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Anti phospho p44 p42 mapk thr202 tyr204

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Anti-phospho-p44/p42 MAPK-Thr202/Tyr204 is an antibody that detects the phosphorylation of p44/42 MAPK (Erk1/2) at Thr202 and Tyr204. This antibody is used to detect the activation of the MAPK/Erk signaling pathway.

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Lab products found in correlation

Anti p44 p42 mapk, by Cell Signaling Technology (3 mentions) Anti β actin, by Merck Group (2 mentions) Nupage gel, by Thermo Fisher Scientific (2 mentions) Rnaimax, by Thermo Fisher Scientific (2 mentions) Anti akt, by Cell Signaling Technology (2 mentions) Anti gsk3β, by Cell Signaling Technology (2 mentions) Targeting cortactin, by Qiagen (2 mentions) Anti epha2, by Abcam (2 mentions) Anti pakt ser473 thr308, by Cell Signaling Technology (2 mentions) Anti pacly ser544, by Cell Signaling Technology (2 mentions) Anti pepha2 ser897, by Cell Signaling Technology (2 mentions) Anti acly, by Cell Signaling Technology (2 mentions) Anti p gsk3β ser9, by Cell Signaling Technology (2 mentions) Anti gapdh, by Merck Group (1 mentions) Anti phospho akt ser473, by Cell Signaling Technology (1 mentions) Anti cyclin a, by Santa Cruz Biotechnology (1 mentions) Mouse monoclonal anti ha antibody 12ca5, by Roche (1 mentions) Anti his antibody, by Merck Group (1 mentions) Ecl system, by GE Healthcare (1 mentions) Anti g6pdh, by Merck Group (1 mentions)

Spelling variants of this product

P44/p42 MAPK (14 citations) Anti-phospho-p42/p44 MAPK (6 citations) Phospho p42/p44 MAPK (5 citations) Anti-p44/p42 MAPK (5 citations) Anti-MAPKs (4 citations) Anti–phospho-p44/p42 MAPK (Thr202/Tyr204) antibody (3 citations) Phospho-MAPKs (2 citations) Anti-phospho-p44/p42 MAPK (ERK1/2) (Thr202/Tyr204) (2 citations)

4 protocols using anti phospho p44 p42 mapk thr202 tyr204

1

Immunoblot Analysis of Signaling Pathways

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Immunoblot analysis was performed as described by our group4 (link) using the following antibodies: anti-p44/p42 MAPK, anti-phospho p44/p42 MAPK (Thr202/Tyr204), and anti-phospho Akt (Ser473) from Cell Signaling Technologies (Danvers, MA); anti-cyclin A (Santa Cruz Biotechnologies, Santa Cruz CA); and anti-GAPDH (Millipore, Billerica MA).
Zhong Y., El-Gamal D., Dubovsky J.A., Beckwith K.A., Harrington B.K., Williams K.E., Goettl V.M., Jha S., Mo X., Jones J.A., Flynn J.M., Maddocks K.J., Andritsos L.A., McCauley D., Shacham S., Kauffman M., Byrd J.C, & Lapalombella R. (2014). Selinexor suppresses Downstream Effectors of B-cell activation, proliferation and migration in chronic lymphocytic leukemia cells. Leukemia, 28(5), 1158-1163.
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2

Western Blotting of Signaling Proteins

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Cells were harvested and lysed in modified RIPA buffer (50 mM Tris-HCl, pH 7.4, 150 mM NaCl, 1 mm EDTA, 1% Nonidet P-40, 0.25% sodium deoxycholate, and 1 mM sodium orthovanadate in the presence of protease inhibitors). Whole cell protein extracts were denatured and separated in NuPAGE gels (Invitrogen), transferred to nitrocellulose membranes, and probed with primary and horseradish peroxidase-conjugated secondary antibodies. Anti-p44/p42 MAPK (9102: 1:1,000), anti-phospho-p44/p42 MAPK-Thr202/Tyr204 (9106: 1:1,000), anti-AKT (9272: 1:1,000), anti-pAKT-Ser473/Thr308 (9271, 2965: 1:1,000), anti-ACLY (4332: 1:1,000), anti-pACLY-Ser544 (4331: 1:1,000), anti-pGSK3β-Ser9 (5538: 1:1,000), anti-GSK3β(9832:1:1,000) and anti-pEPHA2-Ser897 (6347: 1:1,000) were purchased from Cell Signaling Technology. Other antibodies used are anti-EPHA2 (3625: 1:1,000) from Epitomics and anti-β−ACTIN (A5316:1:5,000) from Sigma. Full scans of western blots are provided in Supplementary Fig. 7. 50 nM siRNA (CACCAGGAGCAUAUCAACAUA) targeting cortactin (Qiagen) was used for transfections with RNAiMax (Invitrogene). Cells were harvested 48 hours post transfection for assessing knockdown efficiency or other follow-up experiments.
Wu X., Renuse S., Sahasrabuddhe N.A., Zahari M.S., Chaerkady R., Kim M.S., Nirujogi R.S., Mohseni M., Kumar P., Raju R., Zhong J., Yang J., Neiswinger J., Jeong J.S., Newman R., Powers M.A., Somani B.L., Gabrielson E., Sukumar S., Stearns V., Qian J., Zhu H., Vogelstein B., Park B.H, & Pandey A. (2014). Activation of diverse signaling pathways by oncogenic PIK3CA mutations. Nature communications, 5, 4961.
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3

