KBTBD5 Activators
The chemicals described as KBTBD5 Activators are not direct activators but influence the ubiquitin-proteasome system, where KBTBD5 serves a role in protein ubiquitination. Compounds like MG132, Bortezomib, and Epoxomicin function as proteasome inhibitors, causing the accumulation of proteins that need to be tagged for degradation. This accumulation can activate a cellular response that upregulates the activity of ubiquitin ligases such as KBTBD5 to manage the increased load of proteins that must be processed.
Other compounds like Withaferin A, Tunicamycin, and Thapsigargin exert stress on cells, including proteotoxic stress and endoplasmic reticulum (ER) stress, respectively. Such stresses can activate the unfolded protein response, which often leads to an increase in the ubiquitin-proteasome system's components, including E3 ubiquitin ligases like KBTBD5, to restore cellular proteostasis. Celastrol and Salubrinal elicit similar stress responses, which can result in enhanced KBTBD5 activity to help mitigate the effects of misfolded or damaged proteins. Finally, Chloroquine, which affects autophagy, or compounds like Beta-lactone that specifically target proteasome subunits, can also lead to an upregulation of ubiquitin ligases including KBTBD5, as the cell attempts to balance the disruption in protein degradation.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
A steroidal lactone that disrupts proteasomal function. Its ability to induce proteotoxic stress can stimulate compensatory mechanisms in the ubiquitin-proteasome pathway, which may include the activation of KBTBD5 to tag damaged proteins for degradation. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
A nucleoside antibiotic that inhibits N-linked glycosylation, causing ER stress. ER stress can lead to the activation of the unfolded protein response (UPR), which often results in an increased expression of E3 ubiquitin ligases, potentially activating KBTBD5. | ||||||
Thapsigargin | 67526-95-8 | sc-24017 sc-24017A | 1 mg 5 mg | $136.00 $446.00 | 114 | |
A sesquiterpene lactone that disrupts calcium homeostasis by inhibiting the ER calcium ATPase. This disruption triggers UPR, and part of this response may upregulate the ubiquitin-proteasome system, possibly enhancing the activity of ubiquitin ligases like KBTBD5. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $158.00 | 6 | |
A triterpene that induces heat shock proteins and leads to an increase in cellular stress responses. By triggering these responses, cells may elevate the expression and function of E3 ubiquitin ligases, including KBTBD5, to cope with misfolded proteins. | ||||||
Salubrinal | 405060-95-9 | sc-202332 sc-202332A | 1 mg 5 mg | $34.00 $104.00 | 87 | |
A selective inhibitor of eIF2α dephosphorylation, which leads to an increased phosphorylation state of eIF2α, causing ER stress and activation of UPR. This activation can include upregulation of E3 ubiquitin ligases, potentially affecting the activity of KBTBD5. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
An ansamycin antibiotic that inhibits Hsp90, leading to the degradation of its client proteins. The subsequent protein degradation stress could lead to a compensatory upregulation of ubiquitin ligases such as KBTBD5 to manage the destabilized proteins. | ||||||
Linagliptin | 668270-12-0 | sc-364721 sc-364721A | 5 mg 10 mg | $260.00 $426.00 | 2 | |
A specific proteasome inhibitor that binds irreversibly to the N-terminal threonine of proteasomal subunits. This binding impairs proteasomal activity, potentially increasing the cellular requirement for E3 ubiquitin ligases, including KBTBD5, to label proteins for degradation. | ||||||