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Merck

10269611001

Roche

Neuraminidase (Sialidase)

from Arthrobacter ureafaciens

Sinónimos:

PCR, taq

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About This Item

Comisión internacional de enzimas:
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

signalword

Warning

hcodes

Hazard Classifications

Skin Sens. 1

wgk_germany

nwg

flash_point_f

does not flash

flash_point_c

does not flash


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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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)
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
Lam Raga Anggara Markely et al.
Biotechnology progress, 32(1), 235-241 (2015-11-21)
The serum half-life, biological activity, and solubility of many recombinant glycoproteins depend on their sialylation. Monitoring glycoprotein sialylation during cell culture manufacturing is, therefore, critical to ensure product efficacy and safety. Here a high-throughput method for semi-quantitative fingerprinting of glycoprotein
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)

Protocolos

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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