Rat Notch-2 Biotinylated Antibody

Rat Notch-2 is a 300 kDa, type I transmembrane glycoprotein involved in a number of early-event developmental processes (1). In both vertebrates and invertebrates, Notch signaling is important for specifying cell fates and for defining boundaries between different cell types. The molecule is synthesized as a 2472 amino acid (aa) precursor that contains a putative 27 aa signal sequence, a 1650 aa extracellular region, a 23 aa transmembrane (TM) segment and a 772 aa cytoplasmic domain (2). The large Notch extracellular domain has 36 EGF-like repeats followed by three notch/Lin-12 repeats (LNR). Of the 36 EGF-like repeats, the 11^th and 12^thEGF-like repeats have been shown to be both necessary and sufficient for binding the ligands Serrate and Delta, in Drosophila (3). Cell surface Notch receptor is thought to be a heterodimer consisting of the ligand binding extracellular region associated with the remaining transmembrane protein, as a result of post‑translational proteolytic cleavage by a furin-like enzyme. Upon ligand binding, additional proteolysis events result in the release of the Notch intracellular domain (NICD). NICD translocates into the nucleus and initiates transcription of Notch-responsive genes (4). Thus Notch acts as both a ligand-binding receptor and a nuclear factor that regulates transcription. In addition, an alternative Notch signaling pathway that is mediated by the full-length, uncleaved form of Notch-1 at the cell surface has been reported to suppress differentiation of myoblasts in response to ligand binding (5). Rat Notch-2 shows 92% and 95% aa identity to human and mouse Notch-2 extracellular domains, respectively. Relative to the extracellular region of rat Notch-1, rat Notch-2 exhibits 56% aa identity.