1874 Results for: "L-Ornithine+L-Aspartate"

Supplier: ANTIBODIES.COM

Rabbit polyclonal antibody to NMDAepsilon4 for IHC and ELISA with samples derived from Human, Mouse and Rat.

Supplier: ANTIBODIES.COM

Rabbit polyclonal antibody to GRIN2D for WB and ELISA with samples derived from Human, Mouse and Rat.

Supplier: ProSci Inc.

Cad regulates embryonic abdominal segment formation by zygotically activating expression of knirps (kni) and giant (gt). It plays a role in the establishment of the hindgut and in the invagination of the hindgut primordium during gastrulation. These effects on the gut are achieved by acting combinatorially at the posterior of the embryo to activate transcription of different targets, including folded gastrulation (fog), fork head (fkh) and wingless (wg).

Supplier: Abcam

Mouse monoclonal [N308/48] to NMDAR1 - Neuronal Marker.

Supplier: Abcam

Rabbit monoclonal [EP1858Y] to NMDAR2B (phospho S1303).

Supplier: Abcam

Rabbit polyclonal to SLC25A13/Citrin.

Supplier: Abcam

The most sensitive kit to evaluate potential human Arginase I inhibitors.

Supplier: Bioss

C22orf43 (chromosome 22 open reading frame 43), also known as MGC33025 or MGC75009, is a 229 amino acid protein encoded by a gene located on human chromosome 22, which contains over 500 genes and about 49 million bases. As the second smallest human chromosome, chomosome 22 contains a wide variety of genes with numerous functions. Phelan-McDermid syndrome, Neurofibromatosis type 2 and autism are associated with chromosome 22. A schizophrenia susceptibility locus has been identified on chromosome 22 and studies show that 22q11 deletion symptoms include a high incidence of schizophrenia. Translocations between chromosomes 9 and 22 may lead to the formation of the Philadelphia Chromosome and the subsequent production of the novel fusion protein, BCR-Abl, a potent cell proliferation activator found in several types of leukemia.

Supplier: ProSci Inc.

GRINA Antibody: The transmembrane BAX inhibitor motif (TMBIM) family of proteins includes the founder member TMBIM6/BI-1, TMBIM1/RECS1 (responsive to centrifugal force and shear stress gene 1 protein), TMBIM2/LFG (life guard), TMBIM3/GRINA (glutamate receptor ionotropic NMDA protein 1), TMBIM4/GAAP (Golgi anti-apoptotic-associated protein), and TMBIM5/GHTIM (growth hormone-inducible transmembrane protein). They are highly conserved in mammals and zebrafish and contain a conserved BAX inhibitor-1 motif. GRINA is expressed in the brain and is a potential apoptotic regulator.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

Supplier: Bioss

Aspartyl/asparaginyl beta-hydroxylase (ASPH) is a widely-expressed type II membrane protein involved in calcium homeostasis. Located in the endoplasmic reticulum, ASPH specifically hydroxylates an Asp or Asn residue in the epidermal growth factor-like (EGF) domains of several proteins, using iron as a cofactor. The ASPH gene encodes 3 proteins, ASPH, Junctin, and Junctate (or Humbug), that differ significantly in their C-terminal domains. These ASPH gene products are expressed as five transcript variants that differ by their roles in calcium storage and release, hydroxylation capabilities, and tissue specificity. While all ASPH variants are expressed in skeletal muscle, only some are detected in heart, brain, pancreas, placenta, lung, liver, and kidney tissues. In the lumen of the endoplasmic reticulum, ASPH can be processed into two different forms.

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

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

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

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

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

Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines residing in the dinucleotide CpG motif, and this methylation results in transcriptional repression of the target gene. The Dnmt enzymes are encoded by independent genes. Dnmt1 is the most abundant, and it preferentially methylates hemimethylated DNA and coordinates gene expression during development. Additional mammalian Dnmt proteins include Dnmt2 and Dnmt3. Dnmt2 lacks the large N-terminal regulator domain of Dnmt1, is expressed at substantially lower levels in adult tissues, and is likely involved in methylating newly integrated retroviral DNA. Dnmt3a and Dnmt3b are encoded by two distinct genes, but both are abundantly expressed in embryonic stem cells, where they also methylate CpG motifs on DNA.

Supplier: Bioss

Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines residing in the dinucleotide CpG motif, and this methylation results in transcriptional repression of the target gene. The Dnmt enzymes are encoded by independent genes. Dnmt1 is the most abundant, and it preferentially methylates hemimethylated DNA and coordinates gene expression during development. Additional mammalian Dnmt proteins include Dnmt2 and Dnmt3. Dnmt2 lacks the large N-terminal regulator domain of Dnmt1, is expressed at substantially lower levels in adult tissues, and is likely involved in methylating newly integrated retroviral DNA. Dnmt3a and Dnmt3b are encoded by two distinct genes, but both are abundantly expressed in embryonic stem cells, where they also methylate CpG motifs on DNA.

Supplier: Bioss

Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines residing in the dinucleotide CpG motif, and this methylation results in transcriptional repression of the target gene. The Dnmt enzymes are encoded by independent genes. Dnmt1 is the most abundant, and it preferentially methylates hemimethylated DNA and coordinates gene expression during development. Additional mammalian Dnmt proteins include Dnmt2 and Dnmt3. Dnmt2 lacks the large N-terminal regulator domain of Dnmt1, is expressed at substantially lower levels in adult tissues, and is likely involved in methylating newly integrated retroviral DNA. Dnmt3a and Dnmt3b are encoded by two distinct genes, but both are abundantly expressed in embryonic stem cells, where they also methylate CpG motifs on DNA.

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

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

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

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.