biological source
bacterial (Arthrobacter ureafaciens)
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
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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.
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.
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
Biochem/physiol Actions
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.
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.
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Warning
hcodes
Hazard Classifications
Skin Sens. 1
wgk
nwg
flash_point_f
does not flash
flash_point_c
does not flash
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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)
Chao Gao et al.
bioRxiv : the preprint server for biology (2020-08-09)
The spike (S) glycoprotein in the envelope of SARS-CoV-2 is densely glycosylated but the functions of its glycosylation are unknown. Here we demonstrate that S is recognized in a glycan-dependent manner by multiple innate immune receptors including the mannose receptor
Yizhi Jiang et al.
Cell death and differentiation, 28(11), 3009-3021 (2021-05-17)
The liver has recently been identified as a major organ for destruction of desialylated platelets. However, the underlying mechanism remains unclear. Kupffer cells, which are professional phagocytic cells in the liver, comprise the largest population of resident tissue macrophages in
Jiaqi Wu et al.
BioTechniques, 68(2), 85-90 (2020-01-16)
Carbohydrate-deficient transferrin (CDT) is a reliable biomarker for chronic alcohol abuse. We developed a method for CDT analysis by capillary isoelectric focusing, followed by immunodetection directly in the capillary, in an automated fashion and on a single platform (Peggy Sue™;
Sialylation by ??galactoside ??2,6?sialyltransferase and N?glycans regulate cell adhesion and invasion in human anaplastic large cell lymphoma
Suzuki O, et al.
International Journal of Oncology, 46(3), 973-980 (2015)
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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