N-Acetylneuraminate pyruvate-lyase (N-
|Related Categories||Application Index, Biochemicals and Reagents, Carbohydrate hydrolysis & PTM analysis, Enzymes, Inhibitors, and Substrates, Glycosyltransferases and glycan synthesis More...|
|recombinant||expressed in E. coli BL21|
|shipped in||dry ice|
Enzymatic activity assays are performed in Tris-HCl buffer (100 mM, pH 7.5) containing Neu-5-Ac (10 mM) at 37 °C for 15 min and analyzed using capillary electrophoresis with UV detection at 200 nm.
Sialic acid aldolases, or N-acetylneuraminate lyases, catalyze the reversible aldol cleavage of N-acetylneuraminic acid to form pyruvate and N-acetyl-D-mannosamine. In nature, N-acetylneuraminate lyase mainly occurs in pathogens. 2
One unit will catalyze the formation of 1.0 μmol Neu-5-Ac from Man-N-Ac and pyruvate per minute at 37°C at pH 8.0.
Lyophilized powder containing Tris-HCl and NaCl
Sialic acid aldolase can be used to synthesize unnatural sugars of C(6) to C(10) for the design of antagonists and inhibitors of glycoenzymes. 1
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recombinant, expressed in E. coli BL21, ≥10 units/mg protein
from Escherichia coli, ≥98%
lyophilized powder, ≥20 units/mg protein (biuret)
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