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2-Chloro-4-phenylnicotinonitrile
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2-Chloro-4-phenylnicotinonitrile
Catalog Number:
(10246-544)
Supplier:
Bioss
Description:
The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
Catalog Number:
(75932-304)
Supplier:
Rockland Immunochemical
Description:
The serine/threonine kinase Stk39 belongs to the STE20 family, a group of kinases that are known to interact with inflammation-related kinases (such as p38, JNK, NKCC1, PKC-theta, WNK and MLCK), and with transcription factor AP-1. The STE 20 family is involved in diverse biological phenomena, including cell differentiation, cell transformation/ proliferation, cytoskeleton rearrangement, and the regulation of ion transporters. STK39 contains an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain and is abundantly expressed in the brain. STK39 is activated in response to hypotonic stress, leading to phosphorylation of several cation-chloride-coupled co-transporters. The catalytically active kinase specifically activates the p38 MAP kinase pathway, and its interaction with p38 decreases upon cellular stress, suggesting that this kinase may serve as an intermediate in the response to cellular stress. Recent studies show that STK39 tend to be a novel candidate gene for autism and hypertension.
Catalog Number:
(10246-538)
Supplier:
Bioss
Description:
The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
Catalog Number:
(10246-542)
Supplier:
Bioss
Description:
The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
Catalog Number:
(75932-306)
Supplier:
Rockland Immunochemical
Description:
The serine/threonine kinase Stk39 belongs to the STE20 family, a group of kinases that are known to interact with inflammation-related kinases (such as p38, JNK, NKCC1, PKC-theta, WNK and MLCK), and with transcription factor AP-1. The STE 20 family is involved in diverse biological phenomena, including cell differentiation, cell transformation/ proliferation, cytoskeleton rearrangement, and the regulation of ion transporters. STK39 contains an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain and is abundantly expressed in the brain. STK39 is activated in response to hypotonic stress, leading to phosphorylation of several cation-chloride-coupled co-transporters. The catalytically active kinase specifically activates the p38 MAP kinase pathway, and its interaction with p38 decreases upon cellular stress, suggesting that this kinase may serve as an intermediate in the response to cellular stress. Recent studies show that STK39 tend to be a novel candidate gene for autism and hypertension.
Catalog Number:
(10289-596)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10396-442)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(10396-438)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(10396-432)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(10401-556)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(76077-914)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(10396-434)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(10289-702)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10289-588)
Supplier:
Bioss
Description:
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.
Catalog Number:
(10396-436)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
Catalog Number:
(76077-916)
Supplier:
Bioss
Description:
Functions as a polyspecific organic cation transporter, efficiently transporting many organic cations such as monoamine neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines including serotonin, dopamine, norepinephrine and epinephrine. May play a role in regulating central nervous system homeostasis of monoamine neurotransmitters. May be involved in luminal transport of organic cations in the kidney and seems to use luminal proton gradient to drive organic cation reabsorption. Does not seem to transport nucleoside and nucleoside analogs such as uridine, cytidine, thymidine, adenosine, inosine, guanosine, and azidothymidine. In (PubMed:16873718) adenosine is efficiently transported but in a fashion highly sensitive to extracellular pH, with maximal activity in the pH range 5.5 to 6.5. Glu-206 is essential for the cation selectivity and may function as the charge sensor for cationic substrates. Transport is chloride and sodium-independent but appears to be sensitive to changes in membrane potential. Weakly inhibited by the classical inhibitors of equilibrative nucleoside transport, dipyridamole, dilazep, and nitrobenzylthioinosine. May play a role in the regulation of extracellular adenosine concentrations in cardiac tissues, in particular during ischemia.
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