N5521
α(2→3,6) Neuraminidase from Clostridium perfringens (C. welchii)
recombinant, expressed in E. coli, buffered aqueous solution, ≥250 units/mg protein
Synonym(s):
Acyl-Neuraminyl Hydrolase, Sialidase
recombinant
expressed in E. coli
Quality Level
form
buffered aqueous solution
specific activity
≥250 units/mg protein
mol wt
~41 kDa
foreign activity
proteases, none detected
shipped in
wet ice
storage temp.
2-8°C
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Biochem/physiol Actions
Releases α(2→3)- and α(2→6)-linked N-acetylneuraminic acid from complex oligosaccharides.
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 25 mM NaCl.
Preparation Note
Expressed in glycosidase-free hosts.
Other Notes
One unit will hydrolyze 1 μmole of 4-methylumbelliferyl α-D-N-acetylneuraminide per min at pH 5.0 at 37 °C
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Weijia Wang et al.
Journal of virology, 87(8), 4642-4649 (2013-02-15)
In 2009, we successfully produced a high-yield live attenuated H1N1pdm A/California/7/2009 vaccine (CA/09 LAIV) by substitution of three residues (K119E, A186D, and D222G) in the hemagglutinin (HA) protein. Since then, we have generated and evaluated additional H1N1pdm vaccine candidates from
Andreas Max Ernst et al.
FEBS letters, 587(9), 1411-1417 (2013-03-26)
Influenza A Neuraminidase is essential for virus release from the cell surface of host cells. Given differential structures of the N-terminal sequences including the transmembrane domains of neuraminidase subtypes, we investigated their contribution to transport and localization of subtypes N1
S Bhatt et al.
Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 368(1614), 20120382-20120382 (2013-02-06)
Few questions on infectious disease are more important than understanding how and why avian influenza A viruses successfully emerge in mammalian populations, yet little is known about the rate and nature of the virus' genetic adaptation in new hosts. Here
Longping V Tse et al.
Journal of virology, 87(9), 5161-5169 (2013-03-02)
Influenza virus is well recognized to modulate host tropism and pathogenesis based on mutations in the proteolytic cleavage site of the viral hemagglutinin (HA), which activates HA and exposes the fusion peptide for membrane fusion. Instead of the conventional trypsin-mediated
Andrew T Pavia
Infectious disease clinics of North America, 27(1), 157-175 (2013-02-13)
Respiratory viruses have long been appreciated as a cause of community acquired pneumonia (CAP), particularly among children, people with serious medical comorbidities, and military recruits. They are increasingly recognized as a cause of CAP among adults. Polymerase chain reaction-based testing
Articles
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