Phospho p44 42 mapk erk1 2 thr202 tyr204 d13.14.4e xp rabbit mab

Manufactured by Cell Signaling Technology

The Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP rabbit mAb is a primary antibody that detects endogenous levels of p44 and p42 MAPK (Erk1 and Erk2) proteins when phosphorylated at Thr202/Tyr204.

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Lab products found in correlation

P44 42 mapk erk1 2 137f5 rabbit mab, by Cell Signaling Technology (2 mentions) West save star, by AbFrontier (1 mentions) Luminescent image analyser las 300, by GE Healthcare (1 mentions) Ripa buffer, by Merck Group (1 mentions) Proteinase inhibitor cocktail, by Roche (1 mentions) Image gauge software, by Fujifilm (1 mentions) β actin, by Cell Signaling Technology (1 mentions)

Close spelling variants of this product

Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP® Rabbit mAb #4370 Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) rabbit mAb Phospho-ERK1/2 (Thr202/Tyr204) (D13.14.4E) Phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) Phospho-p44/42 MAPK (Thr202/Tyr204) P44/42 MAPK (ERK1/2) rabbit mAb Thr202/Tyr204; D13.14.4E Phospho-ERK1/2 (D13.14.4E), Phospho-p44/42 MAPK (Erk1/2)

2 protocols using phospho p44 42 mapk erk1 2 thr202 tyr204 d13.14.4e xp rabbit mab

Western Blot Analysis of MAPK Signaling

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SK-OV-3 cell lines were lysed in RIPA buffer (Sigma-Aldrich) containing proteinase inhibitor cocktail (Roche Applied Science, Mannheim, Germany). Proteins (20 μg) were resolved using denaturing 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to polyvinylidene fluoride membranes. Membranes were blocked in 5% skim milk in Tris-buffered saline with 0.1% Tween 20 (TBST) and subsequently incubated overnight at 4 °C with the following primary antibodies: p44/42 MAPK (Erk1/2) (137F5) rabbit mAb (1:2000, Cell Signaling Technology), phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (D13.14.4E) XP rabbit mAb (1:1000, Cell Signaling Technology), and an anti-β-actin antibody produced in rabbit (1:5000, Sigma-Aldrich). After washing, the membranes were incubated with secondary antibodies conjugated to horseradish peroxidase for 1 h at room temperature. Protein bands were detected via chemiluminescence using West Save Star (Ab Frontier, Seoul, Korea) according to the manufacturer's protocol. Bands were visualized using a Luminescent Image analyser LAS-300 (GE Healthcare) and quantified using Image Gauge software (Fuji Photo Film, Tokyo, Japan).

Sung H.Y., Yang S.D., Ju W, & Ahn J.H. (2017). Aberrant epigenetic regulation of GABRP associates with aggressive phenotype of ovarian cancer. Experimental & Molecular Medicine, 49(5), e335-.

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Immunoblot Analysis of FGFR1 and ERK1/2 Signaling

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Extracts were prepared as previously described (18 (link)) and SDS-PAGE was performed using 10% (ERK1/2) or 8% (FGFR1) polyacrylamide gels. Following electrophoretic transfer, the filters were blocked in Tris-buffered saline containing 0.1% Tween-20 and 3% bovine serum albumin and then incubated overnight in the same solution containing antibodies. Antibodies for analysis of downstream targets were purchased from Cell Signaling Technologies (Danvers, MA); phospho-p44/42 MAPK (ERK1/2) (Thr 202/Tyr 204) (D13.14.4E) XP® Rabbit mAb (#4370); p44/42 MAPK (ERK1/2) (137F5) Rabbit mAb (#4695). Antibodies used for immunoblot analysis of FGFR1 were a rabbit monoclonal antibody (D8E4, Cell Signaling Technologies) and mouse monoclonal antibody (M2F12, internal epitope from Santa Cruz Biotechnology, Santa Cruz, CA). Detection of the α-subunit of NaK-ATPase with a mouse monoclonal antibody (Santa Cruz Biotechnology) or β-actin (#4967, Cell Signaling Technology) was performed as a loading control. FGFR1 protein levels detected with the C-terminal antibody were assessed from densitometry of the immunoblot and normalized to the α-subunit of NaK-ATPase; the resulting value for 584-A2 cells was designated as 1.0.

Göke F., Franzen A., Hinz T.K., Marek L.A., Petros Y.o.o.n., Sharma R., Bode M., von Maessenhausen A., Lankat-Buttgereit B., Göke A., Golletz C., Kirsten R., Boehm D., Vogel W., Kleczko E.K., Eagles J.R., Hirsch F.R., Van Bremen T., Bootz F., Schroeck A., Kim J., Tan A.C., Jimeno A., Heasley L.E, & Perner S. (2015). FGFR1 expression levels predict BGJ398-sensitivity of FGFR1-dependent head and neck squamous cell cancers. Clinical cancer research : an official journal of the American Association for Cancer Research, 21(19), 4356-4364.

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