Recombinant Human NEU2 protein
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Recombinant Human NEU2 protein is a Human Fragment protein, in the 180 to 268 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Sialidase-2, Cytosolic sialidase, N-acetyl-alpha-neuraminidase 2, NEU2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human NEU2 protein (AB116967)
12.5% SDS-PAGE showing ab116967 at approximately 35.42kDa stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
General info
Function
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).
Sequence similarities
Belongs to the glycosyl hydrolase 33 family.
Target data
Product promise
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