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Merck

N8271

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

recombinant, expressed in E. coli, buffered aqueous solution

Synonym(s):

Neuraminidase from Arthrobacter ureafaciens, Acyl-neuraminyl Hydrolase, Sialidase

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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
MDL number:

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Product Name

α(2→3,6,8,9) Neuraminidase from Arthrobacter ureafaciens, recombinant, expressed in E. coli, buffered aqueous solution

recombinant

expressed in E. coli

form

buffered aqueous solution

specific activity

≥135 units/mg protein

mol wt

88 kDa
95 kDa

foreign activity

β-Galactosidase, α-mannosidase, β-hexosaminidase, α-fucosidase, and proteases, none detected

shipped in

wet ice

storage temp.

2-8°C

Quality Level

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1 of 4

This Item
N3786N7271480716
specific activity

≥135 units/mg protein

specific activity

≥25 U/vial

specific activity

-

specific activity

≥40 units/mg protein, ≥5 units/mL

form

buffered aqueous solution

form

lyophilized powder

form

buffered aqueous solution

form

liquid

recombinant

expressed in E. coli

recombinant

-

recombinant

-

recombinant

expressed in E. coli

shipped in

wet ice

shipped in

-

shipped in

wet ice

shipped in

wet ice

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

mol wt

88 kDa, 95 kDa

mol wt

-

mol wt

-

mol wt

-

Biochem/physiol Actions

Releases α(2→3), α(2→6), α(2→8), and α(2→9)-linked N-acetylneuraminic acid from complex oligosaccharides.

Other Notes

One unit will hydrolyze 1 μmole of 4-methylumbelliferyl α-D-N-acetylneuraminide per min at pH 5.0 at 37 °C.

Packaging

Provided with 5× reaction buffer (250 mM sodium phosphate, pH 6.0).

Physical form

Solution in 20 mM Tris-HCl, pH 7.5, and 20 mM NaCl.

Preparation Note

Expressed in glycosidase-free hosts.

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
Audu J Natala et al.
Journal of medical entomology, 50(1), 85-93 (2013-02-23)
Amblyomma variegatum F. are obligate hematophagous ectoparasites of livestock that serve as the vectors of Ehrlichia ruminantium (formerly known as Cowdria ruminantium), the causative agent of heartwater disease. In the light of the fact that they are blood-feeding, their salivary
Dominic Meusch et al.
Nature, 508(7494), 61-65 (2014-02-28)
Tripartite Tc toxin complexes of bacterial pathogens perforate the host membrane and translocate toxic enzymes into the host cell, including in humans. The underlying mechanism is complex but poorly understood. Here we report the first, to our knowledge, high-resolution structures
Tadatsugu Imamura et al.
Journal of virology, 88(5), 2374-2384 (2013-12-29)
Increased detection of enterovirus 68 (EV68) among patients with acute respiratory infections has been reported from different parts of the world in the late 2000s since its first detection in pediatric patients with lower-respiratory-tract infections in 1962. However, the underlying
Patricia J Campbell et al.
Journal of virology, 88(7), 3802-3814 (2014-01-17)
The 2009 H1N1 lineage represented the first detection of a novel, highly transmissible influenza A virus genotype: six gene segments originated from the North American triple-reassortant swine lineage, and two segments, NA and M, derived from the Eurasian avian-like swine

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Learn about O-linked glycan strategies, O-glycosidase actions, how to remove sialic acid residues, β-Elimination, and O-glycan modifications.

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