Welcome to LookChem.com Sign In|Join Free

CAS

  • or

5241-71-4

Post Buying Request

5241-71-4 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

5241-71-4 Usage

General Description

H-ASP-PHE-NH2, also known as aspartyl-phenylalanine amide, is a neuropeptide that acts as an agonist at neurotensin receptors. It is a synthetic compound derived from the amino acids aspartic acid and phenylalanine. As a neuropeptide, H-ASP-PHE-NH2 has been found to influence a variety of physiological functions including the regulation of the cardiovascular system, pain perception, and locomotor behavior. H-ASP-PHE-NH2 has also been studied for its potential therapeutic applications, particularly in the treatment of conditions such as schizophrenia, Parkinson's disease, and substance abuse. Overall, H-ASP-PHE-NH2 is a biologically active compound with potential implications for the understanding and treatment of various neurological and psychiatric disorders.

Check Digit Verification of cas no

The CAS Registry Mumber 5241-71-4 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 5,2,4 and 1 respectively; the second part has 2 digits, 7 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 5241-71:
(6*5)+(5*2)+(4*4)+(3*1)+(2*7)+(1*1)=74
74 % 10 = 4
So 5241-71-4 is a valid CAS Registry Number.

5241-71-4SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name H-ASP-PHE-NH2

1.2 Other means of identification

Product number -
Other names ASP-PHE AMIDE

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:5241-71-4 SDS

5241-71-4Relevant articles and documents

Method for preparing aspartylcyclohexyla laninamide

-

Page column 6-7, (2008/06/13)

Disclosure is a method for preparing α-aspartyl-β-cyclohexylalaninamide, comprising carrying out a first step of amide formation of an α-aspartyl phenylamine ester of general formula (II) wherein: R is a C1-C4alkyl radical, and then

Protected-mode Synthesis of N-Linked Glycopeptides: Single-step Preparation of Building Blocks as Peracetyl Glycosylated NαFmoc Asparagine OPfp Esters

Christiansen-Brams, Ida,Meldal, Morten,Bock, Klaus

, p. 1461 - 1472 (2007/10/02)

The preparation of Nα-(fluoren-9-ylmethoxycarbonyl)asparagine pentafluorophenyl esters (Nα-Fmoc-Asn-OPfp) glycosylated with per-O-acetylated β-D-glucose, N-acetyl-β-D-glucosamine, β-D-mannose, 4-O-β-D-glucopyranosyl-β-D-glucose (cellobiose), 4-O-β-D-galactopyranosyl-β-D-glucose (lactose) and 4-O-α-D-glucopyranosyl-β-D-glucose (maltose) is described.The per-O-acetylated glycosylamines were treated selectively with the key compound Nα-Fmoc-Asp(Cl)-OPfp 2, to give, in a single step, the glycosylated building blocks.The acid chloride 2 was prepared in a quantitative one-pot reaction from commercially available Nα-Fmoc-Asp(OBut)-OPfp 1.The acid stability of the N-glycosidic linkage was investigated.The building block 7, containing a maltose moiety, was used in the synthesis of a glycosylated D-Ala1 Peptide-T amide analogue 14.CD spectra were recorded in 85 percent TFE.All compounds were fully characterized by (1)H and (13)C NMR spectroscopy.

PAPAIN-CATALYZED FRAGMENT SYNTHESIS OF PROTECTED CHOLECYSTOKININ DERIVATIVES

Cerovsky, Vaclav,Pirkova, Jana,Majer, Pavel,Slaninova, Jirina,Hlavacek, Jan

, p. 1873 - 1882 (2007/10/02)

Sodium salts of methyl esters of N-tert-butyloxycarbonyl-β-tert-butylaspartyl-O4-sulfotyrosine (II) or N-tert-butyloxycarbonyl-O4-sulfotyrosine (III) were condensed with amino components derived from peptide amides IVb-IVe and IVg (simulating the carboxy-terminal part of cholecystokinin) under catalysis with papain.Rates and yields of conversion of these peptides to the corresponding derivatives Ib-If were compared with the results reported previously for analogous papain-catalyzed fragment synthesis of the protected carboxy-terminal octapeptide of cholecystokinin Ia.In the condensation reactions with the individual amino components quantitative changes were observed in the ability of papain to catalyze the peptide bond synthesis which appeared as differences in the maximum yield (and the time required for achieving it) of the condensation reaction, monitored by HLPC.The observed differences are related not only with the distance of the amino acid substitution from the P'1 subsite in the given amino component but also with the side-chain structure of the substituting amino acid.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 5241-71-4