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The protein encoded by NEU4 belongs to a family of glycohydrolytic enzymes, which remove terminal sialic acid residues from various sialo derivatives, such as glycoproteins, glycolipids, oligosaccharides, and gangliosides. Additionally we are shipping Sialidase 4 Proteins (3) and many more products for this protein.
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The most potent compound tested targeted the human Neu4 isoenzyme, and was able to substantially reduce the rate of cell migration. We found that the lateral mobility of integrins was reduced by treatment of cells with Neu3, suggesting that Neu3 enzyme activity resulted in changes to integrin-co-receptor or integrin-cytoskeleton interactions
The silencing or chemical inhibition of NEU4 changes the entire glycosylation pattern of proteins and lipids, making it more similar to that of differentiated GBM cells and drastically reduces GSCs survival.
The results demonstrate that the proline-rich region can also enhance cell proliferation and retinoic acid (RA)-induced neuronal differentiation and it is also involved in NEU4 interaction with Akt.
Overexpression of NEU4 is associated with neuroblastoma.
NEU4 is involved in regulation of neuronal function by polySia degradation in mammals.
NEU4 plays an important role in control of sialyl Lewis antigen expression and its impairment in colon cancer
The NEU4 long form localizes in mitochondria, while the short form is also associated with the endoplasmic reticulum.
The NEU4 gene, identified by searching sequence databases for entries showing homologies to the human cytosolic sialidase NEU2, maps in 2q37 and encodes a 484-residue protein.
Neu4 is a novel human lysosomal lumen sialidase
Data show that the differentiation of monocytes into macrophages is associated with regulation of the expression of at least three distinct cellular sialidases, Neu1, 3, and 4, with specific up-regulation of the enzyme activity of only Neu1.
related to malignancy and may be potential targets for cancer diagnosis and therapy
These results provide the first in vivo evidence that neuraminidases 3 and 4 have important roles in CNS function by catabolizing gangliosides and preventing their storage in lipofuscin bodies.
Neu4 is not the only sialidase contributing to the metabolic bypass in Hexa(-/-) mice.
Neu4 is a functional component of the ganglioside-metabolizing system, contributing to the postnatal development of the brain and other vital organs.
mouse Neu4 plays an important regulatory role in neurite formation, possibly through desialylation of glycoproteins
The protein encoded by this gene belongs to a family of glycohydrolytic enzymes, which remove terminal sialic acid residues from various sialo derivatives, such as glycoproteins, glycolipids, oligosaccharides, and gangliosides. Alternatively spliced transcript variants encoding different isoforms have been noted for this gene.
, neuraminidase 4