Chemical activators of TRIM40 engage with the protein in various ways to instigate its activation. Zinc Pyrithione, for instance, has an affinity for zinc ions, essential components in the structural makeup of TRIM proteins, due to their zinc-binding domains. When Zinc Pyrithione chelates zinc, it can induce structural modifications that lead to TRIM40 becoming active. Similarly, Piperlongumine acts on TRIM40 by targeting thiol groups within cysteine residues. Since TRIM40 features these cysteine-rich regions, Piperlongumine can bond covalently, altering the protein's conformation and, consequently, its functional state. In the case of Arsenic Trioxide, its primary mode of interaction is with the cysteine residues in the RING domain of TRIM proteins, which could affect TRIM40's E3 ubiquitin ligase activity, a critical aspect of its function.
Moreover, compounds like MG132 and Bortezomib, which are proteasome inhibitors, contribute to the elevation of ubiquitinated proteins within the cell. This accumulation can indirectly activate TRIM40, potentially escalating its E3 ligase activity to manage the heightened load of ubiquitin-protein conjugates and maintain cellular equilibrium. On the other hand, Sulforaphane and Menadione provoke oxidative stress, which often triggers a defensive cellular reaction, including the activation of TRIM proteins like TRIM40, to counteract oxidative damage. Tunicamycin's role is to induce endoplasmic reticulum (ER) stress and the unfolded protein response (UPR), circumstances under which TRIM40 activation may be a part of the cellular adaptative mechanisms to manage protein quality control. Lithium Chloride, through its inhibition of GSK-3beta, may engage TRIM40 activation as part of the response to the upregulated Wnt/beta-catenin signaling pathway. Other compounds such as Leptomycin B, which affects protein nuclear export, and Parthenolide, which inhibits NF-kappaB signaling, may also activate TRIM40 as the protein responds to changes in protein trafficking and inflammation signaling pathways, respectively. Each of these chemicals engages with TRIM40 in a unique manner, prompting its activation and influencing its regulatory role within the cell.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
This compound can activate TRIM40 by chelating zinc ions, which may be critical for the structural integrity and function of many TRIM proteins as they often contain zinc-binding domains. The binding of Zinc Pyrithione could lead to conformational changes in TRIM40 that result in its activation. | ||||||
Piperlongumine | 20069-09-4 | sc-364128 | 10 mg | $107.00 | ||
Piperlongumine can activate TRIM40 through its ability to modify thiol groups in cysteine residues, which can result in the alteration of protein conformation and function. As TRIM40 contains cysteine-rich domains, Piperlongumine can lead to the activation of TRIM40 through direct covalent interactions. | ||||||
Arsenic(III) oxide | 1327-53-3 | sc-210837 sc-210837A | 250 g 1 kg | $87.00 $224.00 | ||
Arsenic Trioxide can lead to the activation of TRIM40 since it influences the ubiquitination process by binding to cysteine residues within the RING domain of TRIM proteins. This interaction could potentially activate TRIM40 by affecting its E3 ubiquitin ligase activity, which is a function associated with many TRIM proteins. | ||||||
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 is a proteasome inhibitor that can increase the levels of ubiquitinated proteins. This buildup can activate TRIM40 indirectly as it may enhance the need for TRIM40's E3 ligase activity to regulate ubiquitin-protein conjugates, leading to an increase in TRIM40 activation to restore homeostasis. | ||||||
D,L-Sulforaphane | 4478-93-7 | sc-207495A sc-207495B sc-207495C sc-207495 sc-207495E sc-207495D | 5 mg 10 mg 25 mg 1 g 10 g 250 mg | $150.00 $286.00 $479.00 $1299.00 $8299.00 $915.00 | 22 | |
Sulforaphane can activate TRIM40 by inducing oxidative stress, which often triggers a cascade of cellular defense mechanisms including the activation of TRIM proteins involved in proteostasis. TRIM40 activation may occur as a part of the cell's response to counteract the effects of oxidative damage. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $169.00 $299.00 | 66 | |
Tunicamycin causes ER stress by inhibiting N-linked glycosylation, leading to the unfolded protein response (UPR). TRIM40 activation may occur as part of the cellular adaptive mechanisms to UPR, given that TRIM proteins are known to be involved in protein quality control. | ||||||
Bortezomib | 179324-69-7 | sc-217785 sc-217785A | 2.5 mg 25 mg | $132.00 $1064.00 | 115 | |
Bortezomib is another proteasome inhibitor that leads to the accumulation of ubiquitinated proteins. TRIM40 activation could occur as it may play a role in the cellular response to the increased levels of ubiquitinated proteins, enhancing its activity to help degrade misfolded proteins. | ||||||
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium Chloride can activate the Wnt/beta-catenin signaling pathway by inhibiting GSK-3beta. Since TRIM proteins have been implicated in modulating this pathway, TRIM40 could be functionally activated as part of the cellular response to heightened Wnt signaling, potentially by regulating the degradation of pathway components. | ||||||
Vitamin K3 | 58-27-5 | sc-205990B sc-205990 sc-205990A sc-205990C sc-205990D | 5 g 10 g 25 g 100 g 500 g | $25.00 $35.00 $46.00 $133.00 $446.00 | 3 | |
Menadione induces oxidative stress and could activate TRIM40 as a cellular defense mechanism, similar to other stress conditions that provoke a response from TRIM proteins. The activation of TRIM40 could be a part of the cellular adaptive processes to mitigate oxidative damage. | ||||||
Thalidomide | 50-35-1 | sc-201445 sc-201445A | 100 mg 500 mg | $109.00 $350.00 | 8 | |
Thalidomide and its analogs are known to induce the degradation of specific proteins. TRIM40 could be activated by such compounds to modulate its E3 ubiquitin ligase activity, as part of the cellular process to regulate protein levels and maintain cellular homeostasis. | ||||||