FLJ13236 Inhibitors
Chemical inhibitors of FLJ13236 act by disrupting the normal chaperone functions with which this protein is associated. Geldanamycin and its derivative 17-AAG, as well as tanespimycin, specifically target Hsp90, causing a chain reaction that leads to the degradation of this chaperone's client proteins. Since FLJ13236 is a co-chaperone that relies on the proper function of Hsp90, these compounds indirectly inhibit FLJ13236 by destabilizing the chaperone complex it is part of. Radicicol works in a similar manner by binding to the ATP-binding pocket of Hsp90, preventing the chaperone from assisting in the proper folding of proteins, which is the fundamental role that FLJ13236 supports. Novobiocin also targets Hsp90 but does so at the C-terminal domain, a different site from the others, leading to the dissociation of co-chaperones such as FLJ13236. On the other hand, luminespib and onalespib bind competitively to the N-terminal ATP-binding domain of Hsp90, again leading to an inhibition of the chaperone cycle and, consequently, the activities of FLJ13236.
Furthermore, sirolimus can indirectly inhibit FLJ13236 by downregulating the expression of Hsp70, another chaperone protein that FLJ13236 works in conjunction with. By reducing Hsp70 levels, sirolimus effectively diminishes the functional activity of FLJ13236. Cyclosporin A, although its primary target is not directly related to the chaperone network, impacts protein folding and stress response pathways that can indirectly inhibit FLJ13236's function. Withaferin A adds to the list of Hsp90 affecting agents by inducing the degradation of client proteins, impacting Hsp90's chaperone cycle and FLJ13236's role within it. PU-H71, a purine-scaffold Hsp90 inhibitor, also contributes to the degradation of Hsp90 clientele, thereby inhibiting FLJ13236. Lastly, zoptarelin doxorubicin, while not a direct chaperone inhibitor, can affect cellular stress pathways, potentially leading to a compromised protein complex stability that includes the chaperone system associated with FLJ13236.
SEE ALSO...
| 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 Hsp90 and inhibits its chaperone activity. Since FLJ13236 is a co-chaperone in association with Hsp70, inhibition of Hsp90 can disrupt the functional complex formation of Hsp70 and its co-chaperones, leading to an inhibition of the chaperoning function that FLJ13236 is involved in. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
Similar to Geldanamycin, 17-AAG targets Hsp90 causing the degradation of client proteins and the associated co-chaperones. By destabilizing the chaperone complexes indirectly, 17-AAG would inhibit the chaperone activity where FLJ13236 is functioning as a co-chaperone. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Radicicol functions as an Hsp90 inhibitor by binding to its ATP-binding pocket, thus preventing the proper functioning of Hsp90 and its associated co-chaperone network, including FLJ13236, leading to an inhibition of its chaperone function. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $128.00 $380.00 | ||
Novobiocin is another Hsp90 inhibitor which binds to the C-terminal ATPase domain, leading to the dissociation of co-chaperones. This action would result in the functional inhibition of FLJ13236 by disrupting its chaperone complex. | ||||||
Rapamycin | 53123-88-9 | sc-3504 sc-3504A sc-3504B | 1 mg 5 mg 25 mg | $63.00 $158.00 $326.00 | 233 | |
Sirolimus is an mTOR inhibitor that can lead to the downregulation of Hsp70 expression through inhibitory feedback loops. As FLJ13236 functions as a co-chaperone with Hsp70, the reduction in Hsp70 levels can lead to a corresponding decrease in FLJ13236 activity. | ||||||
Cyclosporin A | 59865-13-3 | sc-3503 sc-3503-CW sc-3503A sc-3503B sc-3503C sc-3503D | 100 mg 100 mg 500 mg 10 g 25 g 100 g | $63.00 $92.00 $250.00 $485.00 $1035.00 $2141.00 | 69 | |
Cyclosporin A inhibits the protein phosphatase activity of calcineurin. Since calcineurin regulates a variety of signaling pathways including those related to protein folding and stress response, its inhibition can disrupt the function of chaperone proteins, thereby inhibiting FLJ13236 indirectly. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $130.00 $583.00 $4172.00 $20506.00 | 20 | |
Withaferin A disrupts the function of Hsp90 by inducing the degradation of its client proteins. As a co-chaperone, FLJ13236 requires the proper function of Hsp90 to perform its role, therefore the destabilization of Hsp90 client proteins by Withaferin A would inhibit FLJ13236's activity. | ||||||
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, which binds competitively to the N-terminal ATP-binding domain of Hsp90, thereby impairing the chaperone cycle involving Hsp70 and co-chaperones like FLJ13236, leading to the inhibition of its function. | ||||||
AT13387 | 912999-49-6 | sc-364415 sc-364415A | 10 mg 50 mg | $555.00 $1606.00 | ||
Onalespib is an ATP-competitive inhibitor of Hsp90, which by inhibiting Hsp90 can disrupt the chaperone cycle and inhibit the associated co-chaperone activities, including those of FLJ13236. | ||||||
Doxorubicin | 23214-92-8 | sc-280681 sc-280681A | 1 mg 5 mg | $176.00 $426.00 | 43 | |
Zoptarelin Doxorubicin is a targeted cytotoxic agent that can affect cellular stress pathways and thus could influence the stability of protein complexes including those that FLJ13236 is a part of. By disrupting the homeostasis of the intracellular environment, this compound can lead to an inhibition of the chaperone systems that rely on FLJ13236. | ||||||