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|Tested species reactivity||Mouse , Rat|
|Published species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic peptide derived from the mid region of PSD-93 protein.|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.4|
|Contains||0.1% sodium azide|
|Tested Applications||Dilution *|
|Immunofluorescence (IF)||Assay Dependent|
|Immunoprecipitation (IP)||Assay Dependent|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Immunocytochemistry (ICC)||See 1 publications below|
PSD-93, also known as chapsyn-110, is one of a family of plasma membrane-associated proteins found in synaptic junctions. PSD-93 is unique among family members in its expression in Purkinje neuron cell bodies and dendrites. PSD-93 has three ~90 amino acid repeats called PDZ domains, a single interior SH3 domain, and a carboxyl-terminal guanylate kinase homology (GuK) domain that is enzymatically inactive. It is hypothesized that PDZ-domain interactions play a role in receptor and channel clustering which contributes to neuronal plasticiyt. PSD-93 is believed to participate in the clustering of certain proteins, including NMDA receptors and shaker-type potassium channels at the synaptic membrane. There are two principal modes of interaction between PSD-93 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 may interact with PSD-93 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-93 in vitro through a pseudo-homotypic PDZ-PDZ interaction.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Essential contribution of the ligand-binding beta B/beta C loop of PDZ1 and PDZ2 in the regulation of postsynaptic clustering, scaffolding, and localization of postsynaptic density-95.
||Nonaka M,Doi T,Fujiyoshi Y,Takemoto-Kimura S,Bito H||The Journal of neuroscience : the official journal of the Society for Neuroscience (26:763)||2006|
Dlgh2, B230218P12Rik, B330007M19Rik, PSD93, Gm1197, A330103J02Rik
channel-associated protein of synapse-110, chapsyn-110, disks large homolog 2, postsynaptic density protein PSD-93, discs large homolog 2, synaptic density protein PSD-93, Chapsyn-110, Post Synaptic Density 93, Chapsyn-1