Recombinant e.coli nanA protein

E.coli

NanA, also known as N-acetylneuraminate lyase, belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NanA catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetyl-D-mannosamine. This protein was inhibited by reduction with NaBH4 in the presence of the substrate, indicating that it belongs to the Schiff-base-forming Class I aldolases. NanA was strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, and also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde. Recombinant E. coli nanA protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography.

Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 20% glycerol

Aisaka K., et al. (1991) Biochem. J. 276:541-546; ; Izard T., et al. (1994) Structure 2:361-369

Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.