RNF214 Activators
RNF214 can influence its E3 ubiquitin ligase activity through various mechanisms. Zinc pyrithione serves as a metallochaperone, which can enhance the proper folding and metal coordination required for RNF214's activity. Similarly, MG132, by inhibiting proteasome activity, can lead to the accumulation of ubiquitinated proteins. This accumulation can activate RNF214, as the cell may respond to the increased levels of ubiquitinated proteins by enhancing the ubiquitination process. Additionally, compounds like Thalidomide and PS-341, also known as Bortezomib, are known to disrupt the ubiquitin-proteasome pathway. Thalidomide can promote the degradation of proteins, potentially increasing RNF214 activity in this context. PS-341's role as a proteasome inhibitor can also lead to a feedback mechanism where RNF214 activity is upregulated to deal with the excess of proteins marked for degradation.
Chloroquine disrupts lysosomal function and autophagy, which can lead to increased proteasome-mediated degradation, possibly activating RNF214 to manage the protein load. Withaferin A and Piperlongumine can disrupt proteasomal function and increase reactive oxygen species levels, respectively. These changes can enhance the need for RNF214's ubiquitin ligase activity to maintain protein homeostasis. SMER3, by stimulating autophagy, can enhance the turnover of proteins, indirectly increasing RNF214 activity. Tunicamycin can induce ER stress and the unfolded protein response, which in turn can activate RNF214 to help clear the misfolded proteins. Eeyarestatin I inhibits ER-associated degradation, potentially increasing the demand on RNF214's ligase activity. Lastly, MLN4924 inhibits the NEDD8-activating enzyme and Geldanamycin binds to Hsp90, both of which can destabilize certain proteins, possibly resulting in an increased requirement for RNF214's function in targetin
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc pyrithione can activate RNF214 by serving as a metallochaperone, facilitating the correct folding and metal coordination required for the E3 ubiquitin ligase activity of RNF214. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $56.00 $260.00 $980.00 | 163 | |
MG132 inhibits proteasome activity, which could lead to the accumulation of ubiquitinated proteins, potentially enhancing the E3 ubiquitin ligase activity of RNF214 as part of a compensatory cellular response. | ||||||
Thalidomide | 50-35-1 | sc-201445 sc-201445A | 100 mg 500 mg | $109.00 $350.00 | 8 | |
Thalidomide promotes the degradation of specific proteins via the ubiquitin-proteasome system and could thus enhance the functional activity of RNF214 in the targeted ubiquitination of proteins. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
PS-341, also known as Bortezomib, inhibits the 26S proteasome, which may lead to a feedback activation of upstream E3 ubiquitin ligases like RNF214 to tag more substrates for degradation. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine disrupts lysosomal function and autophagy, which might lead to an increased demand on the proteasome for protein degradation, thereby activating the E3 ubiquitin ligase activity of RNF214. | ||||||
Withaferin A | 5119-48-2 | sc-200381 sc-200381A sc-200381B sc-200381C | 1 mg 10 mg 100 mg 1 g | $127.00 $572.00 $4090.00 $20104.00 | 20 | |
Withaferin A disrupts proteasomal function, which could activate RNF214 by increasing the need for its E3 ubiquitin ligase activity to compensate for compromised proteasome activity. | ||||||
SMER28 | 307538-42-7 | sc-222320 | 10 mg | $173.00 | ||
SMER3 stimulates autophagy and could activate RNF214 by increasing the turnover of cellular proteins, indirectly enhancing the ubiquitination activity of RNF214. | ||||||
Piperlongumine | 20069-09-4 | sc-364128 | 10 mg | $107.00 | ||
Piperlongumine increases the levels of reactive oxygen species within cells, which may indirectly activate RNF214 by oxidative modification of substrate proteins, making them more susceptible to ubiquitination. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin triggers ER stress and the unfolded protein response, which may activate RNF214 by increasing the demand for its E3 ubiquitin ligase activity to ubiquitinate misfolded proteins. | ||||||
Eeyarestatin I | 412960-54-4 | sc-358130B sc-358130 sc-358130A sc-358130C sc-358130D sc-358130E | 5 mg 10 mg 25 mg 50 mg 100 mg 500 mg | $112.00 $199.00 $347.00 $683.00 $1336.00 $5722.00 | 12 | |
Eeyarestatin I inhibits ER-associated degradation (ERAD), which could lead to an upregulation of E3 ubiquitin ligase activity of RNF214 in an attempt to clear the accumulated misfolded proteins. | ||||||