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Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Involved in cellular amino acid uptake. Acts as an amino acid exchanger. Involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta. Plays a role in neuronal cell proliferation (neurogenesis) in brain. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. May play an important role in high-grade gliomas. Mediates blood-to-retina L-leucine transport across the inner blood-retinal barrier which in turn may play a key role in maintaining large neutral amino acids as well as neurotransmitters in the neural retina. Acts as the major transporter of tyrosine in fibroblasts.

Supplier: Bioss

Na+/Cl- dependent neurotransmitter transporters are a superfamily of transmembrane proteins that contain 12 membrane spanning regions (1). Specifically, the highly hydrophobic Na+/Cl- dependent glycine transporters (GlyT) are crucial for the termination of neurotransmission at glycinergic synapses (2,3). Two different GlyT genes encode GlyT2 and GlyT1, which exists as two isoforms produced by alternative splicing of the same gene located on human chromosome 1p31.3 (3,4). The GlyT1 gene may be an early marker of neural development and encodes glia-specific transporter proteins (3). Although GlyT1 and GlyT2 are both expressed in the brain and spinal cord, each shows a unique pattern of expression (3,5,6). GlyT1 is found only in the white matter of the CNS, whereas GlyT2 is found in the gray matter of the CNS as well as in macrophages and mast cells in peripheral tissues (3,5). The anatomic distribution of GlyT2 mRNA suggests that glycine may act as a supraspinal neurotransmitter and may function as a chemical messenger outside the CNS (5).

Supplier: Bioss

Na+/Cl- dependent neurotransmitter transporters are a superfamily of transmembrane proteins that contain 12 membrane spanning regions (1). Specifically, the highly hydrophobic Na+/Cl- dependent glycine transporters (GlyT) are crucial for the termination of neurotransmission at glycinergic synapses (2,3). Two different GlyT genes encode GlyT2 and GlyT1, which exists as two isoforms produced by alternative splicing of the same gene located on human chromosome 1p31.3 (3,4). The GlyT1 gene may be an early marker of neural development and encodes glia-specific transporter proteins (3). Although GlyT1 and GlyT2 are both expressed in the brain and spinal cord, each shows a unique pattern of expression (3,5,6). GlyT1 is found only in the white matter of the CNS, whereas GlyT2 is found in the gray matter of the CNS as well as in macrophages and mast cells in peripheral tissues (3,5). The anatomic distribution of GlyT2 mRNA suggests that glycine may act as a supraspinal neurotransmitter and may function as a chemical messenger outside the CNS (5).

Supplier: Bioss

The four isoforms of potassium/chloride co-transport channels (KCC) belong to a superfamily of cation-chloride co-transporters involved in cell volume maintenance. Nitric oxide (NO) donors activate KCCs, while inhibitors of the cGMP pathway prevent NO donor activation. The ubiquitously expressed KCC1 contains 12 transmembrane domains with both cytoplasmic N and C terminal domains. KCC2 expression is limited to neuronal tissues by a restrictive element similar to the neuronal-restrictive silencing factor. In neurons, KCC2 expression is correlated with an inhibitory response to GABA, while the absence of KCC2 is necessary for an unusual excitatory response to GABA. Alterations of KCC2 expression in the inferior colliculus of rat brain may be related to seizure susceptibility. Conversely, KCC3 is not suspected to play a major role in epilepsy. The two splice variants of KCC3, KCC3a and KCC3b, are predominantly expressed in brain and kidney, respectively, while KCC4 is expressed in muscle, brain, lung, heart and kidney.

Supplier: Bioss

The four isoforms of potassium/chloride co-transport channels (KCC) belong to a superfamily of cation-chloride co-transporters involved in cell volume maintenance. Nitric oxide (NO) donors activate KCCs, while inhibitors of the cGMP pathway prevent NO donor activation. The ubiquitously expressed KCC1 contains 12 transmembrane domains with both cytoplasmic N and C terminal domains. KCC2 expression is limited to neuronal tissues by a restrictive element similar to the neuronal-restrictive silencing factor. In neurons, KCC2 expression is correlated with an inhibitory response to GABA, while the absence of KCC2 is necessary for an unusual excitatory response to GABA. Alterations of KCC2 expression in the inferior colliculus of rat brain may be related to seizure susceptibility. Conversely, KCC3 is not suspected to play a major role in epilepsy. The two splice variants of KCC3, KCC3a and KCC3b, are predominantly expressed in brain and kidney, respectively, while KCC4 is expressed in muscle, brain, lung, heart and kidney.

