Our Anti-ERK/MAPK (Thr202/Tyr204) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat ERK/MAPK (Thr202/Tyr204) and is antigen affinity purified from pooled serum. It is great for use in WB, IHC, ICC.
Immunostaining of neurons in the frontal cortex of saline treated mouse brain identifying cytoplasmic and nuclear staining of ERK/MAPK when phosphorylated at Thr202/Tyr204 (cat. p160-2024, red, 1:500). The intense nuclear staining of a few neurons shows stimulation of the neuron resulting in translocation of the protein. The blue is staining nuclei with DAPI. Photo courtesy of Robert Wine.
Anti-ERK/MAPK (Thr202/Tyr204) Antibody
Extracellular-Signal Regulated Kinase/Mitogen-Activated Protein Kinase (ERK/MAPK) is an integral component of cellular signaling during mitogenesis and differentiation of mitotic cells and also is thought to play a key role in learning and memory (Adams and Sweatt, 2002; Ahn, 1993; Tanoue and Nishida, 2003; Johnson and Lapadat, 2002). The activity of this kinase is regulated by dual phosphorylation at Thr202 and Tyr204 (Ahn, 1993).
Antigen Affinity Purified from Pooled Serum
ICC, IHC, WB
Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr202/Tyr204 of rat ERK/MAPK conjugated to keyhole limpet hemocyanin (KLH).
Iwanga, R., et al. 2012. Expression of Six1 in luminal breast cancers predicts poor prognosis and promotes increases in tumor initiating cells by activation of extracellular signal-regulated kinase and transforming growth factor-beta signaling pathways. Breast Cancer Research, 14(4), p.R100.
Morgan, J.E., et al. 2015. The class II transactivator (CIITA) is regulated by post-translational modification cross-talk between ERK1/2 phosphorylation, mono-ubiquitination and Lys63 ubiquitination. Bioscience Reports, 35(4).