You Searched For: N-Fmoc-N-benzyl-glycine

Catalog Number: (BOSSBS-3307R-A647)

Supplier: Bioss

Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-133 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).

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Catalog Number: (BOSSBS-0222R-A350)

Supplier: Bioss

Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).

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Catalog Number: (BOSSBS-3306R-A555)

Supplier: Bioss

Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity).

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Catalog Number: (BOSSBS-11604R-CY3)

Supplier: Bioss

Description: 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).

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Catalog Number: (BOSSBS-5902R)

Supplier: Bioss

Description: This gene is a member of the glycine-rich RNA-binding protein family and encodes a protein with one RNA recognition motif (RRM) domain. Expression of this gene is induced by cold shock and low oxygen tension. A pseudogene exists on chromosome 1. Multiple alternatively spliced transcript variants that are predicted to encode different isoforms have been characterized although some of these variants fit nonsense-mediated decay (NMD) criteria. [provided by RefSeq, Jul 2008].

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Catalog Number: (BOSSBS-11604R-A350)

Supplier: Bioss

Description: 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).

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Catalog Number: (BOSSBS-11604R-HRP)

Supplier: Bioss

Description: 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).

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Catalog Number: (BOSSBS-5040R-A750)

Supplier: Bioss

Description: Involved in bile acid metabolism. In liver hepatocytes catalyses the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyse the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyses the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

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Catalog Number: (BOSSBS-5040R-A555)

Supplier: Bioss

Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

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Catalog Number: (BOSSBS-3806R-A350)

Supplier: Bioss

Description: Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity.

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Catalog Number: (BOSSBS-3873R-A750)

Supplier: Bioss

Description: ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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Catalog Number: (BOSSBS-3873R-A350)

Supplier: Bioss

Description: ATG4A is a cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). Form II, with a revealed C-terminal glycine, is considered to be the phosphatidylethanolamine (PE)-conjugated form, and has the capacity for the binding to autophagosomes.

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Catalog Number: (BOSSBS-3301R-CY7)

Supplier: Bioss

Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors (By similarity).

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Catalog Number: (BOSSBS-3301R-A350)

Supplier: Bioss

Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors (By similarity).

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Catalog Number: (BOSSBS-3301R-A647)

Supplier: Bioss

Description: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors (By similarity).

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Catalog Number: (BOSSBS-14371R-A680)

Supplier: Bioss

Description: DNAJB12 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata, 2000 [PubMed 11147971]).[supplied by OMIM, Mar 2008]

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