613 Results for: "Multi Channel"

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca²⁺ influx and replenishment of Ca²⁺ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca²⁺ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca²⁺-selective current through coaction with the Ca²⁺ sensor Stim1.

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca²⁺ influx and replenishment of Ca²⁺ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca²⁺ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca²⁺-selective current through coaction with the Ca²⁺ sensor Stim1.

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca2+ influx and replenishment of Ca2+ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca2+ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca2+-selective current through coaction with the Ca2+ sensor Stim1.

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca2+ influx and replenishment of Ca2+ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca2+ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca2+-selective current through coaction with the Ca2+ sensor Stim1.

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca2+ influx and replenishment of Ca2+ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca2+ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca2+-selective current through coaction with the Ca2+ sensor Stim1.

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca2+ influx and replenishment of Ca2+ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca2+ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca2+-selective current through coaction with the Ca2+ sensor Stim1.

Supplier: Bioss

Members of the ligand-gated ion channel receptor family are characterized by their fast transmitting response to neurotransmitters. Two important members of this family are the nicotinic acetylcholine and glutamate receptors, both of which are composed of five homologous subunits forming a transmembrane aqueous pore. These transmembrane receptors change conformation in response to their cognate neurotransmitter. Nicotinic acetylcholine receptors (AChRs) are found at the postsynaptic membrane of the neuromuscular junction and bind acetylcholine molecules, allowing ions to move through the pore. Glutamate receptors are found in the postsynaptic membrane of cells in the central nervous system. The activity that is generated at the synapse by the binding of acetylcholine is terminated by acetylcholinesterase, an enzyme that rapidly hydrolyzes acetylcholine. AChR?, also known as LNCR2, PAOD2, NACHRA3 or CHRNA3, is a 505 amino acid multi-pass membrane protein that belongs to the ligand-gated ion channel receptor family and may play a role in neurotransmission.

Supplier: Bioss

Members of the ligand-gated ion channel receptor family are characterized by their fast transmitting response to neurotransmitters. Two important members of this family are the nicotinic acetylcholine and glutamate receptors, both of which are composed of five homologous subunits forming a transmembrane aqueous pore. These transmembrane receptors change conformation in response to their cognate neurotransmitter. Nicotinic acetylcholine receptors (AChRs) are found at the postsynaptic membrane of the neuromuscular junction and bind acetylcholine molecules, allowing ions to move through the pore. Glutamate receptors are found in the postsynaptic membrane of cells in the central nervous system. The activity that is generated at the synapse by the binding of acetylcholine is terminated by acetylcholinesterase, an enzyme that rapidly hydrolyzes acetylcholine. AChR?, also known as LNCR2, PAOD2, NACHRA3 or CHRNA3, is a 505 amino acid multi-pass membrane protein that belongs to the ligand-gated ion channel receptor family and may play a role in neurotransmission.

Supplier: Bioss

Glutamate receptors mediate most excitatory neurotransmission in the brain and play an important role in neural plasticity, neural development and neurodegeneration. Ionotropic glutamate receptors are categorized into NMDA receptors and kainate/AMPA receptors, both of which contain glutamate-gated, cation-specific ion channels. Synaptic and extrasynaptic NMDA receptors have been shown to have opposite effects on neuronal survival, CREB function and gene regulation. As one of the four major proteins of the NMDA receptor ion channel, GRINA (Glutamate [NMDA] receptor-associated protein 1), also designated NMDA receptor glutamate-binding subunit or putative MAPK-activating protein PM02, is a 371 amino acid multi-pass transmembrane protein. Due to the chromosomal location of the gene encoding GRINA, studies have linked possible GRINA involvement with a form of idiopathic generalized epilepsy.

