nanA protein (His tag) (80R-1789)
Purified recombinant E.coli nanA protein
|Synonyms||N-acetylneuraminate lyase protein, npl protein|
Coomassie Blue stained SDS-PAGE of nanA protein (His tag) (80R-1789)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||1-297 amino acids: 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|
|Grade & Purity||> 95% pure|
|Molecular Weight||34.7 kDa (317aa) confirmed by MALDI-TOF|
|Form & Buffer||Supplied as a liquid in 20mM Tris-HCl buffer, pH 8.0, containing 20% glycerol.|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||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.|
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