Home  >  Products  >  Virginiamycin Complex (Virginiamycin M1, Virginiamycin S1, Cebin V, Eskalin V, Eskamicin, Stafac, Stephylomycin, Mikamycin, Ostreogrycin, Patricin, Pristinamycin, Streptogramin, Vernamycin)

Virginiamycin Complex (Virginiamycin M1, Virginiamycin S1, Cebin V, Eskalin V, Eskamicin, Stafac, Stephylomycin, Mikamycin, Ostreogrycin, Patricin, Pristinamycin, Streptogramin, Vernamycin)

Cat no: V2123-59


Supplier: United States Biological
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Virginiamycin complex is defined as a mixture of 75% virginamycin M1 (ostreogrycin A) and 25% virginiamycin S1 and the less abundant S analogs. As the two major components have quite different solubilities these proportions are not readily achieved or used. The individual components are isolated and re-combined to provide the defined components of virginiamycin complex. The structure composition of the complex is important as Virginiamycin S1 acts a synergist binding to the conformational change induced by ostreogrycin A of the peptidyl transferase center of the 50S ribosome. Source: Virginiamycin Complex Molecular Weight: ~525.6-823.9 Solubility: Soluble DMF or DMSO. Viriginiamycin M1 has only limited solubility in ethanol and methanol. Storage and Stability: Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with DMF or DMSO. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: V2123-59
Size: 5mg
Form: Supplied as a white solid.
Purity: (same/more than) 95% by HPLC (75% Virginamycin M1, 20% Virginiamycin S1, ~5% Other minor analogs)
Alternative names: Cebin V, Eskalin V, Eskamicin, Stafac, Stephylomycin, Mikamycin, Ostreogrycin, Patricin, Pristinamycin, Streptogramin, Vernamycin
References: 1. The structures of the minor components of virginiamycin S. Vanderhaeghe, H., et al., Tet. Lett. 2687 (1971). 2. Virginiamycin: nomenclature. Crooy, P. and De Neys, R.J., Antibiot. 25: 371 (1972). 3. Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms. Porse, B.T., and Garrett, R.A., J. Mol. Biol. 286: 375 (1999).

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