Mouse monoclonal primary
ERK2 Mouse Monoclonal Antibody [A10D2] (EM1901-54)
Recombinant protein within human erk2 aa 200-360.
Hela cell lysates, human thyroid tissue, human skin tissue, human breast carcinoma tissue, human pancreas tissue, mouse testis tissue, mouse colon tissue, mouse ovary tissue, K562.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein G affinity purified.
ERK 2 antibody; ERK-2 antibody; ERT1 antibody; Extracellular Signal Regulated Kinase 2 antibody; Extracellular signal-regulated kinase 2 antibody; MAP kinase 1 antibody; MAP kinase 2 antibody; MAP kinase isoform p42 antibody; MAPK 1 antibody; MAPK 2 antibody; Mapk1 antibody; MAPK2 antibody; Mitogen-activated protein kinase 1 antibody; Mitogen-activated protein kinase 2 antibody; MK01_HUMAN antibody; P38 antibody; P40 antibody; P41 antibody; p42-MAPK antibody; P42MAPK antibody; PRKM1 antibody; PRKM2 antibody; protein kinase, mitogen-activated, 1 antibody; protein kinase, mitogen-activated, 2 antibody; protein tyrosine kinase ERK2 antibody
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Phosphorylated upon KIT and FLT3 signaling (By similarity). Dually phosphorylated on Thr-185 and Tyr-187, which activates the enzyme. Undergoes regulatory phosphorylation on additional residues such as Ser-246 and Ser-248 in the kinase insert domain (KID) These phosphorylations, which are probably mediated by more than one kinase, are important for binding of MAPK1/ERK2 to importin-7 (IPO7) and its nuclear translocation. In addition, autophosphorylation of Thr-190 was shown to affect the subcellular localization of MAPK1/ERK2 as well. Ligand-activated ALK induces tyrosine phosphorylation. Dephosphorylated by PTPRJ at Tyr-187. Phosphorylation on Ser-29 by SGK1 results in its activation by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. DUSP3 and DUSP6 dephosphorylate specifically MAPK1/ERK2 and MAPK3/ERK1 whereas DUSP9 dephosphorylates a broader range of MAPKs. Dephosphorylated by DUSP1 at Thr-185 and Tyr-187.; ISGylated.
Nucleus, spindle, centrosome, cytoplasm, caveola.
Mitogen-activated protein kinase (MAPK) signaling pathways involve two closely related MAP kinases, known as extracellular-signal-related kinase 1 (ERK 1, p44) and 2 (ERK 2, p42). Growth factors, steroid hormones, G protein-coupled receptor ligands, and neurotransmitters can initiate MAPK signaling pathways. Activation of ERK1 and ERK2 requires phosphorylation by upstream kinases such as MAP kinase kinase (MEK), MEK kinase and Raf-1. ERK1 and ERK2 phosphorylation can occur at specific tyrosine and threonine sites mapping within consensus motifs that include the Threonine-Glutamate-Tyrosine motif. ERK activation leads to dimerization with other ERKs and subsequent localization to the nucleus. Active ERK dimers phosphorylate serine and threonine residues on nuclear proteins and influence a host of responses that include proliferation, differentiation, transcription regulation and development. The human ERK2 gene maps to chromosome 22q11.21 and encodes a 360-amino acid protein.