Recombinant Human NEU2 protein (His tag) is a Human Full Length protein, in the 1 to 380 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides (PubMed:14613940, PubMed:22228546). Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate. Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles. Hydrolyzes monomeric GM1 ganglioside, but has no activity toward the miscellar form (PubMed:14613940). Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues (PubMed:14613940).
Sialidase-2, Cytosolic sialidase, N-acetyl-alpha-neuraminidase 2, NEU2
Recombinant Human NEU2 protein (His tag) is a Human Full Length protein, in the 1 to 380 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: 20% Glycerol (glycerin, glycerine), 2.9% Sodium chloride, 0.24% Tris
Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides (PubMed:14613940, PubMed:22228546). Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate. Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles. Hydrolyzes monomeric GM1 ganglioside, but has no activity toward the miscellar form (PubMed:14613940). Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues (PubMed:14613940).
Belongs to the glycosyl hydrolase 33 family.
The NEU2 gene encodes for the enzyme neuraminidase 2 also known as sialidase 2. Neuraminidase 2 has a mass of approximately 42 kDa. It plays a critical role in cleaving sialic acids from glycoproteins and glycolipids. NEU2 expression is mainly found in skeletal muscle and has been noted in other tissues such as the heart and kidney. These enzyme activities are important in cell-cell communication and modulation of immune responses.
Neuraminidase 2 participates in the catabolism of sialoglycoconjugates. It is not a part of a larger protein complex but acts independently to remove sialic acids which can alter the properties and functions of substrates like glycoproteins on cell surfaces. These activities impact a number of biological processes including cellular signaling pathways which can influence immune and inflammatory responses.
Neuraminidase 2 is involved in the catabolic process of the sialyl group as part of the glycosphingolipid metabolism. It is closely linked to the lysosomal pathway impacting the degradation and recycling of biomolecules. NEU2’s enzymatic work closely relates to other neuraminidases such as NEU1 and neurominidase-3 which have overlapping functions but different tissue distributions and substrate specificities.
Deficiencies or dysfunctions in neuraminidase 2 have associations with conditions like sialidosis and galactosialidosis. These disorders arise from improper degradation of sialic acids and can impact multiple systems in the body including the central nervous system. The protein NEU1 is another neuraminidase involved in similar disorders but it primarily contributes to lysosomal storage; together they underline the importance of proper sialic acid metabolism in health.
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SDS-PAGE analysis of ab276691
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