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A2027

Sigma-Aldrich

L-Arginine-7-amido-4-methylcoumarin hydrochloride

cathepsin H substrate

Synonyme(s) :

Arginine 4-methyl-7-coumarylamide

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About This Item

Formule empirique (notation de Hill):
C16H21N5O3
Numéro CAS:
Poids moléculaire :
331.37
Numéro MDL:
Code UNSPSC :
12352204
ID de substance PubChem :
Nomenclature NACRES :
NA.83

Pureté

≥97% (TLC)

Forme

powder

Solubilité

acetic acid: water (1:1): 50 mg/mL, clear, colorless to light yellow

Température de stockage

−20°C

Chaîne SMILES 

Cl.CC1=CC(=O)Oc2cc(NC(=O)[C@@H](N)CCCNC(N)=N)ccc12

InChI

1S/C16H21N5O3.ClH/c1-9-7-14(22)24-13-8-10(4-5-11(9)13)21-15(23)12(17)3-2-6-20-16(18)19;/h4-5,7-8,12H,2-3,6,17H2,1H3,(H,21,23)(H4,18,19,20);1H/t12-;/m0./s1

Clé InChI

PFLMUQNBZRXRHD-YDALLXLXSA-N

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Application

L-Arginine-7-amido-4-methylcoumarin hydrochloride has been used as a substrate for cathepsin H from rat muscle homogenate and sarcoplasmic extract. It has also been used as a substrate for arginine amino-peptidase from Daphnia homogenates and recombinant aminopeptidase from Toxoplasma gondii.

Actions biochimiques/physiologiques

L-Arginine-7-amido-4-methylcoumarin hydrochloride is a protease substrate. It is a specific substrate for cathepsin H and not for cathepsin L and B.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


Certificats d'analyse (COA)

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Cathepsin L-like enzyme was purified from the body wall of the sea cucumber Stichopus japonicus by an integral method involving ammonium sulfate precipitation and a series of column chromatographies on DEAE Sepharose CL-6B, Sephadex G-75, and TSK-GEL. The molecular mass
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Toxoplasmosis is a parasitic disease caused by infection with Toxoplasma gondii that currently has few therapeutic options. The M1 aminopeptidase enzymes have been shown to be attractive targets for anti-parasitic agents and/or vaccine candidates, suggesting potential to re-purpose inhibitors between
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Several genetic lineages of obligate parthenogenetic Daphnia pulex, a common zooplankton species, have invaded Japan from North America. Among these, a lineage named JPN1 is thought to have started colonization as a single genotype several hundred to thousand years ago

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