Supplier: Bioss

Na+/Cl- dependent neurotransmitter transporters are a superfamily of transmembrane proteins that contain 12 membrane spanning regions (1). Specifically, the highly hydrophobic Na+/Cl- dependent glycine transporters (GlyT) are crucial for the termination of neurotransmission at glycinergic synapses (2,3). Two different GlyT genes encode GlyT2 and GlyT1, which exists as two isoforms produced by alternative splicing of the same gene located on human chromosome 1p31.3 (3,4). The GlyT1 gene may be an early marker of neural development and encodes glia-specific transporter proteins (3). Although GlyT1 and GlyT2 are both expressed in the brain and spinal cord, each shows a unique pattern of expression (3,5,6). GlyT1 is found only in the white matter of the CNS, whereas GlyT2 is found in the gray matter of the CNS as well as in macrophages and mast cells in peripheral tissues (3,5). The anatomic distribution of GlyT2 mRNA suggests that glycine may act as a supraspinal neurotransmitter and may function as a chemical messenger outside the CNS (5).

Supplier: Brady

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Supplier: VELP SCIENTIFIC

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Supplier: Bioss

The four isoforms of potassium/chloride co-transport channels (KCC) belong to a superfamily of cation-chloride co-transporters involved in cell volume maintenance. Nitric oxide (NO) donors activate KCCs, while inhibitors of the cGMP pathway prevent NO donor activation. The ubiquitously expressed KCC1 contains 12 transmembrane domains with both cytoplasmic N and C terminal domains. KCC2 expression is limited to neuronal tissues by a restrictive element similar to the neuronal-restrictive silencing factor. In neurons, KCC2 expression is correlated with an inhibitory response to GABA, while the absence of KCC2 is necessary for an unusual excitatory response to GABA. Alterations of KCC2 expression in the inferior colliculus of rat brain may be related to seizure susceptibility. Conversely, KCC3 is not suspected to play a major role in epilepsy. The two splice variants of KCC3, KCC3a and KCC3b, are predominantly expressed in brain and kidney, respectively, while KCC4 is expressed in muscle, brain, lung, heart and kidney.

Supplier: Bioss

The four isoforms of potassium/chloride co-transport channels (KCC) belong to a superfamily of cation-chloride co-transporters involved in cell volume maintenance. Nitric oxide (NO) donors activate KCCs, while inhibitors of the cGMP pathway prevent NO donor activation. The ubiquitously expressed KCC1 contains 12 transmembrane domains with both cytoplasmic N and C terminal domains. KCC2 expression is limited to neuronal tissues by a restrictive element similar to the neuronal-restrictive silencing factor. In neurons, KCC2 expression is correlated with an inhibitory response to GABA, while the absence of KCC2 is necessary for an unusual excitatory response to GABA. Alterations of KCC2 expression in the inferior colliculus of rat brain may be related to seizure susceptibility. Conversely, KCC3 is not suspected to play a major role in epilepsy. The two splice variants of KCC3, KCC3a and KCC3b, are predominantly expressed in brain and kidney, respectively, while KCC4 is expressed in muscle, brain, lung, heart and kidney.

Supplier: Sartorius

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Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Essity

Tork Xpress® soft multifold hand towels natural H2, advanced, tear-resistant, 2-ply. Give guests more comfort when drying hands with these large multifold paper hand towels.

Supplier: Bioss

Making up nearly 6% of the human genome, chromosome 6 contains around 1,200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf192 gene product has been provisionally designated C6orf192 pending further characterization.

Supplier: Bioss

Making up nearly 6% of the human genome, chromosome 6 contains around 1,200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf192 gene product has been provisionally designated C6orf192 pending further characterization.

Supplier: Bioss

The four isoforms of potassium/chloride co-transport channels (KCC) belong to a superfamily of cation-chloride co-transporters involved in cell volume maintenance. Nitric oxide (NO) donors activate KCCs, while inhibitors of the cGMP pathway prevent NO donor activation. The ubiquitously expressed KCC1 contains 12 transmembrane domains with both cytoplasmic N and C terminal domains. KCC2 expression is limited to neuronal tissues by a restrictive element similar to the neuronal-restrictive silencing factor. In neurons, KCC2 expression is correlated with an inhibitory response to GABA, while the absence of KCC2 is necessary for an unusual excitatory response to GABA. Alterations of KCC2 expression in the inferior colliculus of rat brain may be related to seizure susceptibility. Conversely, KCC3 is not suspected to play a major role in epilepsy. The two splice variants of KCC3, KCC3a and KCC3b, are predominantly expressed in brain and kidney, respectively, while KCC4 is expressed in muscle, brain, lung, heart and kidney.

