Anti-ErbB4 Antibody, clone mAB10 clone mab10, from rabbit

Receptor tyrosine-protein kinase erbB-4 (UniProt: Q61527; also known as EC: 2.7.10.1, Proto-oncogene-like protein c-ErbB-4) is encoded by the Erbb4 (also known as Mer4) gene (Gene ID: 13869) in murine species. ErbB-4 is a single-pass type I membrane protein of the EGF receptor family that plays an essential role as cell surface receptor for neuregulins (NRG) and EGF family members. ErbB-4 is monomeric in the absence of bound ligand and it homo- or heterodimerizes with another ERBB family member upon ligand binding. ErbB-4 is autophosphorylated on tyrosine residues in response to ligand binding that triggers receptor dimerization and autophosphorylation at specific tyrosine residues, which then serve as binding sites for scaffold proteins and effectors. ErbB-4 is reported to regulate the development of the heart, the central nervous system, and the mammary gland. It is shown to be involved in gene transcription, cell proliferation, differentiation, migration, and apoptosis. It is expressed in the developing and adult cerebral cortex, and represents the major NRG receptor in central neurons and regulates a diverse array of neuronal processes, including migration, differentiation, neurotransmission, and synaptic plasticity. NRG-1 and ErbB-4 are essentials of a signaling pathway that is critical for the proper development of inhibitory cortical and hippocampal circuits. ErbB-4 expression is reported to be restricted to GABAergic neurons in the cerebral cortex where it plays a role in regulating GABAergic synaptic development and interneuron migration. ErbB-4 is synthesized with a signal peptide (aa 1-25), which is cleaved off in the mature form. The mature form has an extracellular domain (aa 26-652), a short transmembrane domain (aa 653-673), and a long cytoplasmic tail (aa 674-1308). Its protein kinase domain is localized in the cytoplasmic tail (aa 718-985). Three isoforms of ErbB-4 have been described that are produced by alternative splicing.