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

Catalog Number: (BOSSBS-11604R-FITC)

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).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11604R-A488)

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).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11604R-A647)

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).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3307R-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. 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).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-0222R-CY3)

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).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6233R-A555)

Supplier: Bioss

Description: NMT2 catalyzes the reaction of N-terminal myristoylation of many signaling proteins. It transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. several distinct NMTs exist, varying in apparent molecular weight and /or subcellular distribution.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6233R-A350)

Supplier: Bioss

Description: NMT2 catalyzes the reaction of N-terminal myristoylation of many signaling proteins. It transfers myristic acid from myristoyl coenzyme A to the amino group of a protein's N-terminal glycine residue. several distinct NMTs exist, varying in apparent molecular weight and /or subcellular distribution.

UOM: 1 * 100 µl

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Catalog Number: (ROCKMB-017)

Supplier: Rockland Immunochemicals

Description: SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis, describes a technique widely used in biochemistry to separate proteins according to their electrophoretic mobility (a function of the length of a polypeptide chain and its charge) and no other physical feature. SDS is an anionic detergent applied to protein sample to linearise proteins and to impart a negative charge to linearised proteins.

UOM: 1 * 1 L

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Catalog Number: (BOSSBS-4008R-A750)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3806R-FITC)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3873R-A555)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4008R-A680)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4008R-HRP)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3806R-HRP)

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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-4008R-A350)

Supplier: Bioss

Description: 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.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12103R-FITC)

Supplier: Bioss

Description: Glutamate receptors mediate most excitatory neurotransmission in the brain and play an important role in neural plasticity, neural development and neuro-degeneration. Ionotropic glutamate receptors are categorized into NMDA receptors and kainate/AMPA receptors, both of which contain glutamate-gated, cation-specific ion channels. Kainate/AMPA receptors co-localize with NMDA receptors in many synapses and consist of seven structurally related subunits designated GluR-1 to 7. The kainate/AMPA receptors are primarily responsible for fast excitatory neurotransmission by glutamate, whereas the NMDA receptors exhibit slow kinesis of Ca2+ ions and a high permeability for Ca2+ ions. One such NMDA receptor, NR3B, is expressed in motor neurons and forms cation channels impermeable to calcium, which can resist many open-channel blockers. NR3B functions in the brain as an excitatory glycine receptor, modifying the normal role of glycine as an inhibitory neurotransmitter.

UOM: 1 * 100 µl

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