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N3786

Sigma-Aldrich

α(2→3,6,8,9) Neuraminidase from Arthrobacter ureafaciens

Proteomics Grade, suitable for MALDI-TOF MS

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Synonym(s):
Neuraminidase from Arthrobacter ureafaciens, Acyl-neuraminyl Hydrolase, Sialidase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.32

form

lyophilized powder

Quality Level

quality

Proteomics Grade

specific activity

≥25 U/vial

suitability

suitable for MALDI-TOF MS

storage temp.

2-8°C

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Application

Neuraminidase is an important deglycosylation enzyme capable of cleaving all non-reducing unbranched N-acetylneuraminic and N-glycolylneuraminic acid residues by hydrolysis of α(2→6), α(2→3), α(2→8), and α(2→9) linkages (affinity in the order given). Branched sialic acids may also be cleaved with the use of high concentrations of enzyme and prolonged incubations. Desialylated glycoproteins may then be further characterized by treatment with various exoglycosidases resulting in partial or complete O-deglycosylation. SDS-PAGE and MALDI-TOF MS are typically utilized in purification, structural analysis, and sequencing process. These techniques also remove heterogeneity and charge from the glycoprotein.

Packaging

Provided with 5× concentrate reaction buffer.

Quality

The buffer solution has been specifically formulated to assure maximum enzyme stability and assay sensitivity.

Unit Definition

One unit will release 1 nmole of 4-methylumbelliferone from 2-(4-methylumbelliferyl) α-D-N-acetylneuraminic acid per minute at pH 5.5 at 37° C.

Physical form

Lyophilized powder

Kit Components Also Available Separately

Product No.
Description
SDS

  • N3536Neuraminidase 5X Reaction Buffer 1.5 mLSDS

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Product No.
Description
Pricing

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Hongyun Li et al.
PloS one, 11(2), e0148238-e0148238 (2016-02-02)
Recent studies have shown that cerebral apoD levels increase with age and in Alzheimer's disease (AD). In addition, loss of cerebral apoD in the mouse increases sensitivity to lipid peroxidation and accelerates AD pathology. Very little data are available, however
Natallia Makarava et al.
Acta neuropathologica communications, 6(1), 92-92 (2018-09-14)
Last decade witnessed an enormous progress in generating authentic infectious prions or PrPSc in vitro using recombinant prion protein (rPrP). Previous work established that rPrP that lacks posttranslational modification is able to support replication of highly infectious PrPSc with assistance
Raiees Andrabi et al.
Immunity, 47(3), 524-537 (2017-09-17)
Apex broadly neutralizing HIV antibodies (bnAbs) recognize glycans and protein surface close to the 3-fold axis of the envelope (Env) trimer and are among the most potent and broad Abs described. The evolution of apex bnAbs from one donor (CAP256)
Ramaiah Arunachalam et al.
Interdisciplinary sciences, computational life sciences, 4(4), 282-290 (2013-01-29)
The aim of the present investigation was to discover the genetic relationships of 2009 pandemic novel influenza A/H1N1 virus (NIV) external antigens Hemagglutinin (HA) and Neuraminidase (NA) with other influenza viruses by performing phylogenetic, comparative and statistical analyses. Phylogenetic trees
Johan Nordholm et al.
The Journal of biological chemistry, 288(15), 10652-10660 (2013-03-01)
Interactions that facilitate transmembrane domain (TMD) dimerization have been identified mainly using synthetic TMDs. Here, we investigated how inherent properties within natural TMDs modulate their interaction strength by exploiting the sequence variation in the nine neuraminidase subtypes (N1-N9) and the

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