|25 units/100 μL protein|
|ml wt||Mᵣ = 55 kDa|
|packaging||300 μL of liquid |
|optimum pH||5.0 - 5.5|
|shipped in||shipped at 4°C|
Use Neuraminidase to hydrolyze 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. 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.
For life science research only. Not for use in diagnostic procedures.
Enzyme/substrate ratio should be in the range of 0.04 U/25-80 μg.
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.
100 μL enzyme solution in 10 mM sodium phosphate were freeze-dried.
Larger quantities for your development, manufacturing or research applications needed?
Please enquire at firstname.lastname@example.org
|Safety Information for this product is unavailable at this time. |
|Datasheet Akkermansia Neuraminidase|
|No Protocol available yet.|
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