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NEU2 Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
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- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9Y3R4 |
|---|---|
| Clone Names | 101008006 |
| Gene ID | 4759 |
|---|---|
| Other Names | Sialidase-2, Cytosolic sialidase, N-acetyl-alpha-neuraminidase 2, NEU2 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | NEU2 |
|---|---|
| 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). |
| Cellular Location | Cytoplasm, cytosol. |
| Tissue Location | Expressed in skeletal muscle, fetal liver and embryonic carcinoma cell line NT2-D1. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene belongs to a family of glycohydrolytic enzymeswhich remove sialic acid residues from glycoproteins andglycolipids. Expression studies in COS7 cells confirmed that thisgene encodes a functional sialidase. Its cytosolic localization wasdemonstrated by cell fractionation experiments. [provided byRefSeq].
References
Stoppani, E., et al. Cell Biol. Int. 33(9):1020-1025(2009)Li, C.Y., et al. Cell Res. 17(4):357-362(2007)Chavas, L.M., et al. J. Biol. Chem. 280(1):469-475(2005)Seyrantepe, V., et al. J. Biol. Chem. 279(35):37021-37029(2004)Tringali, C., et al. J. Biol. Chem. 279(5):3169-3179(2004)
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