Votre recherche pour: N-Fmoc-N-benzyl-glycine

Référence Produit: (BOSSBS-2396R-CY5)

Fournisseur: Bioss

Description: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-2396R-CY7)

Fournisseur: Bioss

Description: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-12103R-CY7)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-4009R-CY7)

Fournisseur: Bioss

Description: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-4009R-A488)

Fournisseur: Bioss

Description: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-2976R-CY3)

Fournisseur: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-2976R-A647)

Fournisseur: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-2976R-A350)

Fournisseur: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-11604R-CY5)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-11604R-CY7)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-2396R-A647)

Fournisseur: Bioss

Description: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine.

UOM: 1 * 100 µl

*Promo

Référence Produit: (BOSSBS-6233R-CY7)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-6233R-A647)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-6233R-A750)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-4008R-CY7)

Fournisseur: 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

*Promo

Référence Produit: (BOSSBS-3873R-CY7)

Fournisseur: 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

*Promo