You Searched For: N-Fmoc-glycine


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Catalog Number: (10366-996)
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).


Supplier: TCI America
Description: [for Fluorometric Determination of Ca] CAS Number: 154071-48-4 MDL Number: MFCD00005049 Molecular Formula: C30H26N2O13 Molecular Weight: 622.54 Form: Crystal Color: Reddish Yellow
Catalog Number: (76117-176)
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.


Supplier: MilliporeSigma

SDS Environmentally Preferable

Catalog Number: (103007-832)
Supplier: Anaspec Inc
Description: This cell permeable peptide is derived from the BH3 domain (a death domain) of Noxa A, amino acid residues 17 to 36. Eight D-Arginine residues and a Glycine linker residue are added to the amino terminal of the peptide.
Sequence:rrrrrrrrGAELPPEFAAQLRKIGDKVYC
MW:3555.2 Da
% peak area by HPLC:95
Storage condition:-20° C


Catalog Number: (10407-222)
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.


Catalog Number: (10433-408)
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.


Catalog Number: (76117-178)
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.


Catalog Number: (10111-652)
Supplier: Prosci
Description: USP48 is a protein containing domains that associate it with the peptidase family C19, also known as family 2 of ubiquitin carboxyl-terminal hydrolases. Family members function as deubiquitinating enzymes, recognizing and hydrolyzing the peptide bond at the C-terminal glycine of ubiquitin. Enzymes in peptidase family C19 are involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.


Catalog Number: (10407-224)
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.


Catalog Number: (10407-214)
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.


Catalog Number: (10072-570)
Supplier: Prosci
Description: LAG-1 is CC chemokine that signals through the CCR5 receptor. LAG-1 is identical to MIP-1beta (ACT II isotype) except for two amino acid substitutions; arginine for histidine at position 22 and serine for glycine at position 47 of the mature protein. LAG-1 chemoattracts monocytes, and exhibits activity as an HIV suppressive factor. Recombinant human LAG-1 is a 7.7 kDa protein containing 69 amino acid residues.


Catalog Number: (10389-144)
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.


Catalog Number: (89163-220)
Supplier: Enzo Life Sciences
Description: Host: Rabbit


Catalog Number: (77437-492)
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.


Supplier: Adipogen
Description: Cold-inducible RNA-binding protein (CIRP) is from the family of cold shock proteins that plays a protective role in the genotoxic and cold stress response. CIRBP functions as an RNA chaperone to facilitate translation and to stabilize transcripts of genes involved in cell survival. CIRP (human) is a 172-aa nuclear protein consisting of one amino-terminal consensus sequence RNA-binding domain and one carboxyl-terminal glycine-rich domain. When overexpressed, CIRP promotes assembly of stress granules (SGs). CIRP is constitutively expressed at low levels in various tissues becoming up-regulated during mild hypothermia as well as exposure to UV irradiation and hypoxia. CIRP is also found extracellularly, where it acts as a proinflammatory mediator causing deleterious effects during hemorrhagic and septic shock.

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