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Référence Produit: (BOSSBS-12933R-CY5)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (PRSI26-123)
Fournisseur: ProSci Inc.
Description: Myristate, a rare 14-carbon saturated fatty acid, is cotranslationally attached by an amide linkage to the N-terminal glycine residue of cellular and viral proteins with diverse functions. N-myristoyltransferase catalyzes the transfer of myristate from CoA to proteins. N-myristoylation appears to be irreversible and is required for full expression of the biologic activities of several N-myristoylated proteins, including the alpha subunit of the signal-transducing guanine nucleotide-binding protein (G protein) GO (GNAO1).
UOM: 1 * 50 µG


Référence Produit: (BOSSBS-12933R-A750)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyse other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesised in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-HRP)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-FITC)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (PRSI91-169)
Fournisseur: ProSci Inc.
Description: Ubiquitin Carboxyl-Terminal Hydrolases (UCHs) are a family of cysteine hydrolases. They catalyze the hydrolysis of amides, thioesters and esters, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin. Up regulation of UCHL3 is associated with uterine cervical neoplasms. UCHL3 is implicated in age related cognitive disorders. UCHL3 also promotes adipogenesis and insulin signaling. In mice, UCHL3 knockout have been shown to be resistant to diet-induced obesity.
UOM: 1 * 50 µG


Référence Produit: (BOSSBS-12933R)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-A680)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyse other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesised in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-A488)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-A647)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-A555)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-12933R-A350)
Fournisseur: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.
UOM: 1 * 100 µl


Référence Produit: (ENZOBMLFA0180050)
Fournisseur: ENZO LIFE SCIENCES
Description: Endogenous cannabinoid. Weak ligand of CB1 (Ki=23.8µM) and CB2 (Ki=13.9µM) receptor. Inhibits fatty acid amide hydrolase (FAAH) (IC50=5.1µM). Immunosuppressant, anti-inflammatory, anti-nociceptive and anti-convulsant in vivo. The exact mode of action has not yet been revealed. It has been suggested that PEA: i) binds to a yet to be discovered cannabinoid receptor similar to CB2; ii) administered in vivo elicits the synthesis of endogenous agonists of CB2; iii) acts as an "entourage" compound by enhancing the activity and/or by influencing the turnover of endogenous agonists of CB2, possibly but not uniquely, by inhibiting their degradation.
UOM: 1 * 50 mg


Fournisseur: Thermo Fisher Scientific
Description: Thermo Scientific Pierce DSG is a water-insoluble, homo-bifunctional N-hydroxysuccinimide ester (NHS-ester) crosslinker often used for conjugating radiolabeled ligands to cell-surface receptors. The NHS ester is the simplest and most commonly used reactive group for crosslinking and labeling proteins and peptides. NHS esters react with primary amines on the N-termini of peptides and the  amine of lysine residues, forming a stable, covalent amide bond and releasing the NHS group.

Référence Produit: (ENZOBPDABS029011)
Fournisseur: ENZO LIFE SCIENCES
Description: Peptide tyrosine-tyrosine (PYY) amide is a 36 amino-acid. PYY is a member of the pancreatic polypeptide (PP) family of peptides (neuropeptide Y (NPY), PYY and PP). While NPY is localized in neurons (both in the central and peripheral nervous system) and PP in the pancreatic islets, PYY is found in both neurons and the gut. PYY is released in response to food intake from the same endocrine cells (L cells) in the intestinal mucosa as the glucagon-like peptides, and inhibits gall bladder secretion, gut motility and pancreatic secretion. These effects are similar to those of PP and overlap with the gut inhibitory activity of GLP-1.
UOM: 1 * 1 mg


Référence Produit: (PRSI92-419)
Fournisseur: ProSci Inc.
Description: Mouse carboxypeptidase A2(CPA2) is a secreted pancreatic procarboxy -peptidase which belongs to the peptidase M14 family. CPA2 consists of a signal peptide, a pro region and a mature chain. It can be activated after cleavage of the pro peptide. CPA2 cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan.
UOM: 1 * 50 µG


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