55508-42-4

Basic information

• Product Name: NEUROTENSIN
• Synonyms: 5-Oxo-L-Pro-L-Leu-L-Tyr-L-Glu-L-Asn-L-Lys-L-Pro-L-Arg-L-Arg-L-Pro-L-Tyr-L-Ile-L-Leu-OH;Neurotensin【ox】;Neurotensin【rat】;C01836;GLP-LEU-TYR-GLU-ASN-LYS-PRO-ARG-ARG-PRO-TYR-ILE-LEU;NEUROTENSIN;NEUROTENSIN (1-13);NEUROTENSIN (HUMAN, BOVINE, CANINE)
• CAS NO: 55508-42-4
• Molecular Formula: C₇₈H₁₂₁N₂₁O₂₀
• Molecular Weight: 1672.92
• Product Categories: Peptide
• Mol File: 55508-42-4.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• Density: 1.46±0.1 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 3.41±0.10(Predicted)
• CAS DataBase Reference: NEUROTENSIN(CAS DataBase Reference)
• NIST Chemistry Reference: NEUROTENSIN(55508-42-4)
• EPA Substance Registry System: NEUROTENSIN(55508-42-4)

Safety Data

• Hazardous Substances Data: 55508-42-4(Hazardous Substances Data)

Usage

Description

Neurotensin is a 13-amino-acid peptide that was initially isolated from the bovine hypothalamus and has since been identified in the intestinal tract, particularly in the ileal mucosa, which contains 90% of the body's total neurotensin. This peptide is known to act as a releasing factor for several adenohypophyseal hormones and exhibits various physiological effects, such as vasodilation, increased vascular permeability, and increased gastrin secretion. Additionally, it has the ability to decrease the secretion of gastric acid and secretin.

Uses

Used in Pharmaceutical Applications:
Neurotensin is used as a therapeutic agent for its potential role in modulating various physiological processes. Its effects on vasodilation, vascular permeability, and hormone release make it a promising candidate for the development of drugs targeting cardiovascular, gastrointestinal, and endocrine systems.
Used in Research and Development:
Neurotensin serves as an important subject of study in the field of neuroscience and endocrinology. Researchers utilize neurotensin to better understand the complex interactions between the nervous and endocrine systems, as well as its potential role in various physiological and pathological processes.
Used in Diagnostic Applications:
Due to its involvement in the release of adenohypophyseal hormones and its effects on the gastrointestinal system, neurotensin can be used as a biomarker in the diagnosis of certain endocrine and gastrointestinal disorders. Measuring neurotensin levels in patients may help in the identification and monitoring of these conditions.
Used in Drug Delivery Systems:
Similar to gallotannin, neurotenin can also be incorporated into drug delivery systems to enhance its therapeutic potential and bioavailability. By employing various carriers, such as organic and metallic nanoparticles, the delivery, efficacy, and targeting of neurotensin to specific tissues or cells can be improved, leading to better treatment outcomes for related conditions.

Upstream product

• 35661-60-0 Fmoc-Leu-OH 
• 71989-31-6 Fmoc-Pro-OH 
• 71989-18-9 Fmoc-Glu(OtBu)-OH 
• 71989-23-6 Fmoc-Ile-OH 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 132388-59-1 L-Asn(Trt) 
• 98-79-3 L-Pyroglutamic acid 
• 187618-60-6 Nα-(9-fluorenylmethyloxycarbonyl)-Nγ-2,2,4,6,7-pentamethyldihydrobenzofuran-5-sulfonyl-L-arginine 

Relevant articles and documents

Protein Modification at Tyrosine with Iminoxyl Radicals

Post-translational modifications (PTMs) of proteins are a biological mechanism for reversibly controlling protein function. Synthetic protein modifications (SPMs) at specific canonical amino acids can mimic PTMs. However, reversible SPMs at hydrophobic amino acid residues in proteins are especially limited. Here, we report a tyrosine (Tyr)-selective SPM utilizing persistent iminoxyl radicals, which are readily generated from sterically hindered oximes via single-electron oxidation. The reactivity of iminoxyl radicals with Tyr was dependent on the steric and electronic demands of oximes; isopropyl methyl piperidinium oxime 1f formed stable adducts, whereas the reaction of tert-butyl methyl piperidinium oxime 1o was reversible. The difference in reversibility between 1f and 1o, differentiated only by one methyl group, is due to the stability of iminoxyl radicals, which is partly dictated by the bond dissociation energy of oxime O-H groups. The Tyr-selective modifications with 1f and 1o proceeded under physiologically relevant, mild conditions. Specifically, the stable Tyr-modification with 1f introduced functional small molecules, including an azobenzene photoswitch, to proteins. Moreover, masking critical Tyr residues by SPM with 1o, and subsequent deconjugation triggered by the treatment with a thiol, enabled on-demand control of protein functions. We applied this reversible Tyr modification with 1o to alter an enzymatic activity and the binding affinity of a monoclonal antibody with an antigen upon modification/deconjugation. The on-demand ON/OFF switch of protein functions through Tyr-selective and reversible covalent-bond formation will provide unique opportunities in biological research and therapeutics.

NOVEL CROSS-LINKERS FOR OBTAINING STRUCTURE INFORMATION ON MOLECULE COMPLEXES

The present invention describes a novel cross-linker, a method for preparing one or more cross-linked biomolecules, biomolecular complexes of two or more biomolecules, a method for preparing cross-linked fragments from such cross-linked biomolecules and/or biomolecular complexes, a method for cleavage and reduction of such cross-linked biomolecules and/or biomolecular complexes, a method for identifying cross-links in such cross-linked biomolecules and/or biomolecular complexes, as well as a method for determining relative amounts of cross-links in a biomolecule or biomolecular complex in two or more samples.