P4023
Phenyl N-acetyl-α-D-galactosaminide
≥98%
Synonyme(s) :
Phenyl 2-acetamido-2-deoxy-α-D-galactopyranoside
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About This Item
Formule empirique (notation de Hill):
C14H19NO6
Numéro CAS:
Poids moléculaire :
297.30
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352201
ID de substance PubChem :
Pureté
≥98%
Température de stockage
2-8°C
Chaîne SMILES
CC(=O)NC1C(O)C(O)C(CO)OC1Oc2ccccc2
Description générale
Phenyl-N-acetyl-α-D-galactosaminide is a competitive inhibitor of N-acetyl-α-D-galactose and N-acetylneuraminic acid transferases.
Application
Phenyl N-acetyl-α-D-galactosaminide has been used in a study to treat papillae in order to assess regeneration of broken tip links and restoration of mechanical transduction in hair cells. It has also been used in a study to inhibit N- and mucin-like O-glycosylation in order to investigate a novel transmembrane serine protease overexpressed in pancreatic cancer.
Code de la classe de stockage
13 - Non Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Y Zhao et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(26), 15469-15474 (1996-12-24)
A hair cell's tip links are thought to gate mechanoelectrical transduction channels. The susceptibility of tip links to acoustic trauma raises questions as to whether these fragile structures can be regenerated. We broke tip links with the calcium chelator 1,2-bis(O-aminophenoxy)
N Gross et al.
Medical and pediatric oncology, 36(1), 139-141 (2001-07-24)
CD44 represents a heterogeneous group of surface glycoproteins involved in cell-cell and cell-matrix interactions. CD44H is the major receptor for hyaluronate, and most if not all CD44H known functions are attributed to its ability to recognize hyaluronate. We have previously
H Sadeghi et al.
Glycobiology, 9(7), 731-737 (1999-06-11)
The human V2 vasopressin receptor contains one consensus site for N-linked glycosylation at asparagine 22 in the predicted extracellular amino terminal segment of the protein. This segment also contains clusters of serines and threonines that are potential sites for O-glycosylation.
C Wallrapp et al.
Cancer research, 60(10), 2602-2606 (2000-05-29)
We report the characterization of a novel serine protease of the chymotrypsin family, recently isolated by cDNA-representational difference analysis, as a gene overexpressed in pancreatic cancer. The 2.3-kb mRNA of the gene, named TMPRSS3, is strongly expressed in a subset
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