Further Information
Chromogenic alpha-mannosidase substrate yielding a absorbent solution upon cleavage. Also used for studies of the crystal structure of the complexes of concanavalin A and binding studies with concanavalin A. 1. Bonay P., Fresno M., Isolation and purification of a neutral alpha(1,2)-mannosidase from Trypanosoma cruzi. Glycobiology 1999, 9, 423-33. 2. Conchie J., Hay A.J., Mammalian glycosidases. 2. Properties of alpha-mannosidase and beta-galactosidase from rat epididymis. Biochem. J. 1959, 73, 327-34. 3. Conchie J., Hay A.J., Mammalian glycosidases. 4. The intracellular localization of beta-galactosidase, alpha-mannosidase, beta-N-acetylglucosaminidase and alpha-L-fucosidase in mammalian tissues. Biochem. J. 1963, 87, 354-61. 4. Hamodrakas S.J., Alexandraki E., Troganis A., Stassinopoulou C.I., Models of binding of 4'-nitrophenyl alpha-D-mannopyranoside to the lectin concanavalin A. Int. J. Biol. Macromol. 1989, 11, 17-22. 5. Jelinek-Kelly S., Akiyama T., Saunier B., Tkacz J.S., Herscovics A., Characterization of a specific alpha-mannosidase involved in oligosaccharide processing in Saccharomyces cerevisiae. J. Biol. Chem. 1985, 260, 2253-7. 6. Kanellopoulos P.N., Pavlou K., Perrakis A., Agianian B., Vorgias C.E., Mavrommatis C., Soufi M., Tucker P.A., Hamodrakas S.J., The crystal structure of the complexes of concanavalin A with 4'-nitrophenyl-alpha-D-mannopyranoside and 4'-nitrophenyl-alpha-D-glucopyranoside. J. Struct. Biol. 1996, 116, 345-55.
Details
Chromogenic alpha-mannosidase substrate yielding a absorbent solution upon cleavage. Also used for studies of the crystal structure of the complexes of concanavalin A and binding studies with concanavalin A. 1. Bonay P., Fresno M., Isolation and purification of a neutral alpha(1,2)-mannosidase from Trypanosoma cruzi. Glycobiology 1999, 9, 423-33. 2. Conchie J., Hay A.J., Mammalian glycosidases. 2. Properties of alpha-mannosidase and beta-galactosidase from rat epididymis. Biochem. J. 1959, 73, 327-34. 3. Conchie J., Hay A.J., Mammalian glycosidases. 4. The intracellular localization of beta-galactosidase, alpha-mannosidase, beta-N-acetylglucosaminidase and alpha-L-fucosidase in mammalian tissues. Biochem. J. 1963, 87, 354-61. 4. Hamodrakas S.J., Alexandraki E., Troganis A., Stassinopoulou C.I., Models of binding of 4'-nitrophenyl alpha-D-mannopyranoside to the lectin concanavalin A. Int. J. Biol. Macromol. 1989, 11, 17-22. 5. Jelinek-Kelly S., Akiyama T., Saunier B., Tkacz J.S., Herscovics A., Characterization of a specific alpha-mannosidase involved in oligosaccharide processing in Saccharomyces cerevisiae. J. Biol. Chem. 1985, 260, 2253-7. 6. Kanellopoulos P.N., Pavlou K., Perrakis A., Agianian B., Vorgias C.E., Mavrommatis C., Soufi M., Tucker P.A., Hamodrakas S.J., The crystal structure of the complexes of concanavalin A with 4'-nitrophenyl-alpha-D-mannopyranoside and 4'-nitrophenyl-alpha-D-glucopyranoside. J. Struct. Biol. 1996, 116, 345-55.
Additional Information
| ART-NO | GBB1294 |
|---|---|
| CAS-NO | 10357-27-4 |
| DETAIL NAME | 4-Nitrophenyl-alpha-D-mannopyranoside, 99% |
| FORMULA | C12H15NO8 |
| MOLECULAR WEIGHT | 301,26 |
| Bezeichnung Mol Ge | g/mole |
| QUANTITY | 5 g |
| neu | N |
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