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11080725001

Roche

Neuraminidase (Sialidase)

from Vibrio cholerae

Sinonimo/i:

Salidase

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About This Item

Classificazione EC (Enzyme Commission):
Codice UNSPSC:
12352204

158,00 €


Per informazioni sulla disponibilità, contatta il Servizio Clienti.

Origine biologica

Vibrio cholerae

Livello qualitativo

Stato

solution

PM

~95 kDa

Confezionamento

pkg of 1 U

Produttore/marchio commerciale

Roche

pH ottimale

5.5-6.2

Compatibilità

suitable for ELISA applications

applicazioni

life science and biopharma
sample preparation

Condizioni di spedizione

wet ice

Temperatura di conservazione

2-8°C

Categorie correlate

Descrizione generale

Approximately 40 U/mg enzyme protein at 37 °C and pH 5.5, with N-acetyl-neuraminosyl-D-lactose as the substrate.
Neuraminidase is an acylneuraminyl hydrolase which hydrolyzes terminal N- or O-acylneuraminic acids which are α2,3-, α2,6-, or α2,8-linked (rate: α2,6 > α2,3 > α2,8) to oligosaccharides, polysaccharides, mucopolysaccharides, glycoproteins, and glycolipids. Noteworthy, for the hydrolysis of glycolipids, the presence of a detergent is necessary. Because of the broad substrate specificity, the enzyme is very well suited for the complete removal of sialic acids from glycoconjugates of a wide variety of biological materials (e.g., in cytology, on cell surfaces, viruses etc.).[1]

Specificità

Hydrolyzes terminal N- or O-acyl-neuraminic acids that are α2,3-, α2,6-, or α2,8-linked to galactose, Hex, NAc, or N- or O-acylated neuraminyl residues in oligosaccharides/glycoconjugates or colominic acid. Relative rate of cleavage is α2,3 >α2,6 >α2,8, determined on bonds in tri- and tetrasaccharides.

Applicazioni

Neuraminidase has been used:
  • to remove cis-acting sialic acids in CHO (chinese hamster ovary) cells[2]
  • for deglycosylation studies[3]

Definizione di unità

One unit is the enzyme activity that hydrolyzes 1 μmol N-acetyl-neuraminosyl-D-lactose within 1 min at +37 °C under the following incubation conditions:
10 mM N-acetyl-neuraminosyl-D-lactose, 50 mM sodium acetate, 4 mM calcium chloride, bovine serum albumin, 100 μg/ml, pH 5.5. The activity is determined by measuring the released D-lactose using the β-galactosidase/galactose dehydrogenase method. Under the same conditions, 1 μmol N-acetylneuraminic acid per min is split off from human acid α1-glycoprotein (10 mg/ml incubation mixture) by 1 U neuraminidase. Released N-acetyl-neuraminic acid can be determined using, for example, the thiobarbituric acid method.

Stato fisico

Solution in 50 mM sodium acetate, 154 mM sodium chloride, 9 mM calcium chloride, 0.1% Micr-O-Protect (w/v), human serum albumin, 25 mg/l, pH 5.5. The preparation contains 10 mM EDTA.
Note: The serum used for this preparation was tested for HBs antigen and for the presence of antibodies to HIV-1, HIV-2, HCV, and found to be negative, according to the current quality control procedures.

Altre note

For life science research only. Not for use in diagnostic procedures.

Note legali

The sale of the Product does not exhaust or grant any rights in third party patents including patents of companies of the F. Hoffmann - La Roche AG group of companies, in particular, for the use of modified antibodies obtained by using the product.

Pittogrammi

Exclamation mark

Avvertenze

Warning

Indicazioni di pericolo

Classi di pericolo

Skin Sens. 1

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

does not flash

Punto d’infiammabilità (°C)

does not flash


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The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). To investigate the importance of pSn sialic acid-binding activity for PRRSV infection, an R(116)-to-E mutation was introduced in the predicted sialic acid-binding
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Hemagglutinin (HA) on the surface of influenza viruses binds to sialic acids, mainly N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid. Neu5Ac and N-glycolylneuraminic acid lie at the terminal end of sugar chains on the cell surface. Human influenza viruses preferentially bind
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Protocolli

Neuraminidase can be used to cleave sialic acids from proteins. In this protocol, the enzyme from Vibrio cholerae is used on fixed cells.

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