Erk1 2

Manufactured by Promega

ERK1/2 is a laboratory product that serves as a key component in the Mitogen-Activated Protein Kinase (MAPK) signaling pathway. It plays a central role in the regulation of cellular processes, including cell proliferation, differentiation, and survival.

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Lab products found in correlation

Close spelling variants of this product

Anti-Erk1/2 (4 citations) Total ERK1/2 (2 citations) P-Erk1/2 (2 citations) Anti- ERK1/2 antibody (2 citations)

3 protocols using erk1 2

Immunoblotting Analysis of Cellular Signaling Pathways

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Protein was extracted in a lysis buffer (1% NP40, 10 mM Tris pH7.6, 50 mM NaCl, 30 mM NaPPi, 50 mM NaF, 1% Triton, 0.5% deoxycholate and 0.1% sodium dodecyl sulfate) concentration determined by the BCA protein assay, and 20 μg of protein per sample was subjected to polyacrylamide gel electrophoresis and transfer to a nitrocellulose membrane. The antibodies used were: ERK1/2 (Promega, 1:10000), ERK5 (Millipore, 1:1000), phosphorylated-ERK1/2 (pERK1/2) and pERK5 (Cell Signaling Technology, 1:1000), cleaved caspase-8 (Cell Signaling Technology, 1:1000), VDAC (Abcam, 1:3200) and GAPDH (Advanced ImmunoChemical, 1:100000). Relative density of bands was quantified using Chemi Doc^™ XRS+ (Bio-Rad, Hercules, CA, USA).

Suzuki T, & Yang J. (2014). Hydrogen Peroxide Activation of ERK5 Confers Resistance to Jurkat Cells Against Apoptosis Induced by the Extrinsic Pathway. Biochemical and biophysical research communications, 444(2), 248-253.

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Quantitative Western Blot Analysis

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Cells were lysed using Mammalian Protein Extraction Reagent (M-PER) (Thermo Fisher Scientific) containing protease inhibitor cocktail (cOmplete tablet; Roche, Mannheim, Germany) and phosphatase inhibitor cocktail (PhosSTOP; Roche). Equal amounts of proteins from cell lysates were separated by SDS-PAGE and transferred to PVDF membranes. Membranes were blocked using 5% ECL blocking agent (GE Healthcare, Chicago, IL) in Tris-buffered saline containing 0.05% Triton X-100. Proteins of interest were detected using primary antibodies against phosphorylated forms of AKT (Ser473; Cell Signaling Technology, Danvers, MA) and ERK1/2 (PROMEGA, Madison, WI), and against IGFBP-3 (B-5; Santa Cruz Biotechnology, Dallas, TX), AKT (Cell Signaling) and β-actin (clone C4; Millipore, Billerica, MA). Following incubation with primary antibodies, membranes were incubated with horseradish peroxidase-conjugated secondary antibodies (Santa Cruz Biotechnology). Detected proteins were visualized with ECL Western Blotting Detection reagents (GE Healthcare). Protein expression levels were quantified using ImageJ^{56 (link)}. Active MAPK/ERK and p-AKT expression levels were normalized to β-actin and total AKT protein levels, respectively.

Ng E.F., Kaida A., Nojima H, & Miura M. (2022). Roles of IGFBP-3 in cell migration and growth in an endophytic tongue squamous cell carcinoma cell line. Scientific Reports, 12, 11503.

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Western Blot Antibody Library

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Antibodies for western blot detection included actin (I-19, Santa Cruz Biotechnology, cat. n. sc-1616, RRID: AB_630836), Akt (Cell Signaling Technology, cat. n. 9272, RRID: AB_329827), Akt pS473 (Cell Signaling Technology, cat. n. 9271, RRID: AB_329825), Cas (BD Transduction Laboratories, cat. n. 610271, RRID: AB_397666), Cas pY410 (Cell Signaling Technology, cat. n. 4011, RRID: AB_2274823), Erk1/2 (Promega), phospho-Erk1/2 (Promega, cat. n. V1141, RRID: AB_430839), FAK (C-20, Santa Cruz Biotechnology, cat. n. sc-558, RRID: AB_2300502), FAK pY397 (Invitrogen, cat. n. 44–624G, RRID: AB_2533701), FAK pY861 (Abgent, cat. n. AJ1285f, RRID: AB_10818227), paxillin (BD Transduction Laboratories, cat. n. 610052, RRID: AB_397464), paxillin pY118 (Cell Signaling Technology, cat. n. 2541, RRID: AB_2174466), Src (clone 184Q20, Invitrogen, cat. n. AHO1152, RRID: AB_2536324), Src pY418 (Cell Signaling Technology, cat. n. 2101, RRID: AB_331697), Stat3 (C-20, Santa Cruz Biotechnology, cat. n. sc-482, RRID: AB_632440), and Stat3 pY705 (Cell Signaling Technology, cat. n. 9131, RRID: AB_331568).

Koudelková L., Pelantová M., Brůhová Z., Sztacho M., Pavlík V., Pánek D., Gemperle J., Talacko P., Brábek J, & Rösel D. (2023). Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase. eLife, 12, e82428.

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