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10269611001

Roche

Neuraminidase (Sialidase)

from Arthrobacter ureafaciens

Synonym(s):

PCR, taq

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204

biological source

bacterial (Arthrobacter ureafaciens)

Quality Level

form

solution

specific activity

~25 units/mg protein

packaging

pkg of 1 U (100 μl)

manufacturer/tradename

Roche

optimum pH

5.0-5.5

storage temp.

2-8°C

General description

Neuraminidase 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.

Specificity

Cleaves terminal sialic-acid residues that are α2,3-, α2,6-, or α2,8-linked to Gal, GlcNAc, GalNAc, AcNeu, GlcNeu, oligosaccharides, glycolipids, or glycoproteins. Relative rate of cleavage is α2,6 >α2,3 >α2,8, determined on bonds in tri- and tetrasaccharides.

Application

  • cell surface lectin array analysis.
  • hemagglutination assays.
  • cell adhesion assay.
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.
Neuraminidase has been used for the:
  • detection of the cell surface glycosylations in human anaplastic large cell lymphoma cells
  • release of sialic acid from cells
  • antibody-overlay lectin microarray

Physical properties

This product is a mixture of isoenzymes (L, M1, M2 and S) with the following molecular weight values: ~ 52 kDa, 66 kDa and 88 kDa.

Physical form

Solution in 10 mM sodium phosphate, 0.1% Micr-O-Protect (w/v), 0.25 mg/ml bovine serum albumin, pH 7

Preparation Note

Working concentration: Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.

Other Notes

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

Pictograms

Exclamation mark

Signal Word

Warning

Hazard Statements

Hazard Classifications

Skin Sens. 1

WGK

nwg

Flash Point(F)

does not flash

Flash Point(C)

does not flash


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Charting the Proteoform Landscape of Serum Proteins in Individual Donors by High-Resolution Native Mass Spectrometry.
Cramer, et al.
Analytical Chemistry, 94, 12732-12741 (2022)
Tomonori Kaifu et al.
The Journal of experimental medicine, 218(12) (2021-11-25)
Dendritic cell immunoreceptor (DCIR) is a C-type lectin receptor with a carbohydrate recognition domain and an immunoreceptor tyrosine-based inhibitory motif. Previously, we showed that Dcir-/- mice spontaneously develop autoimmune enthesitis and sialadenitis, and also develop metabolic bone abnormalities. However, the
Cellular entry of the porcine epidemic diarrhea virus
Li W, et al.
Virus Research, 226, 117-127 (2016)
Sialylation and glycosylation modulate cell adhesion and invasion to extracellular matrix in human malignant lymphoma: Dependency on integrin and the Rho GTPase family
Suzuki O, et al.
International Journal of Oncology, 47(6), 2091-2099 (2015)
Hiroaki Tateno et al.
Stem cells translational medicine, 2(4), 265-273 (2013-03-26)
In comprehensive glycome analysis with a high-density lectin microarray, we have previously shown that the recombinant N-terminal domain of the lectin BC2L-C from Burkholderia cenocepacia (rBC2LCN) binds exclusively to undifferentiated human induced pluripotent stem (iPS) cells and embryonic stem (ES)

Protocols

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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