapk (try 204  (Cell Signaling Technology Inc)
90
Cell Signaling Technology Inc p42mapk (try 202 )/p44mapk (try 204
Gβγ mediates ANG II-induced c-Src, ERK, and EGFR receptor (EGFR) activity. β-Adrenergic receptor kinase (βARK-ct) or empty vector (mock) plasmids were transfected into rabbit proximal tubule cells 24 h before assay. Proximal tubule cells were treated with 0.1% DMSO (vol/vol), arachidonic acid (AA; 15 μmol/l), eicosatetraenoic acid (ETYA; 15 μmol/l), or ANG II (1 μmol/l) for 5 min or with plasmids encoding β1 and γ2, (5 μg each) for 24 h. Extracts from cells were analyzed by Western blotting using anti-phospho-c-Src (Tyr416), <t>anti-phospho-p42MAPK</t> (Try202)/p44MAPK (Try204) (ERK1/2), p42MAPK (Try202)/p44MAPK (Try204), and anti-EGFR antibodies. Equal protein loading was confirmed by membrane reprobing with anti-c-Src, anti-ERK, and anti-EGFR antibodies. The corresponding bands were scanned, and intensities were normalized to anti-c-Src, anti-ERK, and anti-EGFR from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). B: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). C: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ns, Not significant compared with control. **P < 0.01 for comparison with control.
P42mapk (Try 202 )/P44mapk (Try 204, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/p42mapk+(try+202+)/anti+p38/pmc04121571-72-19-34
Average 90 stars, based on 1 article reviews
p42mapk (try 202 )/p44mapk (try 204 - by Bioz Stars, 2026-09
90/100 stars
  Buy from Supplier

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Gβγ mediates ANG II-induced c-Src, ERK, and EGFR receptor (EGFR) activity. β-Adrenergic receptor kinase (βARK-ct) or empty vector (mock) plasmids were transfected into rabbit proximal tubule cells 24 h before assay. Proximal tubule cells were treated with 0.1% DMSO (vol/vol), arachidonic acid (AA; 15 μmol/l), eicosatetraenoic acid (ETYA; 15 μmol/l), or ANG II (1 μmol/l) for 5 min or with plasmids encoding β1 and γ2, (5 μg each) for 24 h. Extracts from cells were analyzed by Western blotting using anti-phospho-c-Src (Tyr416), anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), p42MAPK (Try202)/p44MAPK (Try204), and anti-EGFR antibodies. Equal protein loading was confirmed by membrane reprobing with anti-c-Src, anti-ERK, and anti-EGFR antibodies. The corresponding bands were scanned, and intensities were normalized to anti-c-Src, anti-ERK, and anti-EGFR from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). B: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). C: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ns, Not significant compared with control. **P < 0.01 for comparison with control.

Journal: American Journal of Physiology - Renal Physiology

Article Title: Angiotensin II stimulates fibronectin protein synthesis via a Gβγ/arachidonic acid-dependent pathway

doi: 10.1152/ajprenal.00094.2014

Figure Lengend Snippet: Gβγ mediates ANG II-induced c-Src, ERK, and EGFR receptor (EGFR) activity. β-Adrenergic receptor kinase (βARK-ct) or empty vector (mock) plasmids were transfected into rabbit proximal tubule cells 24 h before assay. Proximal tubule cells were treated with 0.1% DMSO (vol/vol), arachidonic acid (AA; 15 μmol/l), eicosatetraenoic acid (ETYA; 15 μmol/l), or ANG II (1 μmol/l) for 5 min or with plasmids encoding β1 and γ2, (5 μg each) for 24 h. Extracts from cells were analyzed by Western blotting using anti-phospho-c-Src (Tyr416), anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), p42MAPK (Try202)/p44MAPK (Try204), and anti-EGFR antibodies. Equal protein loading was confirmed by membrane reprobing with anti-c-Src, anti-ERK, and anti-EGFR antibodies. The corresponding bands were scanned, and intensities were normalized to anti-c-Src, anti-ERK, and anti-EGFR from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). B: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). C: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ns, Not significant compared with control. **P < 0.01 for comparison with control.

