Phospho-Numb (Ser276) Antibody detects endogenous levels of Numb protein only when phosphorylated on Ser276.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to Ser276 of the human Numb protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Numb contains an amino-terminal phosphotyrosine-binding (PTB) domain and carboxy-terminal endocytic binding motifs for α-adaptin and EH (Eps15 homology) domain-containing proteins, indicating a role in endocytosis (1,2). There are four mammalian Numb splicing isoforms that are differentially expressed and may have distinct functions (3-5). Numb acts as a negative regulator of Notch signaling by promoting ubiquitination and degradation of Notch (6). The protein is asymmetrically segregated into one daughter cell during cell division, producing two daughter cells with different responses to Notch signaling and different cell fates (7,8). The localization of Numb can also be regulated by G-protein coupled receptor (GPCR) and PKC signaling (9).Numb can be phosphorylated at several sites including Ser7, Ser276 and Ser295. Phosphorylation at these sites regulates asymmetric membrane localization of Numb and integrin endocytosis (10-12).