You Searched For: N-Fmoc-glycine

Supplier: Biotium

Description: This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Supplier: Biotium

Description: This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Catalog Number: (75963-970)

Supplier: Biotium

Description: This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Catalog Number: (10671-758)

Supplier: Bioss

Description: Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localizes to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

Catalog Number: (10782-874)

Supplier: Biosensis

Description: Ubiquitin C-terminal hydrolase 1 (UCHL1) has several other names, such as ubiquitin carboxyl esterase L1, ubiquitin thiolesterase, neuron-specific protein PGP9.5 and Park5. It was originally identified as a major component of the neuronal cytoplasm from 2-dimensional gel analysis of brain tissues, and was given the name PGP9.5 (1). The protein is extremely abundant, and was estimated to be present at a concentration of 200-500 µg/g wet weight, representing a major protein component of neuronal cytoplasm (1). This has been claimed to represent 1-2% of total brain protein. It was later found that a ubiquitin C-terminal hydrolase enzyme activity was associated with the PGP9.5 protein, resulting in the renaming of PGP9.5 to ubiquitin C-terminal hydrolase 1.This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. The enzyme also binds to free monoubiquitin and may prevent its degradation in lysosomes.

Supplier: Biotium

Description: This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Catalog Number: (102999-326)

Supplier: Anaspec Inc

Description: In response to Glucose ingestion, proglucagon in the intestinal L cells is cleaved into GLP-1 (1-36). Prior to secretion into the circulation, GLP-1 (1-36) is further processed into amidated GLP-1 (7-36) and small amounts of glycine-extended GLP-1 (7-37). Both GLP-1 (7-36) and GLP-1 (7-37), causes glucose dependent release of insulin by pancreatic beta-cells. They also play a role in gastric motility (gastric emptying), on the suppression of plasma glucagon levels (glucose production) and possibly on the promotion of satiety and stimulation of glucose disposal in peripheral tissues independent of the actions of insulin. GLP-1 peptides such as GLP-1 (1-36) have been used to investigate restoration of pancreatic beta cell function. GLP-1 is also produced in the central nervous system.
Sequence: HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGR-NH2
MW: 4111.5 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Catalog Number: (CAPIPA5-18095)

Supplier: Thermo Scientific

Description: This antibody is predicted to react with rat based on sequence homology. This gene encodes the largest subunit of dynactin, a macromolecular complex consisting of 10 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit interacts with dynein intermediate chain by its domains directly binding to dynein and binds to microtubules via a highly conserved glycine-rich cytoskeleton-associated protein domain in its N-terminus. Alternative splicing of this gene results in multiple transcript variants encoding distinct isoforms. Mutations in this gene cause distal hereditary motor neuronopathy type VIIB which is also known as distal spinal and bulbar muscular atrophy .

Catalog Number: (10070-330)

Supplier: Prosci

Description: NMDA receptors are members of the ionotropic class of glutamate receptors, which also includes Kainate and AMPA receptors. NMDA receptors consist of NR1 subunits combined with one or more NR2 (A-D) or NR3 (A-B) subunits. The ligand-gated channel is permeable to cations including Ca2+, and at resting membrane potentials NMDA receptors are inactive due to a voltage-dependent blockade of the channel pore by Mg2+. NMDA receptor activation, which requires binding of glutamate and glycine, leads to an influx of Ca2+ into the postsynaptic region where it activates several signaling cascades, including pathways leading to the induction of long-term potentiation (LTP) and depression (LTD). NMDA receptors have a critical role in excitatory synaptic transmission and plasticity in the CNS. They govern a range of physiological conditions including neurological disorders caused by excitotoxic neuronal injury, psychiatric disorders and neuropathic pain syndromes.

Catalog Number: (10663-778)

Supplier: Bioss

Description: GOX is a 370 amino acid protein that is expressed in liver and pancreas. HAO1 is localized to peroxisomes and aids in organic acid metabolism via 2-hydroxyacid oxidase activity. 2-hydroxyacid oxidases, such as HAO1, are enzymes that require a flavin cofactor to oxidize 2-hydroxyacids to 2-ketoacids while reducing oxygen to hydrogen peroxide. HAO1 prefenentially oxidizes the substrate glycolate and also oxidizes other substrates, including 2-hydroxy fatty acids as well as L-?hydroxy acids of moderately short chain lengths. The oxidation of glycolate yields glyoxylate which is utilized for peroxisomal synthesis of glycine. HAO1 is also able to convert glyoxylate to oxalate. HAO1 is thought to play a role in the pathophysiology of hyperoxaluria type 1, which is caused by defects in AGXT, a peroxisomal enzyme, leading to accumulation of glyoxylate. Hyperoxaluria type 1 is characterized by an accumulation of oxalate that is thought to lead to precipitates of calcium oxalate in kidneys which can be fatal.

Catalog Number: (10813-936)

Supplier: Prosci

Description: NMDA receptors are members of the ionotropic class of glutamate receptors, which also includes Kainate and AMPA receptors. NMDA receptors consist of NR1 subunits combined with one or more NR2 (A-D) or NR3 (A-B) subunits. The ligand-gated channel is permeable to cations including Ca2+, and at resting membrane potentials NMDA receptors are inactive due to a voltage-dependent blockade of the channel pore by Mg2+. NMDA receptor activation, which requires binding of glutamate and glycine, leads to an influx of Ca2+ into the postsynaptic region where it activates several signaling cascades, including pathways leading to the induction of long-term potentiation (LTP) and depression (LTD). NMDA receptors have a critical role in excitatory synaptic transmission and plasticity in the CNS. They govern a range of physiological conditions including neurological disorders caused by excitotoxic neuronal injury, psychiatric disorders and neuropathic pain syndromes.