Supplier: Bioss

Orai2 is a 254 amino acid multi-pass membrane protein that belongs to the orai family of proteins. Localizing to the plasma membrane, Orai2 plays an important role in store-operated calcium (SOC) entry, a process involving Ca2+ influx and replenishment of Ca2+ stores formerly emptied through the action of inositol 1,4,5-trisphosphate production and other Ca2+ mobilizing agents. CRAC channels are responsible for medi-ating calcium influx in T-cells and play an important role in the immune response. Orai2 specifically increases the Ca2+-selective current through coaction with the Ca2+ sensor Stim1.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

CALHM1 is a 346 amino acid multi-pass endoplasmic reticulum membrane protein that belongs to the FAM26 family. CALHM1 co-localizes with GRP 78 to the endoplasmic reticulum. Predominantly expressed in adult brain, CALHM1 may be a pore-forming ion channel that controls cytosolic Ca2+ permeability and cytosolic Ca2+ concentration in the cell. It is suggested that CALHM1 regulates amyloid precursor protein proteolysis and aggregated amyloid-beta peptides levels in a Ca2+ dependent manner. CALHM1 homomultimerizes and shares strong sequence similarities with the selectivity filter of the NMDA receptor, which generates a large Ca2+ conductance across the plasma membrane. CALHM1 may be a potential factor involved in the pathogenesis of Alzheimer's disease.

Supplier: Bioss

CALHM1 is a 346 amino acid multi-pass endoplasmic reticulum membrane protein that belongs to the FAM26 family. CALHM1 co-localizes with GRP 78 to the endoplasmic reticulum. Predominantly expressed in adult brain, CALHM1 may be a pore-forming ion channel that controls cytosolic Ca2+ permeability and cytosolic Ca2+ concentration in the cell. It is suggested that CALHM1 regulates amyloid precursor protein proteolysis and aggregated amyloid-beta peptides levels in a Ca2+ dependent manner. CALHM1 homomultimerizes and shares strong sequence similarities with the selectivity filter of the NMDA receptor, which generates a large Ca2+ conductance across the plasma membrane. CALHM1 may be a potential factor involved in the pathogenesis of Alzheimer's disease.

Supplier: Bioss

CALHM1 is a 346 amino acid multi-pass endoplasmic reticulum membrane protein that belongs to the FAM26 family. CALHM1 co-localizes with GRP 78 to the endoplasmic reticulum. Predominantly expressed in adult brain, CALHM1 may be a pore-forming ion channel that controls cytosolic Ca2+ permeability and cytosolic Ca2+ concentration in the cell. It is suggested that CALHM1 regulates amyloid precursor protein proteolysis and aggregated amyloid-beta peptides levels in a Ca2+ dependent manner. CALHM1 homomultimerizes and shares strong sequence similarities with the selectivity filter of the NMDA receptor, which generates a large Ca2+ conductance across the plasma membrane. CALHM1 may be a potential factor involved in the pathogenesis of Alzheimer's disease.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Bioss

CALHM1 is a 346 amino acid multi-pass endoplasmic reticulum membrane protein that belongs to the FAM26 family. CALHM1 co-localizes with GRP 78 to the endoplasmic reticulum. Predominantly expressed in adult brain, CALHM1 may be a pore-forming ion channel that controls cytosolic Ca2+ permeability and cytosolic Ca2+ concentration in the cell. It is suggested that CALHM1 regulates amyloid precursor protein proteolysis and aggregated amyloid-beta peptides levels in a Ca2+ dependent manner. CALHM1 homomultimerizes and shares strong sequence similarities with the selectivity filter of the NMDA receptor, which generates a large Ca2+ conductance across the plasma membrane. CALHM1 may be a potential factor involved in the pathogenesis of Alzheimer's disease.

Supplier: Bioss

CALHM1 is a 346 amino acid multi-pass endoplasmic reticulum membrane protein that belongs to the FAM26 family. CALHM1 co-localizes with GRP 78 to the endoplasmic reticulum. Predominantly expressed in adult brain, CALHM1 may be a pore-forming ion channel that controls cytosolic Ca2+ permeability and cytosolic Ca2+ concentration in the cell. It is suggested that CALHM1 regulates amyloid precursor protein proteolysis and aggregated amyloid-beta peptides levels in a Ca2+ dependent manner. CALHM1 homomultimerizes and shares strong sequence similarities with the selectivity filter of the NMDA receptor, which generates a large Ca2+ conductance across the plasma membrane. CALHM1 may be a potential factor involved in the pathogenesis of Alzheimer's disease.

