anti-PSD-95 (palmitoylated), mAb (rec.) (PF11)

anti-PSD95 Palmitoylated, mAb (rec.) (PF11) is composed of human variable regions (VH and VL) (lambda-chain) of immunoglobulin fused to the human lgG2 Fc domain. anti-PSD95 Palmitoylated (human), monoclonal recombinant antibody (blocking) (PF11) is an antibody developed by antibody phage display technology using a human naive antibody gene library. These libraries consist of scFv (single chain fragment variable) composed of VH (variable domain of the human immunoglobulin heavy chain) and VL (variable domain of the human immunoglobulin light chain) connected by a polypeptide linker. The antibody fragments are displayed on the surface of filamentous bacteriophage (M13). This scFv was selected by affinity selection on antigen in a process termed panning. Multiple rounds of panning are performed to enrich for antigen-specific scFv-phage. Monoclonal antibodies are subsequently identified by screening after each round of selection. The selected monoclonal scFv is cloned into an appropriate vector containing a Fc portion of interest and then produced in mammalian cells to generate an IgG like scFv-Fc fusion protein. Recognizes human, mouse and rat palmitoylated PSD-95. Isotype: Human IgG2. Clone: PF11. Applications: ICC, IHC. Liquid. In PBS containing 10% glycerol. PSD-95 is a member of proteins located at a specialized postsynaptic membrane region, called the postsynaptic density (PSD). PSD-95 is the most abundant scaffold protein specifically enriched in the PSD. It contains three PDZ domains, an SH3 domain and a guanylate kinase (GuK)-like domain. Through its PDZ domains, PSD-95 assembles various synaptic components at the PSD including intracellular signaling molecules (e.g. SynGAP and kalirin-7), ion channels (e.g. stargazin/AMPA receptors [AMPARs] and NMDA receptors) and cell adhesion molecules (e.g. neuroligin). PSD-95 plays a primary role in synaptic development and maturation and is regulated by palmitoylation at its N-terminal cysteine residues leading to its postsynaptic targeting. Palmitoylation of PSD-95 is triggered by DHHC2, a plasma membrane-inserted palmitoylating enzyme. Palmitoylated PSD-95 is almost exclusively localized at excitatory synapses in neurons.