Catalog Number: (10068-650)

Supplier: Prosci

Description: NMDA receptors are members of the ionotropic class of glutamate receptors, which also includes Kainate and AMPA receptors. NMDA receptors consist of NR1 subunits combined with one or more NR2 (A-D) or NR3 (A-B) subunits. The ligand-gated channel is permeable to cations including Ca2+, and at resting membrane potentials NMDA receptors are inactive due to a voltage-dependent blockade of the channel pore by Mg2+. NMDA receptor activation, which requires binding of glutamate and glycine, leads to an influx of Ca2+ into the postsynaptic region where it activates several signaling cascades, including pathways leading to the induction of long-term potentiation (LTP) and depression (LTD). NMDA receptors have a critical role in excitatory synaptic transmission and plasticity in the CNS. They govern a range of physiological conditions including neurological disorders caused by excitotoxic neuronal injury, psychiatric disorders and neuropathic pain syndromes.

Catalog Number: (10813-862)

Supplier: Prosci

Description: NMDA receptors are members of the ionotropic class of glutamate receptors, which also includes Kainate and AMPA receptors. NMDA receptors consist of NR1 subunits combined with one or more NR2 (A-D) or NR3 (A-B) subunits. The ligand-gated channel is permeable to cations including Ca2+, and at resting membrane potentials NMDA receptors are inactive due to a voltage-dependent blockade of the channel pore by Mg2+. NMDA receptor activation, which requires binding of glutamate and glycine, leads to an influx of Ca2+ into the postsynaptic region where it activates several signaling cascades, including pathways leading to the induction of long-term potentiation (LTP) and depression (LTD). NMDA receptors have a critical role in excitatory synaptic transmission and plasticity in the CNS. They govern a range of physiological conditions including neurological disorders caused by excitotoxic neuronal injury, psychiatric disorders and neuropathic pain syndromes.

Supplier: Anaspec Inc

Description: This is fluorescent GLP-1 labeled at the peptide C-terminus with FAM, Abs/Em=494/521 nm. In response to Glucose ingestion, proglucagon in the intestinal L cells is cleaved into GLP-1 (1-36). Prior to secretion into the circulation, GLP-1 (1-36) is further processed into amidated GLP-1 (7-36)-and small amounts of glycine-extended GLP-1 (7-37). Both GLP-1 (7-36) and GLP-1 (7-37), causes glucose dependent release of insulin by pancreatic beta-cells. They also play a role in gastric motility (gastric emptying), on the suppression of plasma glucagon levels (glucose production) and possibly on the promotion of satiety and stimulation of glucose disposal in peripheral tissues independent of the actions of insulin. GLP-1 peptides such as GLP-1 (1-36) have been used to investigate restoration of pancreatic beta cell function. GLP-1 is also produced in the central nervous system.
Sequence: FAM-HDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGR-NH2
MW: 4469.8 Da
% Peak area by HPLC: 95
Storage condition: -20° C

Catalog Number: (10085-978)

Supplier: Proteintech

Description: The FXYD family is a group of small single-span transmembrane proteins characterized by a signature sequence containing an FXYD motif, two conserved glycines and a serine residue. Members of the FXYD family, including FXYD1 (phospholemman), FXYD2 (gamma subunit of Na,K-ATPase), FXYD3 (Mat8), FXYD4 (CHIF), FXYD5 (RIC), FXYD6 (phosphohippolin) and FXYD7, are tissue specific regulators of the Na,K-ATPase. FXYD6 is primarily expressed in the brain. It modulates the kinetic activity of Na,K-ATPase and has long-term physiological importance in maintaining cation homeostasis. It may play a role in endolymph composition, and has a potential important role in neuronal excitability of the CNS during postnatal development and in the adult brain. On the SDS-PAGE FXYD6 migrates with an apparent molecular weight of approximately 20 kDa, which is larger than the calculated molecular weight of 10.5 kDa . The gene encodes FXYD6 is located on chromosome 11q23.3, and it might be a susceptibility gene of schizophrenia.

Catalog Number: (76120-928)

Supplier: Bioss

Description: The formation of the spliceosome includes the assembly of Sm proteins in an ordered manner onto snRNAs. This process is mediated by the survival of motor neuron (SMN) protein, and is enhanced by modification of specific arginine residues in the Sm proteins to symmetrical dimethylarginines (sDMAs). sDMA modification of Sm proteins is catalyzed by the methylosome, a complex comprised of the type II methyltransferase PRMT5 (also designated Jak-binding protein 1, JBP1), pICln, and two novel factors. PRMT5 binds the Sm proteins via their arginine- and glycine-rich (RG) domains, while pICln binds the Sm domains. pICln also acts as an inhibitor of SnRNP assembly by preventing specific interactions between Sm proteins required for the formation of the Sm core. pICln is a highly conserved, ubiquitously expressed protein that localizes primarily to the cytoplasm, and may play a role as a swelling-activated anion channel or a channel regulator in addition to its function in the methylosome. The gene encoding human pICln maps to chromosome 11q14.1.