Description_x000D_ General description_x000D_ Neurabin II belongs to a family of F-actin-binding proteins, highly enriched in dendritic spines and involved in neurite formation. It consists of an F-actin binding domain at the N-terminus, a single PDZ-interacting-domain and a C-terminal coiled-coil domain._x000D_ Immunogen_x000D_ synthetic peptide corresponding to amino acids 800-817 located at the C-terminal region of rat neurabin II. The sequence is identical in human and mouse neurabin II and not found in neurabin I._x000D_ Application_x000D_ Anti-Neurabin II (C-terminal) antibody has been used in_x000D_ • immunoblotting_x000D_ • immunoprecipitation_x000D_ • immunocytochemistry_x000D_ Physical form_x000D_ Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ Neurabins appear to function as bridging proteins by targeting other proteins to the synapse or by linking plasma membrane proteins to the actin cytoskeleton. Neurabin II binds to several proteins including F-actin, protein phosphatase 1 (PP1), at least two subfamilies of G-protein coupled receptors (GPCRs), the α2 adrenergic receptor (α2AR) subtypes and the D2 dopamine receptor. Neurabin II blocks arrestin function in vitro and in vivo at GPCRs and has been also shown to modulate, in vitro and in vivo, both glutaminergic synaptic transmission and the formation and function of dendritic spines. Neurabin II and neurabin I target PP1 subunits that are highly concentrated in dendritic spines and post-synaptic densities. Phosphorylation of neurabin II modulates its interaction with actin filaments, via the anchoring of the neurabin II-PP1 complex within dendritic spines, thereby contributing to the efficacy and plasticity of synaptic transmission.