Mouse Monoclonal Antibody
Catalog No. M29-60CM
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ERK1 is a protein serine/threonine kinase that is a member of the extracellular signal-regulated kinases (ERKs) which are activated in response to numerous growth factors and cytokines (1). Activation of ERK1 requires both tyrosine and threonine phosphorylation that is mediated by MEK. ERK1 is ubiquitously distributed in tissues with the highest expression in heart, brain and spinal cord. Activated ERK1 translocates into the nucleus where it phosphorylates various transcription factors (e.g., Elk-1, c-Myc, c-Jun, c-Fos, and C/EBP beta).
1. Boulton, TG. et al: Purification and properties of extracellular signal-regulated kinase 1, an insulin-stimulated microtubule-associated protein 2 kinase. Biochemistry. 1991 Jan 8;30(1):278-86.
Recognizes only the ERK1 protein
Immunoprecipitate ERK1 from Human
ERK1 from other species may also be detectable.
Host / Isotype / Clone#:
Mouse, IgG2b, E40
Recombinant full length ERK1 protein
Affinity purified using Protein G
Store at 4°C (add 0.1% NaN3) for several months, and at -20°C for longer periods. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For optimal performance, avoid repeated handling and multiple freeze/thaw cycles.
Representative immunoprecipitation (0.1µg, 0.5µg, 1.0µg of Anti-ERK1) using 50µg of HEK-293 cell lysate.
Li Saiqun et al., RAS/ERK Signaling Controls Proneural Genetic Programs in Cortical Development and Gliomagenesis Journal of Neuroscience February 2014 10.1523/JNEUROSCI.4077-13.2014
Tonga Junfeng et al., Phosphorylation of Rac1 T108 by Extracellular Signal-Regulated Kinase in Response to Epidermal Growth Factor: a Novel Mechanism To Regulate Rac1 Function Molecular and Cellular Biology November 2013 10.1128/MCB.00822-13
E. Franklin Norah et al., Differential phosphorylation of the phosphoinositide 3-phosphatase MTMR2 regulates its association with early endosomal subtypes Journal of Cell Science February 2013 10.1242/jcs.113928
Tyler Moore et al., IRF3 and ERK MAP-kinases control nitric oxide production from macrophages in response to poly-I:C FEBS Letters September 2013 10.1016/j.febslet.2013.07.025
Yanga Shuping et al., Phosphorylation of KIBRA by the extracellular signal-regulated kinase (ERK)?ribosomal S6 kinase (RSK) cascade modulates cell proliferation and migration Cellular Signaling February 2014 10.1016/j.cellsig.2013.11.012
Neise Denise et al., Evidence for a differential modulation of p53-phosphorylating kinases by the cyclin-dependent kinase inhibitor p21WAFI/C1P1 Cell Cycle September 2010 10.4161/cc.9.17.12799
AL Lasek et al., The Functional Significance of Posttranslational Modifications on Polo-Like Kinase 1 Revealed by Chemical Genetic Complementation. PLoS One February 2016 10.1371/journal.pone.0150225
Tong Junfeng et al., Phosphorylation and Activation of RhoA by ERK in Response to Epidermal Growth Factor Stimulation PLoS One January 2016 10.1371/journal.pone.0147103
N Sato et al., MEK and PI3K catalytic activity as predictor of the response to molecularity targeted agents in triple-negative breast cancer Biochemical and Biophysical Research Communications August 2017
Bhandaria Deepali et al., Cyclin-dependent kinase 5 activates guanine nucleotide exchange factor GIV/Girdin to orchestrate migration?proliferation dichotomy PNAS July 2015 10.1073/pnas.1514157112
K Fujita et al., HMGB1, a pathogenic molecule that induces neurite degeneration via TLR4-MARCKS, is a potential therapeutic target for Alzheimer's disease. Science Reports August 2016 10.1038/srep31895
Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, Neurobiology