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Merck

A1057

Sigma-Aldrich

L-Asparaginsäure-β-(7-amido-4-methylcumarin)

≥98%, suitable for ligand binding assays

Synonym(e):

L-Asparaginsäure-β-(4-methyl-7-cumarinylamid), L-Asparaginsäure-4-(4-methyl-7-cumarinylamid)

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About This Item

Empirische Formel (Hill-System):
C14H14N2O5
CAS-Nummer:
Molekulargewicht:
290.27
MDL-Nummer:
UNSPSC-Code:
12352209
PubChem Substanz-ID:
NACRES:
NA.26

Produktbezeichnung

L-Asparaginsäure-β-(7-amido-4-methylcumarin), fluorescent amino acid

Qualitätsniveau

Assay

≥98%

Form

powder

Methode(n)

ligand binding assay: suitable

Farbe

white to off-white

Lagertemp.

−20°C

SMILES String

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

InChI

1S/C14H14N2O5/c1-7-4-13(18)21-11-5-8(2-3-9(7)11)16-12(17)6-10(15)14(19)20/h2-5,10H,6,15H2,1H3,(H,16,17)(H,19,20)/t10-/m0/s1

InChIKey

ARZPQBJTLVVDNP-JTQLQIEISA-N

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Biochem./physiol. Wirkung

L-Aspartic acid β-(7-amido-4-methylcoumarin) is used as a fluorogenic substrate for studying the specificity and kinetics of lysosomal glycoasparaginase(s) (aspartylglucosaminidase) and L-asparaginase(s).
L-Aspartic acid-β-7-amido-4-methylcoumarin is sensitive and specific fluorogenic substrate used to assay for lysosomal glycoasparaginase (aspartylglucosaminidase) activity and the diagnosis of aspartylglucosaminuria.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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Voznyi YaV et al.
Journal of inherited metabolic disease, 16(6), 929-934 (1993-01-01)
L-Aspartic acid-beta-7-amido-4-methylcoumarin is a sensitive and specific fluorogenic substrate for lysosomal glycoasparaginase (aspartylglucosaminidase). Fibroblasts and leukocytes from 8 patients with aspartylglucosaminuria, showed 1-7% of the mean normal glycoasparaginase activity. Heterozygotes showed intermediate activities. Glycoasparaginase activity in chorionic villi, cultured trophoblasts
P Ylikangas et al.
Analytical biochemistry, 280(1), 42-45 (2000-05-11)
The antineoplastic enzyme L-asparaginase is commonly used for the induction of remission in acute lymphoblastic leukemia (ALL). There is no simple method available for measuring the activity of this highly toxic drug. We incubated L-asparaginase from Erwinia chrysanthemi with L-aspartic
I Mononen et al.
Clinical chemistry, 40(3), 385-388 (1994-03-01)
Serum, plasma, and lymphocytes from aspartylglycosaminuria (AGU) patients and carriers and from normal controls were incubated with a fluorescent glycosylasparaginase substrate, L-aspartic acid beta-(7-amido-4-methylcoumarin), and the release of 7-amino-4-methylcoumarin was measured fluorometrically after incubation for 1-4 h. The mean glycosylasparaginase
I T Mononen et al.
Analytical biochemistry, 208(2), 372-374 (1993-02-01)
Recent experimental work on the mechanism of action of glycosylasparaginase suggests that the enzyme specifically reacts toward the L-asparagine or L-aspartic acid moiety of its substrates. Based on this, a new sensitive assay for glycosylasparaginase activity has been developed using
Seiji Saito et al.
Biochemical and biophysical research communications, 377(4), 1168-1172 (2008-11-11)
To elucidate the basis of aspartylglucosaminuria (AGU) from the viewpoint of enzyme structure, we constructed structural models of mutant aspartylglucosaminidase (AGA) proteins using molecular modeling software, TINKER. We classified the amino acid substitutions responsible for AGU and divided them into

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