N7271
α(2→3) Neuraminidase from Streptococcus pneumoniae
buffered aqueous solution
Synonyme(s) :
Acyl-neuraminyl Hydrolase, Acylneuraminyl hydrolase, Receptor-destroying enzyme, Sialidase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.32
MDL number:
Biological source:
Streptococcus pneumoniae
Concentration:
≥5 units/mL
Service technique
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Laissez-nous vous aiderbiological source
Streptococcus pneumoniae
Quality Level
form
buffered aqueous solution
concentration
≥5 units/mL
foreign activity
β-Galactosidase, α-mannosidase, β-hexosaminidase, α-fucosidase, and proteases, none detected
shipped in
wet ice
storage temp.
2-8°C
Gene Information
Streptococcus pneumoniae R6 ... nanB(933504)
Biochem/physiol Actions
Releases α(2→3)-linked N-acetylneuraminic acid from complex oligosaccharides.
Packaging
Provided with 5× reaction buffer (250 mM sodium phosphate, pH 6.0).
Physical form
Solution in 50 mM sodium phosphate, pH 7.5
Preparation Note
Expressed in glycosidase-free hosts.
Other Notes
One unit will hydrolyze 1μmole of 4-methylumbelliferyl α-D-N-acetylneuraminide per min at pH 5.0 at 37 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
13 - Non Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Contenu apparenté
Datasheet
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
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
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