TRIM64B Inhibitors
Chemical inhibitors of TRIM64B can interfere with the protein's function in a variety of ways, primarily by targeting the proteasomal and lysosomal degradation pathways. Proteasome inhibitors such as MG132, Lactacystin, Epoxomicin, Bortezomib, and Withaferin A obstruct the proteasome's ability to degrade ubiquitinated proteins. Since TRIM64B is thought to be involved in tagging proteins for degradation, the accumulation of these proteins due to the inhibition of the proteasome can lead to an inhibition of TRIM64B function. This is because the normal cycle of tagging and degradation that TRIM64B is a part of is disrupted, leading to an accumulation of proteins that would otherwise be degraded.
Other compounds, such as MLN4924, disrupt processes that are upstream of TRIM64B's role in protein turnover. MLN4924 inhibits the NEDD8-activating enzyme, thus potentially affecting TRIM64B indirectly by altering the regulation of cullin-RING ubiquitin ligases (CRLs) that might be necessary for TRIM64B's function. Lysosomal function disruptors such as Chloroquine, Concanamycin A, Leupeptin, and Pepstatin A, impede different aspects of the lysosomal degradation pathway. Chloroquine and Concanamycin A disrupt lysosomal acidification, whereas Leupeptin and Pepstatin A inhibit lysosomal proteases. Since lysosomal function is crucial for the degradation of cellular components, inhibition of lysosomes can result in an inhibition of TRIM64B if it relies on this pathway. Lastly, O-phenanthroline disrupts metalloprotease activity, which could inhibit TRIM64B if its function is contingent upon metalloprotease-mediated processes. Eeyarestatin I specifically inhibits components of the ER-associated degradation pathway, which could affect TRIM64B if it is involved in this cellular mechanism.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 the proteasome, which is responsible for degrading ubiquitinated proteins. TRIM64B, as a member of the TRIM protein family, is thought to participate in the ubiquitination process. By inhibiting the proteasome, MG132 can lead to the accumulation of substrates that TRIM64B may ubiquitinate, thereby functionally inhibiting TRIM64B's ability to mediate protein degradation. | ||||||
Lactacystin | 133343-34-7 | sc-3575 sc-3575A | 200 µg 1 mg | $165.00 $575.00 | 60 | |
Lactacystin is a specific inhibitor of the proteasome. Given TRIM64B's potential role in protein ubiquitination, the inhibition of the proteasome would prevent the degradation of TRIM64B's substrates, thereby inhibiting its functional role in the cell. | ||||||
Epoxomicin | 134381-21-8 | sc-201298C sc-201298 sc-201298A sc-201298B | 50 µg 100 µg 250 µg 500 µg | $134.00 $215.00 $440.00 $496.00 | 19 | |
Epoxomicin selectively inhibits the proteasome, and by doing so, it can inhibit the degradation of proteins that TRIM64B may target for ubiquitination. This would result in a functional inhibition of TRIM64B by preventing it from fulfilling its role in protein turnover. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
Bortezomib is a proteasome inhibitor used to block the degradation of ubiquitinated proteins. By blocking the proteasome, Bortezomib can inhibit the degradation of proteins targeted by TRIM64B, thereby inhibiting the functional activity of TRIM64B in the ubiquitin-proteasome pathway. | ||||||
ATM/ATR Kinase Inhibitor Inhibitor | 905973-89-9 | sc-202964 | 5 mg | $104.00 | 8 | |
MLN4924 inhibits the NEDD8-activating enzyme, which is crucial for the neddylation process that affects the activity of cullin-RING ubiquitin ligases (CRLs). TRIM64B, if it interacts with CRLs or is regulated by neddylation, would be functionally inhibited by MLN4924 due to the suppression of this post-translational modification that is essential for its activity. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine disrupts lysosomal function by raising the lysosomal pH. If TRIM64B has a role in lysosome-related degradation pathways or is dependent on a lysosomal function for its activity, the inhibition of lysosomes by Chloroquine would lead to a functional inhibition of TRIM64B. | ||||||
Concanamycin A | 80890-47-7 | sc-202111 sc-202111A sc-202111B sc-202111C | 50 µg 200 µg 1 mg 5 mg | $65.00 $162.00 $650.00 $2550.00 | 109 | |
Concanamycin A inhibits the V-ATPase proton pump, which is essential for acidification within lysosomes. Since lysosomal degradation is crucial for the turnover of certain cellular components, and if TRIM64B's function is connected to this process, inhibiting lysosomal acidification would functionally inhibit TRIM64B. | ||||||
Leupeptin hemisulfate | 103476-89-7 | sc-295358 sc-295358A sc-295358D sc-295358E sc-295358B sc-295358C | 5 mg 25 mg 50 mg 100 mg 500 mg 10 mg | $72.00 $145.00 $265.00 $489.00 $1399.00 $99.00 | 19 | |
Leupeptin acts as an inhibitor of certain proteases within the lysosome. If TRIM64B's function is related to the activation of these proteases or is dependent on proteolytic processes within lysosomes, Leupeptin would inhibit TRIM64B's role in these processes. | ||||||
o-Phenanthroline monohydrate | 5144-89-8 | sc-202256 sc-202256A | 1 g 25 g | $42.00 $184.00 | 1 | |
O-phenanthroline is an inhibitor of metalloproteases. If TRIM64B's function is associated with the activity of metalloproteases, such as in the processing of proteins or signaling pathways that involve metalloprotease activity, the inhibition by O-phenanthroline would result in the functional inhibition of TRIM64B. | ||||||
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 is known to disrupt proteasomal activity. If TRIM64B's role involves the regulation of proteasomal degradation, Withaferin A would inhibit this process and therefore functionally inhibit TRIM64B by preventing the degradation of its ubiquitinated targets. | ||||||