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A2264

β-N-Acetylglucosaminidase from Canavalia ensiformis (Jack bean)

ammonium sulfate suspension, ≥8 units/mg protein

Synonyme(s) :

β-N-Acetyl-D-hexosaminide N-acetylhexosaminohydrolase, β-N-Acetylhexosaminidase

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-730-2
MDL number:
Numéro CE :
Specific activity:
≥8 units/mg protein
Biological source:
Canavalia ensiformis
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biological source

Canavalia ensiformis

Quality Level

form

ammonium sulfate suspension

specific activity

≥8 units/mg protein

foreign activity

α- and β-galactosidase, and α-L-fucosidase ≤0.1%, α-mannosidase ≤0.5%

storage temp.

2-8°C

Application

β -N-acetylglucosaminidase is a lysosomal enzyme used to hydrolyze N-acetyl-β-D-glucosaminides and N-acetyl-β-Dgalactosaminides. It is used in chemoenzymatic synthesis of oligosaccharides based on their effective transglycosylation of β-GlcNAc and β-GalNAcc. It may be a useful tool to study Alzheimer′s Disease [1]. Acetylglucosaminidase from Canavalia ensiformis has been used to study enzymic detachment of biofilms [2].

Biochem/physiol Actions

This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates.
This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors.

Physical form

Suspension in 2.5 M (NH4)2SO4, pH 7.0

Analysis Note

At pH 4.0, p-nitrophenyl β-N-acetylgalactosaminide is hydrolyzed at approximately 50% of the rate of hydrolysis of p-nitrophenyl β-N-acetylglucosaminide at pH 5.0.

Other Notes

One unit will hydrolyze 1.0 μmole of p-nitrophenyl N-acetyl-β-D-glucosaminide to p-nitrophenol and N-acetyl-D-glucosamine per min at pH 5.0 at 25 °C.

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Cet article
M7257G4142M9400
biological source

Canavalia ensiformis

biological source

Canavalia ensiformis

biological source

bovine

biological source

-

specific activity

≥8 units/mg protein

specific activity

≥15 units/mg protein (biuret)

specific activity

1.0-3.0 units/mg protein (modified Warburg-Christian)

specific activity

-

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

ammonium sulfate suspension

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

foreign activity

α- and β-galactosidase, and α-L-fucosidase ≤0.1%, α-mannosidase ≤0.5%

foreign activity

β-galactosidase, β-N-acetylglucosaminidase, α-galactosidase and α-L-fucosidase <0.05%

foreign activity

α- and β-glucosidase ≤0.2%, α-fucosidase ≤0.2%, α-galactosidase ≤0.2%, α-mannosidase ≤0.2%, β-N-acetylglucosaminidase ≤1.0%

foreign activity

β-N-acetylglucosaminidase and α-mannosidase <1.0%

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200


flash_point_f

Not applicable

flash_point_c

Not applicable

Classe de stockage

10 - Combustible liquids



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Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions


Mohammed A Al-Fattani et al.
Journal of medical microbiology, 55(Pt 8), 999-1008 (2006-07-20)
Matrix material was extracted from biofilms of Candida albicans and Candida tropicalis and analysed chemically. Both preparations contained carbohydrate, protein, hexosamine, phosphorus and uronic acid. However, the major component in C. albicans matrix was glucose (32%), whereas in C. tropicalis
T Berger et al.
Journal of reproduction and fertility, 86(2), 559-565 (1989-07-01)
An assay to determine the binding of pig spermatozoa to the zona pellucida (ZP) of pig oocytes was developed using conditions compatible with in-vitro fertilization of pig eggs and with pig sperm penetration of zona-free hamster ova. These conditions were
Chaeyoung Kim et al.
Neurobiology of aging, 34(1), 275-285 (2012-04-17)
Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD). It is unknown, however, how these two processes are related in AD. Here we examined the relationship between O-GlcNAcylation, which is



Numéro d'article de commerce international

RéférenceGTIN
A2264-25UN04061832841311
A2264-10UN04061832841304
A2264-1VL04061837145964
A2264-5UN04061833349953

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