TID-1 refers to a human protein that is a member of the Hsp40 (Heat Shock Protein 40) family, also known as DNAJA3, which acts as a co-chaperone involved in mitochondrial import and the unfolded protein response. However, the identification and description of chemical activators for TID-1 are not part of the well-established scientific literature.
In general, activators of proteins are usually small molecules, peptides, or other biologic agents that bind to the protein in question and increase its biological activity. If TID-1 Activators would interact directly with the TID-1 protein to enhance its function as a molecular chaperone. This could involve stabilizing a more active form of the protein, promoting its interaction with other proteins or substrates, or enhancing its ability to facilitate the correct folding of other proteins. To speculate based on the common patterns of protein activators, such TID-1 Activators would be valuable tools in cell biology and biochemistry for probing the cellular functions of TID-1. They could help clarify the role of TID-1 in mitochondrial function, protein homeostasis, and the response to cellular stress conditions. By manipulating the activity of TID-1 in a controlled manner, researchers could gain insights into the molecular mechanisms of protein folding and the maintenance of cellular health in the context of the complex environment of the cell. It would also allow for the exploration of the network of interactions in which TID-1 is involved, including its co-chaperones and the substrates it helps to fold and transport.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Geldanamycin | 30562-34-6 | sc-200617B sc-200617C sc-200617 sc-200617A | 100 µg 500 µg 1 mg 5 mg | $38.00 $58.00 $102.00 $202.00 | 8 | |
Geldanamycin binds to Heat Shock Protein 90 (Hsp90) and inhibits its chaperone activity, which leads to the degradation of proteins that require Hsp90 for stability. TID-1, a co-chaperone of Hsp70, can have its activity enhanced as the cellular stress response shifts to compensate for the inhibited Hsp90 pathway. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $66.00 $153.00 | 16 | |
17-AAG is an Hsp90 inhibitor similar to Geldanamycin. By inhibiting Hsp90, it disrupts its chaperone function, causing a compensatory increase in Hsp70 activity. As TID-1 is an Hsp70 co-chaperone, this indirectly enhances TID-1 functional activity as part of the stress response. | ||||||
Methylene blue | 61-73-4 | sc-215381B sc-215381 sc-215381A | 25 g 100 g 500 g | $42.00 $102.00 $322.00 | 3 | |
Methylene Blue acts as an alternative electron acceptor in the mitochondrial electron transport chain, which can reduce oxidative stress. By modulating mitochondrial function, it may indirectly enhance TID-1 activity due to TID-1's role in maintaining mitochondrial integrity and apoptosis regulation. | ||||||
2-Deoxy-D-glucose | 154-17-6 | sc-202010 sc-202010A | 1 g 5 g | $65.00 $210.00 | 26 | |
2-Deoxy-D-glucose is a glucose analog that inhibits glycolysis. By simulating a state of energy deprivation, it can activate AMP-activated protein kinase (AMPK), which can lead to an upregulation of cellular stress response pathways, indirectly enhancing the activity of TID-1 as the cell attempts to restore homeostasis. | ||||||
Oltipraz | 64224-21-1 | sc-205777 sc-205777A | 500 mg 1 g | $286.00 $622.00 | ||
Oltipraz upregulates the expression of phase II detoxification enzymes via the Nrf2 pathway. Nrf2 activation can lead to an increased cellular stress response, potentially increasing the demand for molecular chaperones, including TID-1, to maintain protein homeostasis. | ||||||
Curcumin | 458-37-7 | sc-200509 sc-200509A sc-200509B sc-200509C sc-200509D sc-200509F sc-200509E | 1 g 5 g 25 g 100 g 250 g 1 kg 2.5 kg | $36.00 $68.00 $107.00 $214.00 $234.00 $862.00 $1968.00 | 47 | |
Curcumin is known to induce heat shock response by upregulating heat shock proteins. This upregulation could indirectly enhance the activity of TID-1 by increasing the pool of co-chaperones and chaperones, including Hsp70 with which TID-1 associates, to cope with enhanced protein folding demand. | ||||||
Salubrinal | 405060-95-9 | sc-202332 sc-202332A | 1 mg 5 mg | $33.00 $102.00 | 87 | |
Salubrinal selectively inhibits dephosphorylation of eukaryotic translation initiation factor 2 alpha (eIF2α), leading to an enhanced stress response. This may indirectly increase TID-1 activity as part of the cellular effort to manage misfolded protein accumulation. | ||||||
D-(+)-Trehalose Anhydrous | 99-20-7 | sc-294151 sc-294151A sc-294151B | 1 g 25 g 100 g | $29.00 $164.00 $255.00 | 2 | |
Trehalose is a disaccharide that has been shown to enhance autophagy. Through the activation of autophagy, cellular stress responses are heightened, which can lead to an increased requirement for molecular chaperones including TID-1 to handle misfolded or aggregated proteins. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $155.00 | 6 | |
Celastrol triggers heat shock response by increasing the expression of heat shock proteins. This response may indirectly enhance the activity of TID-1 by facilitating its role as an Hsp70 co-chaperone during periods of increased cellular stress and protein misfolding. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
1-Hydroxypyridine-2-thione zinc salt induces oxidative stress, which can lead to a cellular compensatory increase in stress response pathways, including the upregulation of molecular chaperones. Subsequently, TID-1 activity may be enhanced as part of the cell's defense mechanism against oxidative damage. | ||||||