Recombinant human ERK2 (p42, MAPK1), protein kinase, unactive, 10 µg

Background: Extracellular signal-regulated kinase (ERK) is a serine/threonine protein kinase that functions as the major effector of the Ras protein, a small GTPase. The so called “ERK cascade” consists of three enzymes, the initial GTPase-regulated kinase Raf, (MAP3K) that phosphorylates and activates an intermediate kinase MEK (MAP2K) that, in turn, phosphorylates a threonine and a tyrosine residue of the activation loop of the effector kinase ERK (MAPK).  Both, ERK1 and ERK2 share a high sequence identity (90%) and are co-expressed in most tissues but differ in their relative abundance. The substrate specificities of the  ERK1 and ERK2 protein kinases are very similar. The consensus sequence for ERK1 substrates has been identified as -Pro- Leu-Ser/Thr-Pro. Both kinases are involved in proliferation, differentiation, cell cycle processes, and survival.  ERK1 / 2 differentially phosphorylates a variety of nuclear (Elk-1, c-Myc), cytosolic (MNK1/2, Raf) and cytoskeletal (MAP2, Tau) targets. Since the ERK pathway is often up-regulated in human tumors it represents an attractive target for anticancer drugs development.

Human ERK2/MAPK1, recombinantly expressed in E. coli. Unactive form not phosphorylated by MEK1.

Expression system: E.coli   
Molecular weight: 42,79 kDa
Protein concentration (Bradford with BSA as standard)        1.6 mg/ml
Purity: 95% by SDS PAGE
Specific activity: no significant activity detected
Buffer composition: 20% Glycerol, 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0.

Entrez Gene ID: 5594
UniProtKB: P28482

Ordering information: shipped on dry ice

Product specific literature references:

Gonzalez FA, Raden DL, Davis RJ (1991) "Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases" J. Biol. Chem. 266(33):22159-63

Haycock JW, Ahn NG, Cobb MH, Krebs EG (1992) "ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ" Proc. Natl. Acad. Sci. U S A. 89(6):2365-9

Volente C, Angelastro JM, Greene LA (1993) "Association of protein kinases ERK1 and ERK2 with p75 nerve growth factor receptors" J. Biol. Chem. 268(28):21410-5

Veeranna, Amin ND, Ahn NG, Jaffe H, Winters CA, Grant P, Pant HC (1998) "Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M"  J. Neurosci. 18(11):4008-21