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Erk1 (pT202/pY204)+Erk2 (pT185/pY187) Recombinant Rabbit monoclonal Antibody IgG

SKU: BA111613-100µl
$279.00Price

Fig1: Western blot analysis of Erk1(pT202/pY204)+Erk2(pT185/pY187) on A431 lysates using anti-Erk1(pT202/pY204)+Erk2(pT185/pY187) antibody at 1/1,000 dilution.

 

 

Bon Opus Cat. #BA111613
Size
  • Host Species; Species Reactivity

    Rabbit; Human, Mouse, Rat
  • Immunogen

    Synthetic phospho-Peptide corresponding to residues surrounding Thr 202 and Tyr204 of human Erk1 + Thr 185 and Tyr187 of human Erk2.
  • Application Summary

    WB, IP
  • Purification; Formulation

    ProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
  • ALTnames

    Mitogen-activated protein kinase 1, ERT1, Extracellular signal-regulated kinase 2, MAP kinase isoform p42, Mitogen-activated protein kinase 2, Mitogen-activated protein kinase 3, ERT2, Extracellular signal-regulated kinase 1, Insulin-stimulated MAP2 kinase, MAP kinase isoform p44, Microtubule-associated protein 2 kinase, p44-ERK1
  • Background

    The activation of signal transduction pathways by growth factors, hormones and neurotransmitters is mediated through two closely related MAP kinases, p44 and p42, designated extracellular-signal related kinase 1 (ERK 1) and ERK 2, respectively. ERK proteins are regulated by dual phosphorylation at Tyrosine 204 and 187 and Threonine 177 and 160 residues mapping within a characteristic Thr-Glu-Tyr motif. Phosphorylation at both the Threonine 202 and Tyrosine 204 residues of ERK1 and Threonine 185 and Tyrosine 187 residues of ERK2 is required for full enzymatic activation. The structural consequences of dual-phosphorylation in the ERK2 include active site closure, alignment of key catalytic residues that interact with ATP, and remodeling of the activation loop. In response to activation, MAP kinases phosphorylate downstream components on serine and threonine. Upstream MAP kinase regulators include MAP kinase kinase (MEK), MEK kinase and Raf-1. The ERK family has three additional members: ERK 3, ERK 5 and ERK 6.(ET1610-13)