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NEU2 belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Additionally we are shipping NEU2 Proteins (7) and NEU2 Kits (3) and many more products for this protein.
Showing 10 out of 58 products:
Human Polyclonal NEU2 Primary Antibody for EIA, FACS - ABIN954803
Stoppani, Rossi, Marchesini, Preti, Fanzani: Defective myogenic differentiation of human rhabdomyosarcoma cells is characterized by sialidase Neu2 loss of expression. in Cell biology international 2009
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Human Polyclonal NEU2 Primary Antibody for EIA, IHC (fro) - ABIN117994
Fanzani, Giuliani, Colombo, Zizioli, Presta, Preti, Marchesini: Overexpression of cytosolic sialidase Neu2 induces myoblast differentiation in C2C12 cells. in FEBS letters 2003
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Human Monoclonal NEU2 Primary Antibody for ELISA, WB - ABIN518292
Bilyy, Shkandina, Tomin, Muñoz, Franz, Antonyuk, Kit, Zirngibl, Fürnrohr, Janko, Lauber, Schiller, Schett, Stoika, Herrmann: Macrophages discriminate glycosylation patterns of apoptotic cell-derived microparticles. in The Journal of biological chemistry 2012
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Human Polyclonal NEU2 Primary Antibody for FACS, IF - ABIN656123
Seyrantepe, Landry, Trudel, Hassan, Morales, Pshezhetsky: Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells. in The Journal of biological chemistry 2004
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Neu2 from thymus exhibited sialidase activity with fetuin (show AHSG Antibodies) at pH 7.0.
Our data demonstrate that IGF-1 (show IGF1 Antibodies)-induced myoblast differentiation and hypertrophy are driven, at least in part, by Neu2 upregulation and further support the significant role of cytosolic sialidase in myoblasts.
the lack of soluble sialidase activity in the SM/J mouse thymus is due to the thymus-specific low expression level of the Neu2 gene
30-40% of B and C forms of Neu2 activity was located in the crude membrane-fraction, and hydrolyzed ganglioside effectively, while both soluble fraction showed particular behavior with substrate specificity.
cytosolic GBA3 (show GBA3 Antibodies) is likely involved in the catabolism of cytosolic sialyl free N-glycans, possibly by stabilizing the activity of the NEU2 protein
Circular dichroism (CD) spectra at variable temperatures have been recorded for human cytosolic sialidase NEU2 in buffered water solutions and in the presence of divalent cations.
Q136K is a novel mutation in an expressed NEU2 protein that was discovered during crystallographic analysis.
the present study demonstrated NEU2 expression to be detectable but very low in many human tissues and cells, and suggested possible functional roles in PC-3 (show PCSK1 Antibodies) prostate cancer cells.
NEU2 appears to be activated when lysine 45 and glutamine (show GFPT1 Antibodies) 112 are mutated to alanine.
the first high resolution x-ray structures of sialidase, human Neu2
Neu2 loss of expression might exacerbate the defective myogenic differentiation of rhabdomyosarcoma cells.
This gene belongs to a family of glycohydrolytic enzymes which remove sialic acid residues from glycoproteins and glycolipids. Expression studies in COS7 cells confirmed that this gene encodes a functional sialidase. Its cytosolic localization was demonstrated by cell fractionation experiments.
sialidase 2 (cytosolic sialidase)
, N-acetyl-alpha-neuraminidase 2
, brain sialidase
, cystolic sialidase
, cytosolic sialidase
, murine thymic sialidase
, skeletal muscle sialidase
, neuraminidase 2