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Antiphospho thr202 tyr204 p44 42 mapk erk1 2

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Antiphospho-Thr202/Tyr204-p44/42 MAPK (Erk1/2) is a laboratory reagent that specifically detects the phosphorylation of threonine 202 and tyrosine 204 residues on the p44/42 mitogen-activated protein kinase (MAPK) proteins, also known as extracellular signal-regulated kinases 1 and 2 (Erk1/2). This reagent can be used to monitor the activation and regulation of the MAPK/Erk signaling pathway in various experimental systems.

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Lab products found in correlation

Anti phospho akt ser473, by Cell Signaling Technology (2 mentions) Cleaved caspase 3, by Cell Signaling Technology (1 mentions) Total akt, by Cell Signaling Technology (1 mentions) Anti phospho mtor ser2448, by Cell Signaling Technology (1 mentions) Anti phospho gsk3β ser9, by Cell Signaling Technology (1 mentions) Anti phospho akt thr308, by Cell Signaling Technology (1 mentions) Anti beta actin antibody sc 1615, by Santa Cruz Biotechnology (1 mentions) Total p44 42 mapk erk1 2, by Cell Signaling Technology (1 mentions) Anti p44 42 mapk erk1 2, by Cell Signaling Technology (1 mentions) Image lab 3, by Bio-Rad (1 mentions) Anti akt, by Cell Signaling Technology (1 mentions) Bovine serum albumin (bsa), by Euromedex (1 mentions) Anti α tubulin, by Merck Group (1 mentions) Immuno detection kit ecl luminata classico, by Merck Group (1 mentions) Molecular image chemidoc xrs, by Bio-Rad (1 mentions)

Spelling variants of this product

ERK1/2 (1487 citations) P44/42 MAPK (Erk1/2) (135 citations) P44/42 MAPK (90 citations) ERK1/2 MAPK (3 citations) (Thr202/Tyr204) ERK1/2 (2 citations) ERK1/2 p44/42 (2 citations) Antiphospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) rabbit mAb (2 citations)

2 protocols using antiphospho thr202 tyr204 p44 42 mapk erk1 2

1

AKT Signaling Pathway Antibody Panel

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Antiphospho-Ser473-AKT (#4060), antiphospho-Thr308-AKT (#2965), total AKT (#4691), AKT1 (#2938), AKT2 (#2964), AKT3 (#8018), antiphospho-Ser136-BAD (#4366), antiphospho-Ser9-GSK3β (#5558), antiphospho-Thr24-FoxO1/-Thr32-FoxO3 (#9464), antiphospho-Ser2448-mTOR (#5536), antiphospho-Ser2481-mTOR (#2974), antiphospho-Thr202/Tyr204-p44/42 MAPK (Erk1/2) (#9101; #4370), total p44/42 MAPK (Erk1/2) (#9102) and cleaved caspase-3 (#9664) antibodies were purchased from Cell Signaling Technology (Danvers, MA); Anti-Beta Actin antibody (sc-1615) was purchased from Santa Cruz Biotechnology (Dallas, TX). Peroxidase-labeled affinity purified anti-rabbit IgG (074–1506), anti-mouse IgG (074–1806), anti-mouse IgM (074–1803) and anti-goat IgG (14-13-06) antibodies were purchased from KPL (Gaithersburg, MD).
Thompson S.M., Callstrom M.R., Jondal D.E., Butters K.A., Knudsen B.E., Anderson J.L., Lien K.R., Sutor S.L., Lee J.S., Thorgeirsson S.S., Grande J.P., Roberts L.R, & Woodrum D.A. (2016). Heat Stress-Induced PI3K/mTORC2-Dependent AKT Signaling Is a Central Mediator of Hepatocellular Carcinoma Survival to Thermal Ablation Induced Heat Stress. PLoS ONE, 11(9), e0162634.
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2

Immunoblotting Analysis of Signaling Proteins

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Proteins were extracted and immunoblotted as previously described (Dessalle et al. 2012). All membranes were blocked with 4% BSA (Bovine Serum Albumin, Euromedex, Souffelweyersheim, France) and probed with anti‐N‐RAS (sc‐31, Santa Cruz Biotechnology, Palo Alto, CA), anti‐ROCK1 (sc‐5560, Santa Cruz), anti‐α‐Tubulin (T5168, Sigma, Lyon, France), anti‐phospho‐Ser473 Akt (#4060, Cell Signaling Technology, Leiden, the Netherlands), anti‐Akt (#4691, Cell Signaling), anti‐phospho‐Thr202/Tyr204 p44/42 MAPK (Erk1/2) (Cell Signaling), and anti‐p44/42 MAPK (Erk1/2) (Cell Signaling). The membranes were incubated with secondary corresponding antimouse (172‐1011, Bio‐Rad, Marnes‐la‐Coquette, France) or antirabbit (172‐1019, Bio‐Rad) HRP conjugated antibody. Signals were revealed with Immunodetection kit ECL Luminata Classico (Millipore) and the imager Molecular Image® ChemiDoc™XRS+ (Bio‐Rad). Proteins quantification was achieved using ImageLab 3.0 (Bio‐Rad).
Gastebois C., Chanon S., Rome S., Durand C., Pelascini E., Jalabert A., Euthine V., Pialoux V., Blanc S., Simon C, & Lefai E. (2016). Transition from physical activity to inactivity increases skeletal muscle miR‐148b content and triggers insulin resistance. Physiological Reports, 4(17), e12902.
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