nanA (1-297, His-tag) Escherichia coli Protein

Specifications

Product Data
Species	Escherichia coli
Expression Host	E. coli
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) 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
Predicted MW	34.7 kDa
Concentration	lot specific
Purity	>95%
Buffer	Presentation State: Purified State: Liquid purified protein Buffer System: 20 mM Tris-HCl buffer (pH 8.0) containing 20% glycerol
Preparation	Liquid purified protein
Protein Description	Recombinant E.coli nanA protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Storage	Store undiluted at 2-8°C for up to two weeks or (in aliquots) at -20°C or -70°C for longer. Avoid repeated freezing and thawing.
Stability	Shelf life: one year from despatch.
Reference Data
Summary	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.

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