85-1401-35　Glutamate Transporter, Rat (GTRAP48, EAAT4, Associated Protein) Control Peptide 100ug　G4005-95A

特徴

• A 15aa synthetic peptide near the N-terminus of rat GTRAP48 was synthesized, conjugated to KLH.
• Glutamate is the main excitatory neurotransmitter in the brain. To date five glutamate Transporters have been cloned: GLAST (EAAT1), GLT1 (EAAT2), EAAC1 (EAAT3), EAAT4, and EAAT5. These transporters are believed to be critical in reducing potentially toxic extracellular concentration of glutamate by rapid uptake into nerve terminals and glial cells. Most recently two proteins, designated GTRAP41 and GTRAP48 (for glutamate transporter EAAT4 associated protein) that specifically interact with the intracellular carboxy-terminal domain of EAAT4 have been cloned and characterized. The proteins are proposed to modulate glutamate transport activity. GTRAP41 is 2388 aa protein (~270kD). It has seventeen 16-amino acid spectrin repeats, 2 alpha-actinin domains, and a pleckstrin homology domain. GTRAP48 is 1527 aa (~170kD). GTRAP48 possesses a PDZ domain, a regulatory G protein-signaling sequence, tandem dbl homology and pleckstrin homology domains characteristic of guanine nucleotide exchange factors for the Rho family of G proteins, and 2 proline-rich sequences. brain tissue. GTRAP41 and GTRAP48 are mainly expressed in the brain, and lower levels were also detected in liver and kidney. EAAT4, GTRAP41, and GTRAP48 are all immunolocalized in cerebellar Purkinje cell soma and dendrites, with little axonal staining. GTRAP48 was found to activate Rho. Expression of GTRAP48 induced the reorganization of the actin cytoskeleton. When GTRAP41 and GTRAP48 are coexpressed, GTRAP41 colocalized with actin in structures that resemble actin-stress fibers, a typical Rho-dependent effect. Overexpression of GTRAP41 and GTRAP48 enhanced glutamate uptake. GTRAP41 and GTRAP48 may therefore enhance glutamate transport either through an increase in the catalytic rate of the transporter or through an increase in cell-surface availability or by stabilizing EAAT4 at the membrane.