GRASP / Unconjugated / Polyclonal

Product Details

Description	Tamalin, also named General receptor for phosphoinositides 1-associated scaffold protein (GRASP) is a PDZ (post-synaptic density protein/Drosophila disc large tumor suppressor/zo-1) domain-containing protein that interacts with group 1 metabotropic glutamate receptors (mGluRs). The PDZ domain-containing amino-terminal half of Tamalin binds directly to the class I PDZ-binding motif of group 1 mGluRs. The carboxyl-terminal half of Tamalin binds to cytohesins, which are guanine nucleotide exchange factors (GEFs) specific for the ADP-ribosylation factor (ARF) family of small GTP-binding proteins. Tamalin forms a protein complex with group 1 mGluRs at the post-synaptic site of specific neuronal cells and serves as a key scaffold protein that links a complex formation between mGluR1a and cytohesins. It is reported that Tamalin plays a key role in the association of group 1 mGluRs with the ARF-specific GEF proteins and contributes to intracellular trafficking and the macromolecular organization of group 1 mGluRs at synapses.
Conjugate	Unconjugated
Clone	Polyclonal
Target Species	Mouse
Applications	ELISA, WB, IP
Supplier	Aviva Systems Biology
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About GRASP
This gene encodes a protein that functions as a molecular scaffold, linking receptors, including group 1 metabotropic glutamate receptors, to neuronal proteins. The encoded protein contains conserved domains, including a leucine zipper sequence, PDZ domain and a C-terminal PDZ-binding motif. Alternately spliced transcript variants have been observed for this gene.[provided by RefSeq, Dec 2012]

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