Invitrogen™ PSD-95 Recombinant Rabbit Monoclonal Antibody (23H23L19)

Beschreibung

700902 has been successfully used in immunofluorescence analysis of PSD95 in human motor neurons derived from iPSCs. Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.

Post Synaptic Density 95 kDa (PSD-95), also known as synapse associated protein 90 kDa (SAP90), is one of a family of membrane-associated proteins found in the postsynaptic density in forebrain neurons and certain presynaptic structures in the cerebellum. Like other members of the family, PSD-95 has three 90 amino acid repeats called PDZ domains followed by an SH3 domain and a yeast guanylate kinase homology (GuK) domain. PSD-95 is believed to participate in the clustering of certain proteins, including NMDA receptors, Shaker-type potassium channels at the synaptic membrane in central nervous system (CNS) neurons. There are two principal modes of interaction between PSD-95 and other proteins. NMDA receptors and shaker-type potassium channels both share C-terminal sequence homology consisting of a threonine/serine-X-valine-COOH (T/SXV) motif. Other neuronal proteins that share this motif (beta 1 adrenergic receptor, some serotonin receptors, some sodium channel subunits, and additional potassium channel subunits), and some of these proteins may interact with PSD-95 by binding to its PDZ domains. Neuronal nitric oxide synthase (nNOS), which lacks the T/SXV motif but which has its own PDZ domain, has been shown to associate with PSD-95 in vitro through a pseudo-homotypic PDZ-PDZ interaction.