Supplier: Bioss

Na+/Cl- dependent neurotransmitter transporters are a superfamily of transmembrane proteins that contain 12 membrane spanning regions (1). Specifically, the highly hydrophobic Na+/Cl- dependent glycine transporters (GlyT) are crucial for the termination of neurotransmission at glycinergic synapses (2,3). Two different GlyT genes encode GlyT2 and GlyT1, which exists as two isoforms produced by alternative splicing of the same gene located on human chromosome 1p31.3 (3,4). The GlyT1 gene may be an early marker of neural development and encodes glia-specific transporter proteins (3). Although GlyT1 and GlyT2 are both expressed in the brain and spinal cord, each shows a unique pattern of expression (3,5,6). GlyT1 is found only in the white matter of the CNS, whereas GlyT2 is found in the gray matter of the CNS as well as in macrophages and mast cells in peripheral tissues (3,5). The anatomic distribution of GlyT2 mRNA suggests that glycine may act as a supraspinal neurotransmitter and may function as a chemical messenger outside the CNS (5).

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: SI Analytics

The Powerful TW 7450 developed for high sample throughput.

Supplier: Bioss

Na+/Cl- dependent neurotransmitter transporters are a superfamily of transmembrane proteins that contain 12 membrane spanning regions (1). Specifically, the highly hydrophobic Na+/Cl- dependent glycine transporters (GlyT) are crucial for the termination of neurotransmission at glycinergic synapses (2,3). Two different GlyT genes encode GlyT2 and GlyT1, which exists as two isoforms produced by alternative splicing of the same gene located on human chromosome 1p31.3 (3,4). The GlyT1 gene may be an early marker of neural development and encodes glia-specific transporter proteins (3). Although GlyT1 and GlyT2 are both expressed in the brain and spinal cord, each shows a unique pattern of expression (3,5,6). GlyT1 is found only in the white matter of the CNS, whereas GlyT2 is found in the gray matter of the CNS as well as in macrophages and mast cells in peripheral tissues (3,5). The anatomic distribution of GlyT2 mRNA suggests that glycine may act as a supraspinal neurotransmitter and may function as a chemical messenger outside the CNS (5).

Supplier: Bioss

Na+/Cl- dependent neurotransmitter transporters are a superfamily of transmembrane proteins that contain 12 membrane spanning regions (1). Specifically, the highly hydrophobic Na+/Cl- dependent glycine transporters (GlyT) are crucial for the termination of neurotransmission at glycinergic synapses (2,3). Two different GlyT genes encode GlyT2 and GlyT1, which exists as two isoforms produced by alternative splicing of the same gene located on human chromosome 1p31.3 (3,4). The GlyT1 gene may be an early marker of neural development and encodes glia-specific transporter proteins (3). Although GlyT1 and GlyT2 are both expressed in the brain and spinal cord, each shows a unique pattern of expression (3,5,6). GlyT1 is found only in the white matter of the CNS, whereas GlyT2 is found in the gray matter of the CNS as well as in macrophages and mast cells in peripheral tissues (3,5). The anatomic distribution of GlyT2 mRNA suggests that glycine may act as a supraspinal neurotransmitter and may function as a chemical messenger outside the CNS (5).

Supplier: Bioss

Making up nearly 6% of the human genome, chromosome 6 contains around 1,200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf192 gene product has been provisionally designated C6orf192 pending further characterization.

Supplier: Sartorius Balances

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Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

The four isoforms of potassium/chloride co-transport channels (KCC) belong to a superfamily of cation-chloride co-transporters involved in cell volume maintenance. Nitric oxide (NO) donors activate KCCs, while inhibitors of the cGMP pathway prevent NO donor activation. The ubiquitously expressed KCC1 contains 12 transmembrane domains with both cytoplasmic N and C terminal domains. KCC2 expression is limited to neuronal tissues by a restrictive element similar to the neuronal-restrictive silencing factor. In neurons, KCC2 expression is correlated with an inhibitory response to GABA, while the absence of KCC2 is necessary for an unusual excitatory response to GABA. Alterations of KCC2 expression in the inferior colliculus of rat brain may be related to seizure susceptibility. Conversely, KCC3 is not suspected to play a major role in epilepsy. The two splice variants of KCC3, KCC3a and KCC3b, are predominantly expressed in brain and kidney, respectively, while KCC4 is expressed in muscle, brain, lung, heart and kidney.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.

Supplier: Bioss

Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.