You Searched For: N-Fmoc-glycine

Catalog Number: (10107-826)

Supplier: Prosci

Description: RBMY1A1 is a protein containing an RNA-binding motif in the N-terminus and four SRGY (serine, arginine, glycine, tyrosine) boxes in the C-terminus. The gene that encodes RBMY1A1 is Y-linked. RBMY1A1 may be involved in spermatogenesis. It is required for sperm development, possibly by participating in pre-mRNA splicing in the testis.

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: (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.

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

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

SDS Certificates

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.

Supplier: MilliporeSigma

SDS

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).

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: (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: (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: (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: (10108-140)

Supplier: Prosci

Description: HNRPA0 belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind RNAs, followed by a glycine-rich C-terminus.This gene belongs to the A/B subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has two repeats of quasi-RRM domains that bind RNAs, followed by a glycine-rich C-terminus.

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.

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.