JIP-2 (N601) polyclonal antibody

C-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family. JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser 63 and Ser 73, resulting in transcriptional activation. Two additional JNK family members have been identified as JNK2 and JNK3. JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding. Multiple splice variants of JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain.

C-Jun-amino-terminal kinase-interacting protein 2; JIP-2; JNK-interacting protein 2; Islet-brain-2; IB-2; JNK MAP kinase scaffold protein 2; Mitogen-activated protein kinase 8-interacting protein 2; MAPK8IP2; IB2; JIP2; PRKM8IPL

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .