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A3010

Sigma-Aldrich

Acylase I aus Schweineniere

Grade I, lyophilized powder, ≥1500 units/mg protein

Synonym(e):

Aminoacylase, N-Acylaminosäure-Amidohydrolase

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100 MG
€ 120,00
500 MG
€ 313,00
1 G
€ 538,00
5 G
€ 2.120,00

€ 120,00

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100 MG
€ 120,00
500 MG
€ 313,00
1 G
€ 538,00
5 G
€ 2.120,00

About This Item

CAS-Nummer:
9012-37-7
EC-Nummer:
3.5.1.14 (BRENDA, IUBMB)
EG-Nummer:
232-732-3
MDL-Nummer:
MFCD00081285
UNSPSC-Code:
12352204
NACRES:
NA.54

€ 120,00

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Typ

Grade I

Qualitätsniveau

200

Form

lyophilized powder

Spezifische Aktivität

≥1500 units/mg protein

Zusammensetzung

Protein, ≥60%

UniProt-Hinterlegungsnummer

P37111

Lagertemp.

−20°C

Angaben zum Gen

pig ... ACY1(396930)

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Anwendung

Acylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues [1]. Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids [2].

Biochem./physiol. Wirkung

Acylase I catalyzes the deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. n-Butylmalonic acid is an inhibitor of acylase I. S-alkyl-N-acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents have been found to be good acylase I substrates .

Einheitendefinition

1 U hydrolysiert 1.0 μmol N-Acetyl-L-methionin pru Stunde bei pH 7.0 und 25 °C.

Hinweis zur Analyse

Proteingehalt mittels Biuret-Reaktion bestimmt.

Piktogramme

Health hazardExclamation mark
GHS08,GHS07

Signalwort

Danger

Gefahreneinstufungen

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Zielorgane

Respiratory system

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)

Hier finden Sie alle aktuellen Versionen:

Analysenzertifikate (COA)

Lot/Batch Number
0000431473
0000431472
0000431471
0000431471
0000431472

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Die Dokumentenbibliothek aufrufen

Y Fukagawa et al.
The Journal of antibiotics, 33(6), 543-549 (1980-06-01)
PS-5 was deacetylated to NS-5 (deacetylated PS-5) by l-amino acid acylase from porcine kidney and D-amino acid acylase from Streptomyces olivaceus but not by l-amino acid acylase from Aspergillus sp. Using PS-5, N-chloroacetyl-l-phenylalanine and N-chloroacetyl-D-valine as substrates, acylase producers were
K Kubo et al.
The Journal of antibiotics, 33(6), 556-565 (1980-06-01)
L-Amino acid acylase and D-amino acid acylase were stable below 50 degrees C, although the D-enzyme was more thermostable than the L-enzyme at higher temperatures. At 30 degrees C they showed the highest reaction velocity in phosphate buffer of pH
Jinit Masania et al.
Oxidative medicine and cellular longevity, 2019, 4851323-4851323 (2019-12-13)
Glycation, oxidation, nitration, and crosslinking of proteins are implicated in the pathogenic mechanisms of type 2 diabetes, cardiovascular disease, and chronic kidney disease. Related modified amino acids formed by proteolysis are excreted in urine. We quantified urinary levels of these
Debby Ngo et al.
JCI insight, 6(5) (2021-02-17)
Recent advances in proteomic technologies have made high-throughput profiling of low-abundance proteins in large epidemiological cohorts increasingly feasible. We investigated whether aptamer-based proteomic profiling could identify biomarkers associated with future development of type 2 diabetes (T2DM) beyond known risk factors.
V Uttamsingh et al.
Chemical research in toxicology, 11(7), 800-809 (1998-07-22)
The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography
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