Geldanamycin from Streptomyces hygroscopicus
≥98% (HPLC)
- Product Code: 96285
CAS:
30562-34-6
Molecular Weight: | 560.64 g./mol | Molecular Formula: | C₂₉H₄₀N₂O₉ |
---|---|---|---|
EC Number: | MDL Number: | MFCD00274570 | |
Melting Point: | 255 °C | Boiling Point: | |
Density: | Storage Condition: | -20°C |
Product Description:
Geldanamycin is primarily used in research due to its ability to inhibit the function of heat shock protein 90 (Hsp90). By binding to Hsp90, it disrupts the protein's role in stabilizing and activating various client proteins, many of which are involved in cancer progression. This makes it a valuable tool in studying cancer biology and exploring potential therapeutic strategies. Additionally, geldanamycin has been investigated for its potential in treating neurodegenerative diseases, as Hsp90 inhibition can influence pathways associated with protein misfolding and aggregation. Its application extends to studying cellular stress responses and protein degradation mechanisms, providing insights into various disease processes.
Product Specification:
Test | Specification |
---|---|
CARBON | 61.6 62.6% |
NITROGENN | 4.5 5.5% |
PURITYHPLC | 98 100% |
APPEARANCE | YELLOW TO YELLOW-ORANGE POWDER |
PROTON NMR SPECTRUM | Conforms to Structure |
SOLUBILITY | YELLOW TO ORANGE CLEAR SOLUTION (5MG/ML,DICHLOROM |
Sizes / Availability / Pricing:
Size (g) | Availability | Price | Quantity |
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0.010 | 10-20 days | ฿2,130.00 |
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0.050 | 10-20 days | ฿5,340.00 |
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0.250 | 10-20 days | ฿12,020.00 |
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Geldanamycin from Streptomyces hygroscopicus
Geldanamycin is primarily used in research due to its ability to inhibit the function of heat shock protein 90 (Hsp90). By binding to Hsp90, it disrupts the protein's role in stabilizing and activating various client proteins, many of which are involved in cancer progression. This makes it a valuable tool in studying cancer biology and exploring potential therapeutic strategies. Additionally, geldanamycin has been investigated for its potential in treating neurodegenerative diseases, as Hsp90 inhibition can influence pathways associated with protein misfolding and aggregation. Its application extends to studying cellular stress responses and protein degradation mechanisms, providing insights into various disease processes.
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