Neomycin Sulfate

Aminoglycoside antibiotic that inhibits translation by binding to the small subunit of prokaryotic ribosomes. Inhibitor of phospholipase C due to binding to inositol phospholipids. Neomycin inhibits phosphatidylcholine-phospholipase D activity. Blocks voltage sensitive Ca2+ channels without affecting Na+/Ca2+ antiporter in nerve cells.\n\nPotency:(same/more than) 600 IU/mg (dry basis)\n\npH: 5.0-7.5\nAppearance: White to light yellow crystaline powder\nIdentity: Conforms to USP reference\nLoss on Drying: (same/less than) 8.0%\n

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SPECIFICATIONS

Catalog Number

N2010

Size

100g

Form

Light yellow crystaline powder

References

1. Effects of neomycin on calcium and polyphosphoinositide metabolism of guinea pig synaptosomes: H.D. Griffin, et al.; J. Neurochem. 34 , 750 (1980) Abstract. 2. Phosphoinositides in mitogenesis: neomycin inhibits thrombin-stimulated phosphoinositide turnover and initiation of cell proliferation: D.H. Carney, et al.; Cell 42 , 479 (1985) Abstract. 3. Inositol 1,4,5-trisphosphate: a possible chemical link in excitation- contraction coupling in muscle: J. Vergara, et al.; PNAS 82 , 6352 (1985) Abstract. 4. Neomycin is a potent agent for arachidonic acid release in human platelets: S. Nakashima, et al.; BBRC 146 , 820 (1987) Abstract. 5. Binding of neomycin to phosphatidylinositol 4,5-bisphosphate (PIP2): E. Gabev, et al.; Biochim. Biophys. Acta 979 , 105 (1989) Abstract. 6. Inhibition of neural phospholipase D activity by aminoglycoside antibiotics: M. Liscovitch, et al.; Biochem. J. 279 , 319 (1991) Abstract. 7. Gadolinium and neomycin block voltage-sensitive Ca2+ channels without interfering with the Na(+)-Ca2+ antiporter in brain nerve endings: L.M. Canzoniero, et al.; Eur. J. Pharmacol. 245 , 97 (1993) Abstract. 8. Neomycin inhibition of hormone-stimulated smooth muscle contractions in myometrial tissue: M. Philippe; BBRC 205 , 245 (1994) Abstract. 9. Nerve extracts and substance P activate the phosphatidylinositol signaling pathway and mitogenesis in newt forelimb regenerates: M.J. Smith, et al.; Dev. Biol. 167 , 239 (1995) Abstract.