4933422H20Rik Activators
Chemical activators of tripartite motif-containing 80 (TRIM80) include various compounds that can influence its E3 ubiquitin ligase activity through different mechanisms. Zinc pyrithione engages with TRIM80 by enhancing its zinc-binding ability, which is crucial for maintaining the protein's structural integrity and function. This interaction can prompt a conformational change in TRIM80, activating its E3 ubiquitin ligase activity. Similarly, MG132, by inhibiting proteasomes, causes an accumulation of ubiquitinated proteins, which indirectly activates TRIM80 by increasing the substrates for its E3 ligase function. Leptomycin B, through its inhibition of nuclear export, leads to the nuclear retention of TRIM80, potentially facilitating its interaction with nuclear substrates and enhancing its ligase activity. On another front, thalidomide, known for promoting the degradation of specific proteins, can recruit TRIM80 to the E3 ligase complex, elevating its ubiquitination activity.
Further, Chloroquine activates TRIM80 by disrupting the lysosomal acidification, indirectly bolstering the protein's role in the turnover of other proteins. Withaferin A binds to co-chaperones associated with heat shock proteins, which can aid in the proper folding and stabilization of TRIM80, augmenting its ligase function. Piperlongumine raises intracellular levels of reactive oxygen species, which can activate TRIM80 via oxidative modifications that enhance its ligase activity. Disulfiram's ability to chelate zinc ions might modify TRIM80's structure, thereby facilitating a more effective substrate binding and ubiquitination process. Moreover, MLN4924, by inhibiting the NEDD8-activating enzyme, leads to an increased presence of neddylated proteins, which may serve as substrates for TRIM80's ligase activity. In the context of cellular stress, tunicamycin triggers the unfolded protein response, where the demand for E3 ligases, including TRIM80, is elevated to degrade misfolded proteins. Lastly, geldanamycin, by binding to HSP90, can free TRIM80 from HSP90 complexes, potentially enhancing its availability for ubiquitination processes. Meanwhile, dimethyloxalylglycine stabilizes hypoxia-inducible factors, thus inducing a state that can modify TRIM80's activity as part of the cell's response to hypoxic conditions.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc pyrithione can activate tripartite motif-containing 80 by binding to the protein and enhancing its ability to coordinate zinc, which is necessary for the structural integrity and function of many TRIM proteins. This coordination can catalyze the conformational change required for the activation of its E3 ubiquitin ligase activity. | ||||||
MG-132 [Z-Leu- Leu-Leu-CHO] | 133407-82-6 | sc-201270 sc-201270A sc-201270B | 5 mg 25 mg 100 mg | $60.00 $265.00 $1000.00 | 163 | |
MG132 inhibits proteasomes, which can lead to an accumulation of ubiquitinated proteins, indirectly activating tripartite motif-containing 80 by increasing the substrates available for its E3 ubiquitin ligase function, thereby enhancing its activity within the ubiquitin-proteasome pathway. | ||||||
Leptomycin B | 87081-35-4 | sc-358688 sc-358688A sc-358688B | 50 µg 500 µg 2.5 mg | $107.00 $416.00 $1248.00 | 35 | |
Leptomycin B inhibits nuclear export by binding to exportin 1, which could lead to the nuclear accumulation of proteins including tripartite motif-containing 80, promoting its activation by facilitating interactions with nuclear substrates or partners necessary for its ubiquitin ligase activity. | ||||||
Thalidomide | 50-35-1 | sc-201445 sc-201445A | 100 mg 500 mg | $111.00 $357.00 | 8 | |
Thalidomide and its derivatives promote the degradation of specific substrates by the E3 ubiquitin ligase complex. This can activate tripartite motif-containing 80 by recruiting it to the E3 ligase complex, thereby enhancing its ligase activity. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $69.00 | 2 | |
Chloroquine can activate tripartite motif-containing 80 by alkalizing the intracellular environment, specifically within lysosomes. This alkalization can interfere with protein degradation pathways, indirectly enhancing the role of E3 ubiquitin ligases like tripartite motif-containing 80 in protein turnover. | ||||||
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 binds to and activates co-chaperones that interact with heat shock proteins (HSPs), which can activate tripartite motif-containing 80 by facilitating its proper folding and stabilization, enhancing its E3 ligase activity. | ||||||
Piperlongumine | 20069-09-4 | sc-364128 | 10 mg | $107.00 | ||
Piperlongumine increases reactive oxygen species (ROS) levels, which can activate tripartite motif-containing 80 by modifying the oxidative state within the cell, potentially enhancing the protein's ligase activity through redox-sensitive cysteine modifications in its structure. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Disulfiram can activate tripartite motif-containing 80 by chelating zinc ions, potentially leading to alterations in the structure of the protein that enhance its E3 ubiquitin ligase activity through a more favorable conformation for substrate binding and ubiquitination. | ||||||
MLN 4924 | 905579-51-3 | sc-484814 | 1 mg | $286.00 | 1 | |
MLN4924 inhibits the NEDD8-activating enzyme, leading to the buildup of neddylated proteins. This can activate tripartite motif-containing 80 by increasing the number of substrates available for its E3 ligase activity, as neddylated proteins often require ubiquitination for their processing or degradation. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tunicamycin inhibits N-linked glycosylation, which can activate tripartite motif-containing 80 by causing ER stress and the unfolded protein response (UPR), during which the demand for E3 ubiquitin ligase activity is increased to help degrade misfolded proteins, thereby possibly enhancing the activity of tripartite motif-containing 80. | ||||||