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Conditions of optimal NANA Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
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Introduction
N-acetylneuraminate lyase (NanA) is a member of a 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. NanA is inhibited by reduction with NaBH4 in the presence of the substrate, which indicates that it belongs to the Schiff-base-forming Class I aldolases. NanA is strongly inhibited by Cu2+ ions, p-chloromercuribenzoate and N-bromosuccinimide, it is also inhibited competitively by the reaction product, pyruvate, and its structurally related compounds, dihydroxyacetone and DL-glyceraldehyde.
BP002564-ENZ-128: Recombinant E.Coli N-Acetylneuraminate Lyase (NANA) Enzyme
Source: E. coli-derived.
A single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a.) and having a molecular mass of 34.7 kDa. NANA is fused to a 20 amino acid His-tag at N-terminus.
Purity: > 95% as determined by SDS-PAGE.
Formulation: The NANA protein solution (1 mg/ml) 20 mM Tris-HCl buffer (pH8.0) and 20% glycerol.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
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