Supplier: Bioss

Myotonic dystrophy protein kinase is a multi-domain protein kinase found in muscle that is activated in response to G protein second messengers and proteolysis (1). DMPK is implicated in myotonic muscular dystrophy (DM), an autosomal dominant-inherited disorder that predominately affects skeletal and cardiac muscle and causes defects in cardiac conduction (2,3). DM arises through expansion of CTG repeats in the 3’-UTR of the DMPK gene (4). Mutant DMPK transcripts with an extended region of CUG repeats are retained in the nucleus (5). These transcripts also influence the expression of the DM locus-associated homeodomain protein (DMAHP)/SIX5, to mediate in part the DM phenotype (6). Other substrates for DMPK include myogenin, L-type calcium channels, and Phospholemman (PLM) (1).

Supplier: Prosci

Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the Fo complex, required for F1 and Fo interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. A pseudogene exists on chromosome Yp11.

Supplier: Bioss

MLC1 is a 377 amino acid multi-pass membrane protein that may serve as a non-selective neuronal cation channel in brain. Mutant MLC1 proteins that show impaired folding have been corrected in vitro with the addition of a Ca(2+)-ATPase inhibitor, curcumin. Mutations in the gene encoding MLC1 is the cause of megalencephalic leukoencephalopathy with subcortical cysts, also known as van der Knaap disease, a rare syndrome characterized early in life by progressive brain destruction causing mental retardation and incoordination. Single nucleotide polymorphisms within the MLC1 gene may be associated with periodic catatonia, but there seems to be conflicting evidence on whether or not the gene is implicated in general schizophrenia.

Supplier: Prosci

Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the d subunit of the Fo complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.

Supplier: Bioss

Myotonic dystrophy protein kinase is a multi-domain protein kinase found in muscle that is activated in response to G protein second messengers and proteolysis (1). DMPK is implicated in myotonic muscular dystrophy (DM), an autosomal dominant-inherited disorder that predominately affects skeletal and cardiac muscle and causes defects in cardiac conduction (2,3). DM arises through expansion of CTG repeats in the 3’-UTR of the DMPK gene (4). Mutant DMPK transcripts with an extended region of CUG repeats are retained in the nucleus (5). These transcripts also influence the expression of the DM locus-associated homeodomain protein (DMAHP)/SIX5, to mediate in part the DM phenotype (6). Other substrates for DMPK include myogenin, L-type calcium channels, and Phospholemman (PLM) (1).

Supplier: Bioss

Myotonic dystrophy protein kinase is a multi-domain protein kinase found in muscle that is activated in response to G protein second messengers and proteolysis (1). DMPK is implicated in myotonic muscular dystrophy (DM), an autosomal dominant-inherited disorder that predominately affects skeletal and cardiac muscle and causes defects in cardiac conduction (2,3). DM arises through expansion of CTG repeats in the 3’-UTR of the DMPK gene (4). Mutant DMPK transcripts with an extended region of CUG repeats are retained in the nucleus (5). These transcripts also influence the expression of the DM locus-associated homeodomain protein (DMAHP)/SIX5, to mediate in part the DM phenotype (6). Other substrates for DMPK include myogenin, L-type calcium channels, and Phospholemman (PLM) (1).

Supplier: Bioss

Myotonic dystrophy protein kinase is a multi-domain protein kinase found in muscle that is activated in response to G protein second messengers and proteolysis (1). DMPK is implicated in myotonic muscular dystrophy (DM), an autosomal dominant-inherited disorder that predominately affects skeletal and cardiac muscle and causes defects in cardiac conduction (2,3). DM arises through expansion of CTG repeats in the 3’-UTR of the DMPK gene (4). Mutant DMPK transcripts with an extended region of CUG repeats are retained in the nucleus (5). These transcripts also influence the expression of the DM locus-associated homeodomain protein (DMAHP)/SIX5, to mediate in part the DM phenotype (6). Other substrates for DMPK include myogenin, L-type calcium channels, and Phospholemman (PLM) (1).