XAP2 Inhibitors
Chemical inhibitors of XAP2 function primarily by disrupting its interaction with the chaperone protein Hsp90, which is essential for the stability and proper folding of XAP2. Geldanamycin, a benzoquinone ansamycin antibiotic, binds to the ATP/ADP-binding pocket of Hsp90. This binding event interferes with the chaperone cycle of Hsp90, leading to the destabilization of the XAP2-Hsp90 complex. As a result, XAP2 is unable to maintain its proper conformation and is targeted for degradation. Similar in action, Alvespimycin, Onalespib, and Luminespib are all established Hsp90 inhibitors that incapacitate the chaperone's function. This results in the inhibition of the stabilizing effect Hsp90 has on XAP2, thereby reducing the functional competency of XAP2 within the cell. Ganetespib, another Hsp90 antagonist, binds to the chaperone and suppresses its activity, which is a prerequisite for the maturation and functional activity of XAP2. Consequently, XAP2 is destabilized without the support of Hsp90, leading to its functional inhibition.
PU-H71, SNX-2112, BIIB021, Debio 0932, and KW-2478 constitute a group of Hsp90 inhibitors that all share a similar mechanism of action in regards to the inhibition of XAP2. These compounds effectively bind to Hsp90, disrupting its interaction with XAP2. The result of this disruption is the inhibition of the chaperone-assisted stabilization and function of XAP2. Without the necessary chaperone activity of Hsp90, XAP2 is unable to properly fold and is marked for proteasomal degradation. This series of interactions and subsequent loss of functional XAP2 highlights the reliance of XAP2 on Hsp90 for its stability and activity within the cellular environment.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $39.00 $59.00 $104.00 $206.00 | 8 | |
Geldanamycin binds to the ATP/ADP-binding pocket of Hsp90 (Heat shock protein 90), which is known to form a complex with XAP2, leading to the destabilization of the XAP2-Hsp90 interaction, thereby inhibiting the stabilizing effect of Hsp90 on XAP2. | ||||||
17-DMAG | 467214-20-6 | sc-202005 | 1 mg | $205.00 | 8 | |
Alvespimycin, another Hsp90 inhibitor, similarly disrupts the association between Hsp90 and XAP2, which can inhibit the proper folding and functioning of XAP2, as Hsp90 is crucial for its chaperone activity. | ||||||
AT13387 | 912999-49-6 | sc-364415 sc-364415A | 10 mg 50 mg | $555.00 $1606.00 | ||
Onalespib targets Hsp90, preventing its interaction with client proteins such as XAP2, and therefore inhibits the chaperone-assisted stabilization and function of XAP2. | ||||||
NVP-AUY922 | 747412-49-3 | sc-364551 sc-364551A sc-364551B sc-364551C sc-364551D sc-364551E | 5 mg 25 mg 100 mg 250 mg 1 g 5 g | $150.00 $263.00 $726.00 $1400.00 $2900.00 $11000.00 | 3 | |
Luminespib is an Hsp90 inhibitor that impairs the chaperone’s function, thus inhibiting the stabilization and proper folding of XAP2, which relies on Hsp90 for its activity. | ||||||
Ganetespib | 888216-25-9 | sc-364496 sc-364496A | 10 mg 250 mg | $273.00 $1040.00 | ||
Ganetespib binds to Hsp90, disrupting its chaperone function, which leads to the destabilization and degradation of client proteins, including XAP2, effectively inhibiting XAP2's function. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
BIIB021 is an Hsp90 inhibitor that disrupts its interaction with XAP2, leading to the inhibition of XAP2's functionality as it relies on Hsp90 for its stability and activity. | ||||||
Debio 0932 | 1061318-81-7 | sc-507516 | 10 mg | $280.00 | ||
Debio 0932 inhibits Hsp90, which is associated with XAP2, leading to the functional inhibition of XAP2 due to the lack of chaperone-mediated stability and activity. | ||||||