| Product Name | nanA, 1-297aa |
|---|---|
| Description | 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. |
| Synonyms | N-acetylneuraminate lyase, npl |
| Host | E. coli |
| Molecular Weight | 39.9 kDa (355aa) confirmed by MALDI-TOF (Molecular weight on SDS-PAGE will appear higher) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG VGALKQTSGD LYQMEQIRRE HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 20% glycerol, 5mM DTT, 0.2M NaCl. |
| Concentration | 0.5 mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Aisaka K., et al. (1991) Biochem. J. 276:541-546 Izard T., et al. (1994) Structure 2:361-369 |
| Background | 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. |
| Supplier | ARP |
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