Western Blotting of Signaling Proteins

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Cells were harvested and lysed in modified RIPA buffer (50 mM Tris-HCl, pH 7.4, 150 mM NaCl, 1 mm EDTA, 1% Nonidet P-40, 0.25% sodium deoxycholate, and 1 mM sodium orthovanadate in the presence of protease inhibitors). Whole cell protein extracts were denatured and separated in NuPAGE gels (Invitrogen), transferred to nitrocellulose membranes, and probed with primary and horseradish peroxidase-conjugated secondary antibodies. Anti-p44/p42 MAPK (9102: 1:1,000), anti-phospho-p44/p42 MAPK-Thr202/Tyr204 (9106: 1:1,000), anti-AKT (9272: 1:1,000), anti-pAKT-Ser473/Thr308 (9271, 2965: 1:1,000), anti-ACLY (4332: 1:1,000), anti-pACLY-Ser544 (4331: 1:1,000), anti-pGSK3β-Ser9 (5538: 1:1,000), anti-GSK3β(9832:1:1,000) and anti-pEPHA2-Ser897 (6347: 1:1,000) were purchased from Cell Signaling Technology. Other antibodies used are anti-EPHA2 (3625: 1:1,000) from Epitomics and anti-β−ACTIN (A5316:1:5,000) from Sigma. Full scans of western blots are provided in Supplementary Fig. 7. 50 nM siRNA (CACCAGGAGCAUAUCAACAUA) targeting cortactin (Qiagen) was used for transfections with RNAiMax (Invitrogene). Cells were harvested 48 hours post transfection for assessing knockdown efficiency or other follow-up experiments.
Wu X., Renuse S., Sahasrabuddhe N.A., Zahari M.S., Chaerkady R., Kim M.S., Nirujogi R.S., Mohseni M., Kumar P., Raju R., Zhong J., Yang J., Neiswinger J., Jeong J.S., Newman R., Powers M.A., Somani B.L., Gabrielson E., Sukumar S., Stearns V., Qian J., Zhu H., Vogelstein B., Park B.H, & Pandey A. (2014). Activation of diverse signaling pathways by oncogenic PIK3CA mutations. Nature communications, 5, 4961.
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4

Immunodetection of Yeast Proteins

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In experiments carried out with budding yeast, immunodetection of Glucose-6-phosphate dehydrogenase (G6PDH) and Myc-tagged proteins was carried out using polyclonal anti-G6PDH (Sigma) and monoclonal 4A6 (Millipore) or 9E10 (Santa Cruz Biotechnology) antibodies, respectively. Polyclonal anti-phospho-p44/p42 MAPK (Thr202/Tyr204) (Cell Signaling), anti-GST (Santa Cruz Biotechnology) and anti-His antibodies (Sigma) were also used as described previously [18] (link). The primary antibodies were detected using a fluorescently-conjugated secondary antibody with an Odyssey Infrared Imaging System (LI-COR Biosciences).
In experiments performed with fission yeast, dual phosphorylation in Pmk1 was detected with polyclonal anti-phospho-p42/p44 as above, whereas total Pmk1 was detected after incubation with mouse monoclonal anti-HA antibody (12CA5, Roche Molecular Biochemicals).The immunoreactive bands were revealed with an anti-mouse-HRP-conjugated secondary antibody (Sigma) and the ECL system (GE Healthcare). GST fusions were detected with a goat anti-GST-HRP conjugated polyclonal antibody (GE Healthcare).
Sacristán-Reviriego A., Madrid M., Cansado J., Martín H, & Molina M. (2014). A Conserved Non-Canonical Docking Mechanism Regulates the Binding of Dual Specificity Phosphatases to Cell Integrity Mitogen-Activated Protein Kinases (MAPKs) in Budding and Fission Yeasts. PLoS ONE, 9(1), e85390.
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