Article Snippet: Antibodies against phospho-c-Src (Tyr 416 ), phospho-cPLA 2 (Ser 505 ), phospho-p42MAPK (Try 202 )/p44MAPK (Try 204 ; ERK1/2), p42MAPK (Try 202 )/p44MAPK (Try 204 ), cPLA 2 , and c-Src were purchased from Cell Signaling Technology.

Techniques: Activity Assay, Plasmid Preparation, Transfection, Western Blot, Expressing

Effect of different Gβγ combinations on EGFR, c-Src, and ERK activity. Rabbit proximal tubule cells were transiently transfected without (mock) or with 10 μg of the expression plasmids for Gβ1, Gβ2, Gβ3, Gβ4, or Gγ2. Equal amounts of cell lysates (30 μg) were resolved by SDS-PAGE followed by Western blotting with anti-EGFR, anti-phospho-c-Src (Tyr416), and anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), and p42MAPK (Try202)/p44MAPK (Try204) antibodies. Equal protein loading was confirmed by membrane reprobing with anti-EGFR, anti-c-Src, or anti-ERK antibodies. The corresponding bands were scanned, and intensities were normalized to anti-EGFR, anti-c-Src, and anti-ERK from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). B: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). C: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ***P < 0.001, **P < 0.01 for comparison with control.

Journal: American Journal of Physiology - Renal Physiology

Article Title: Angiotensin II stimulates fibronectin protein synthesis via a Gβγ/arachidonic acid-dependent pathway

doi: 10.1152/ajprenal.00094.2014

Figure Lengend Snippet: Effect of different Gβγ combinations on EGFR, c-Src, and ERK activity. Rabbit proximal tubule cells were transiently transfected without (mock) or with 10 μg of the expression plasmids for Gβ1, Gβ2, Gβ3, Gβ4, or Gγ2. Equal amounts of cell lysates (30 μg) were resolved by SDS-PAGE followed by Western blotting with anti-EGFR, anti-phospho-c-Src (Tyr416), and anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), and p42MAPK (Try202)/p44MAPK (Try204) antibodies. Equal protein loading was confirmed by membrane reprobing with anti-EGFR, anti-c-Src, or anti-ERK antibodies. The corresponding bands were scanned, and intensities were normalized to anti-EGFR, anti-c-Src, and anti-ERK from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). B: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). C: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ***P < 0.001, **P < 0.01 for comparison with control.

Article Snippet: Antibodies against phospho-c-Src (Tyr 416 ), phospho-cPLA 2 (Ser 505 ), phospho-p42MAPK (Try 202 )/p44MAPK (Try 204 ; ERK1/2), p42MAPK (Try 202 )/p44MAPK (Try 204 ), cPLA 2 , and c-Src were purchased from Cell Signaling Technology.

Techniques: Activity Assay, Transfection, Expressing, SDS Page, Western Blot

Gβγ mediates ANG II-induced c-Src, ERK, and EGFR receptor (EGFR) activity. β-Adrenergic receptor kinase (βARK-ct) or empty vector (mock) plasmids were transfected into rabbit proximal tubule cells 24 h before assay. Proximal tubule cells were treated with 0.1% DMSO (vol/vol), arachidonic acid (AA; 15 μmol/l), eicosatetraenoic acid (ETYA; 15 μmol/l), or ANG II (1 μmol/l) for 5 min or with plasmids encoding β1 and γ2, (5 μg each) for 24 h. Extracts from cells were analyzed by Western blotting using anti-phospho-c-Src (Tyr416), anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), p42MAPK (Try202)/p44MAPK (Try204), and anti-EGFR antibodies. Equal protein loading was confirmed by membrane reprobing with anti-c-Src, anti-ERK, and anti-EGFR antibodies. The corresponding bands were scanned, and intensities were normalized to anti-c-Src, anti-ERK, and anti-EGFR from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). B: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). C: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ns, Not significant compared with control. **P < 0.01 for comparison with control.

