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A9378

Sigma-Aldrich

L-Amino Acid Oxidase from Crotalus adamanteus

Type IV, ≥4.0 units/mg protein, aqueous suspension

Sinônimo(s):

L-AAO, L-Amino acid:oxygen oxidoreductase (deaminating)

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2 MG
R$ 1.753,00
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R$ 3.503,00
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R$ 6.022,00

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2 MG
R$ 1.753,00
5 MG
R$ 3.503,00
10 MG
R$ 6.022,00

About This Item

Número CAS:
Número da licença da enzima:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

R$ 1.753,00


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tipo

Type IV

Formulário

aqueous suspension

atividade específica

≥4.0 units/mg protein

peso molecular

~130 kDa

contém

toluene as preservative

concentração

≥5.0 mg/mL

solubilidade

H2O: soluble 1.0 mg/mL, clear

temperatura de armazenamento

2-8°C

Aplicação

L-amino acid oxidase (LAAO) is used to convert L-amino acids to their corresponding α-keto acids. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays.[1] 35S dimethylsulfoniopropionate (DMSP) has been synthesized chemically from 35S L-methionine using LAAO from Sigma to form 35S 3-methiolpropionate.[2]

Ações bioquímicas/fisiológicas

L-Amino acid oxidase is a flavoprotein with a molecular weight of 130 kDa. It consists of two different subunits of approximately 70,000 Da. Each molecule of holoenzyme has two FAD molecules. It is a glycoprotein containing about 2-5% carbohydrate, including sialic acid. Optimum pH is approximately 7.5.The enzyme may be reversibly inactivated by incubation in phosphate buffer, pH 7.5 at 38 °C. L-amino acid oxidase is involved in various metabolic pathways such as alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis.[3] It occurs in many snake venoms apart from microorganisms and animal tissue, especially in kidney and liver.

Embalagem

Package size based on protein content

Definição da unidade

One Unit oxidizes one micromole of L-leucine per minute at 25 °C, pH 7.6

Nota de preparo

Dissolves in water at 1 mg/mL concentration to form a clear solution.

Pictogramas

Skull and crossbones

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

Acute Tox. 1 Inhalation - Acute Tox. 2 Dermal - Acute Tox. 2 Oral

Código de classe de armazenamento

6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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Stefania Digiovanni et al.
Scientific reports, 10(1), 10135-10135 (2020-06-25)
Reactive Intermediate Deaminase (Rid) protein superfamily includes eight families among which the RidA is conserved in all domains of life. RidA proteins accelerate the deamination of the reactive 2-aminoacrylate (2AA), an enamine produced by some pyridoxal phosphate (PLP)-dependent enzymes. 2AA
Identification and enumeration of bacteria assimilating dimethylsulfoniopropionate (DMSP) in the North Atlantic and Gulf of Mexico
Malmstrom RR, et al.
Limnology and Oceanography, 49(2), 597-606 (2004)
Jiro Arima et al.
The Journal of biological chemistry, 281(9), 5885-5894 (2006-01-13)
Streptomyces griseus leucine aminopeptidase (SGAP), which has two zinc atoms in its active site, is clinically important as a model for understanding the structure and mechanism of action of other metallopeptidases. SGAP is a calcium-activated and calcium-stabilized enzyme, and its
Joseph M Boggs et al.
Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases, 12(5), 1005-1009 (2012-03-15)
Phylogenetic analysis of 10 amino acid sequences from 19 Streptococcus species showed that S. oligofermentans clustered within the mitis group. However, the l-amino acid oxidase (LAAO) of S. oligofermentans showed a different clustering pattern from the other proteins analyzed implicating
Hong-Sen Chen et al.
Biochimie, 94(2), 335-344 (2011-08-02)
To investigate the structure-function relationships and geographic variations of L-amino acid oxidase (LAAO) from Daboia venoms, a single LAAO (designated as DrLAO) was purified from eastern Indian Daboia russelii venom and characterized. The purified DrLAO showed subunit molecular mass of

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