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7-Amino-4-methyl-3-coumarinylacetic acid

$280

  • Brand : BIOFRON

  • Catalogue Number : BN-O1448

  • Specification : 98%(HPLC)

  • CAS number : 106562-32-7

  • Formula : C12H11NO4

  • Molecular Weight : 233.22

  • PUBCHEM ID : 129367

  • Volume : 50mg

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Catalogue Number

BN-O1448

Analysis Method

Specification

98%(HPLC)

Storage

-20℃

Molecular Weight

233.22

Appearance

Cryst.

Botanical Source

This product is isolated and purified from the herbs of Guazuma ulmifolia

Structure Type

Category

SMILES

CC1=C(C(=O)OC2=C1C=CC(=C2)N)CC(=O)O

Synonyms

AMCA-H/2H-1-Benzopyran-3-acetic acid,AMCA-H,Aminomethyl coumarin acetic acid/7-amino-4-methylcoumarine-3-acetic acid/7-amino-4-methylcumarin-3-acetic acid/2H-1-Benzopyran-3-acetic acid AMCA-H Aminomethyl coumarin acetic acid/7-Amino-4-methyl-3-coumarinylacetic acid/7-Amino-4-methylcoumarin-3-acetic Acid/2-(7-Amino-4-methyl-2-oxo-2H-chromen-3-yl)acetic acid/2H-1-Benzopyran-3-aceticacid,7-amino-4-methyl-2-oxo/AMCA-H [7-Amino-4-methyl-3-coumarinylacetic acid ]

IUPAC Name

Density

1.391g/cm3

Solubility

Flash Point

263.6ºC

Boiling Point

512.2ºC at 760mmHg

Melting Point

InChl

InChl Key

QEQDLKUMPUDNPG-UHFFFAOYSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:106562-32-7) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

21095569

Abstract

Huntington’s Disease (HD) is characterized by a mutation in the huntingtin (Htt) gene encoding an expansion of glutamine repeats on the N terminus of the Htt protein. Numerous studies have identified Htt proteolysis as a critical pathological event in HD postmortem human tissue and mouse HD models, and proteases known as caspases have emerged as attractive HD therapeutic targets. We report the use of the substrate activity screening method against caspase-3 and -6 to identify three novel, pan-caspase inhibitors that block proteolysis of Htt at caspase-3 and -6 cleavage sites. In HD models these irreversible inhibitors suppressed Hdh(111Q/111Q)-mediated toxicity and rescued rat striatal and cortical neurons from cell death. In this study, the identified nonpeptidic caspase inhibitors were used to confirm the role of caspase-mediated Htt proteolysis in HD. These results further implicate caspases as promising targets for HD therapeutic development.

Copyright © 2010 Elsevier Ltd. All rights reserved

Title

Identification and evaluation of small molecule pan-caspase inhibitors in Huntington's disease models.

Author

Leyva MJ, Degiacomo F, Kaltenbach LS, Holcomb J, Zhang N, Gafni J, Park H, Lo DC, Salvesen GS, Ellerby LM, Ellman JA.

Publish date

2010 Nov 24;

PMID

17406604

Abstract

Substrate activity screening (SAS) is a fragment-based method for the rapid development of novel substrates and their conversion into non-peptidic inhibitors of Cys and Ser proteases. The method consists of three steps: (i) a library of N-acyl aminocoumarins with diverse, low-molecular-weight N-acyl groups is screened to identify protease substrates using a simple fluorescence-based assay; (ii) the identified N-acyl aminocoumarin substrates are optimized by rapid analog synthesis and evaluation; and (iii) the optimized substrates are converted into inhibitors by direct replacement of the aminocoumarin with known mechanism-based pharmacophores. This protocol describes a general procedure for the solid-phase synthesis of a library of N-acyl aminocoumarin substrates and the screening procedure to identify weak binding substrates.

Title

Substrate activity screening (SAS): a general procedure for the preparation and screening of a fragment-based non-peptidic protease substrate library for inhibitor discovery.

Author

Patterson AW1, Wood WJ, Ellman JA.

Publish date

2007;

PMID

11371187

Abstract

In solution, the TATA box binding protein from S. cerevisiae (yTBP) is only minimally oriented when bound to the adenovirus major late promoter (AdMLP) and the yeast CYC1 promoter. At equilibrium, approximately 60% of the complexes are assembled in the orientation observed within crystal structures; 40% are assembled in the opposite orientation. Here we use stopped-flow fluorescence resonance energy transfer (FRET) to study the association kinetics of the two TBP.TATA box orientational isomers. Kinetics were determined by monitoring FRET between a unique tryptophan residue engineered into either the C- or the N-terminal stirrup of the conserved C-terminal subunit of yeast TBP (yTBPc) and an aminocoumarin moiety appended either upstream or downstream of the TATA box. Together, these constructs permitted a simultaneous yet independent monitor of the kinetics of TBP binding in both orientations. Not only did our results provide an independent confirmation of the free energy difference between the two orientational isomers, but they also showed that the orientational binding preference at equilibrium is a result of a faster association rate when TBP binds DNA in the orientation observed in the crystal structure.

Title

Kinetic preference for oriented DNA binding by the yeast TATA-binding protein TBP.

Author

Liu Y1, Schepartz A.

Publish date

2001 May 29;


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