Journal: American Journal of Physiology - Renal Physiology

Article Title: Angiotensin II stimulates fibronectin protein synthesis via a Gβγ/arachidonic acid-dependent pathway

doi: 10.1152/ajprenal.00094.2014

Figure Lengend Snippet: Gβγ mediates ANG II-induced c-Src, ERK, and EGFR receptor (EGFR) activity. β-Adrenergic receptor kinase (βARK-ct) or empty vector (mock) plasmids were transfected into rabbit proximal tubule cells 24 h before assay. Proximal tubule cells were treated with 0.1% DMSO (vol/vol), arachidonic acid (AA; 15 μmol/l), eicosatetraenoic acid (ETYA; 15 μmol/l), or ANG II (1 μmol/l) for 5 min or with plasmids encoding β1 and γ2, (5 μg each) for 24 h. Extracts from cells were analyzed by Western blotting using anti-phospho-c-Src (Tyr416), anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), p42MAPK (Try202)/p44MAPK (Try204), and anti-EGFR antibodies. Equal protein loading was confirmed by membrane reprobing with anti-c-Src, anti-ERK, and anti-EGFR antibodies. The corresponding bands were scanned, and intensities were normalized to anti-c-Src, anti-ERK, and anti-EGFR from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). B: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). C: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ns, Not significant compared with control. **P < 0.01 for comparison with control.

Article Snippet: Antibodies against phospho-c-Src (Tyr 416 ), phospho-cPLA 2 (Ser 505 ), phospho-p42MAPK (Try 202 )/p44MAPK (Try 204 ; ERK1/2), p42MAPK (Try 202 )/p44MAPK (Try 204 ), cPLA 2 , and c-Src were purchased from Cell Signaling Technology.

Techniques: Activity Assay, Plasmid Preparation, Transfection, Western Blot, Expressing

Effect of different Gβγ combinations on EGFR, c-Src, and ERK activity. Rabbit proximal tubule cells were transiently transfected without (mock) or with 10 μg of the expression plasmids for Gβ1, Gβ2, Gβ3, Gβ4, or Gγ2. Equal amounts of cell lysates (30 μg) were resolved by SDS-PAGE followed by Western blotting with anti-EGFR, anti-phospho-c-Src (Tyr416), and anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), and p42MAPK (Try202)/p44MAPK (Try204) antibodies. Equal protein loading was confirmed by membrane reprobing with anti-EGFR, anti-c-Src, or anti-ERK antibodies. The corresponding bands were scanned, and intensities were normalized to anti-EGFR, anti-c-Src, and anti-ERK from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). B: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). C: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ***P < 0.001, **P < 0.01 for comparison with control.

Journal: American Journal of Physiology - Renal Physiology

Article Title: Angiotensin II stimulates fibronectin protein synthesis via a Gβγ/arachidonic acid-dependent pathway

doi: 10.1152/ajprenal.00094.2014

Figure Lengend Snippet: Effect of different Gβγ combinations on EGFR, c-Src, and ERK activity. Rabbit proximal tubule cells were transiently transfected without (mock) or with 10 μg of the expression plasmids for Gβ1, Gβ2, Gβ3, Gβ4, or Gγ2. Equal amounts of cell lysates (30 μg) were resolved by SDS-PAGE followed by Western blotting with anti-EGFR, anti-phospho-c-Src (Tyr416), and anti-phospho-p42MAPK (Try202)/p44MAPK (Try204) (ERK1/2), and p42MAPK (Try202)/p44MAPK (Try204) antibodies. Equal protein loading was confirmed by membrane reprobing with anti-EGFR, anti-c-Src, or anti-ERK antibodies. The corresponding bands were scanned, and intensities were normalized to anti-EGFR, anti-c-Src, and anti-ERK from the same tubular cell protein extract. One representative Western blot is shown for every experiment. A: phosphorylation of EGFR (top) compared with total expression of EGFR (bottom). B: phosphorylation of c-Src (p-c-Src; top) compared with total expression of c-Src (bottom). C: phosphorylation of ERK (p-ERK; top) compared with total expression of ERK (bottom). Bar graphs depict the quantitative densitometry analysis for Western blot densitometry data. Values are means ± SE of 4 independent experiments. ***P < 0.001, **P < 0.01 for comparison with control.

Article Snippet: Antibodies against phospho-c-Src (Tyr 416 ), phospho-cPLA 2 (Ser 505 ), phospho-p42MAPK (Try 202 )/p44MAPK (Try 204 ; ERK1/2), p42MAPK (Try 202 )/p44MAPK (Try 204 ), cPLA 2 , and c-Src were purchased from Cell Signaling Technology.

Techniques: Activity Assay, Transfection, Expressing, SDS Page, Western Blot