57462-42-7

Basic information

• Product Name: ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2
• Synonyms: [NLE11]-SUBSTANCE P;ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2;H-ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2;substance P, NleNH2(11)-;Substance P, [Nle11];[Nle11]-Substance P;(Nle-NH211)-Substance P;[Norleucinamide11]substance P
• CAS NO: 57462-42-7
• Molecular Formula: C64H100N18O13
• Molecular Weight: 1329.59
• Product Categories: Peptide
• Mol File: 57462-42-7.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: −20°C
• CAS DataBase Reference: ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2(57462-42-7)
• EPA Substance Registry System: ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2(57462-42-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 57462-42-7(Hazardous Substances Data)

Usage

General Description

The chemical "ARG-PRO-LYS-PRO-GLN-GLN-PHE-PHE-GLY-LEU-NLE-NH2" is a peptide composed of the amino acids arginine, proline, lysine, glutamine, phenylalanine, glycine, leucine, and Nle (norleucine). The sequence of these amino acids forms a specific molecular structure with potential biological functions. This peptide may have applications in biochemistry, pharmaceuticals, and biotechnology, and its properties and activities may be studied for potential therapeutic use.

Upstream product

• 4530-20-5 BOC-glycine 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 6404-28-0 Boc-Nle-OH 

Relevant articles and documents

Synthesis of peptides by the solid-phase method. 7. Substance P and analogues

Substance P and 21 related peptides containing isosteric or isofunctional groups were prepared by the solid-phase method. After purification by gel filtration and ion-exchange chromatography, the compounds were characterized by thin-layer chromatography, paper electrophoresis, and amino acid and elemental analysis. The biological activities of the peptides were evaluated in vitro on the guinea pig ileum, the rabbit mesenteric vein, and the dog common carotid artery and in vivo on the rat blood pressure. It is shown that the replacement of some residues in the undecapeptide substance P causes variable losses of apparent affinity with a little or no change in the intrinsic activity. All the analogues used in the present study were found to be inactive as antagonists.