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 proteincoupled receptor ligands and neurotransmitters can initiate MAPK signaling pathways. Activation of ERK 1 and ERK 2 requires phosphorylation by upstream kinases such as MAP kinasekinase (MEK), MEK kinase and Raf-1. ERK 1 and ERK 2 phosphorylation can occur at specific tyrosine and threonine sites mapping within consensus motifs that include the threonine-glutamatetyrosine 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 ERK 1 gene maps to chromosome 16p11.2 and encodes a 379 amino acid protein that shares 83% sequence identity to ERK 2.
Immunogen
Amino acids 101-172 mapping near the N-terminus of ERK 2 of human origin.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIF
WB:1:100-1:1,000 IP:1-2 μg per 100-500 μg of total protein (1 ml of cell lysate) IF:1:50-1:500
