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Concanamycin A (Folimycin, Antibiotic TAN 1323B)

Cat no: C7852-20


Supplier: United States Biological
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Concanamycin A is the major analogue of the concanamycin complex produced by Streptomyces sp. It has has been shown to act as a potent and specific vacuolar-APTase inhibitor. Concanamycin A inhibits the acidification of organelles and blocks cell surface expression of viral envelope glycoproteins without affecting their synthesis. It also interferes with intracellular protein trafficking and inhibits perforin- and Fas-based lytic pathways in cell-mediated cytotoxicity. Concanamycins are structurally related to the bafilomycins. Purity: >99% by HPLC Solubility: Soluble in ethanol, methanol, DMF or DMSO Related to: Bafilomycin A1, Bafilomycin B1, Bafilomycin C1 Storage and Stability: Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with ethanol, methanol, 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: C7852-20
Size: 250ug
Form: Supplied as a white lyophilized powder
Purity: ~90% by HPLC
Alternative names: Folimycin, Antibiotic TAN 1323B
References: 1. The V-ATPase inhibitors concanamycin A and bafilomycin A lead to Golgi swelling in tobacco BY-2 cells. Robinson D.G. et al. Protoplasma 2004, 224, 255. 2. Concanamycin A, a powerful tool for characterization and estimation of contribution of perforin- and Fas-based lytic pathways in cell-mediated cytotoxicity. Kataoka T. et al. J. Immunol. 1996, 156, 3678. 3. Specific inhibitors of vacuolar type H(+)-ATPases induce apoptotic cell death. Nishihara T. et al. Biochem. Biophys. Res. Commun. 1995, 212, 255. 4. Folimycin (concanamycin A), a specific inhibitor of V-ATPase, blocks intracellular translocation of the glycoprotein of vesicular stomatitis virus before arrival to the Golgi apparatus. Muroi M. et al. Cell Struct. Funct. 1993, 18, 139.

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