TID-1L inhibitors are a class of chemical compounds that have garnered significant attention in the realm of molecular biology and biochemistry due to their pivotal role in the modulation of specific cellular processes. TID-1L, short for Tumor Necrosis Factor Receptor-Associated Protein 1-Like, is a protein found within the cells of various organisms, particularly in mammals. It belongs to the Hsp40 co-chaperone family, which functions in conjunction with heat shock proteins (Hsps) to assist in protein folding, stabilization, and transport. TID-1L itself plays a crucial part in the regulation of protein homeostasis and, by extension, cellular function.
TID-1L inhibitors are designed to interfere with the normal function of TID-1L, thereby affecting various cellular pathways and molecular interactions. These inhibitors can target specific domains or sites on the TID-1L protein, preventing its binding to other proteins or altering its conformation. By doing so, they disrupt the intricate network of chaperone-mediated processes, affecting protein folding and degradation, which can lead to a cascade of downstream effects on cellular homeostasis. Scientists and researchers employ these inhibitors to dissect the complex mechanisms underlying protein quality control, cellular stress responses, and the progression of various diseases, providing valuable insights into the fundamental biology of the cell. This class of inhibitors continues to be a subject of extensive investigation, contributing to our understanding of the intricacies of cellular function and offering potential avenues for further research and drug development.
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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 | $39.00 $59.00 $104.00 $206.00 | 8 | |
Binds to the N-terminal ATP-binding pocket of Hsp90, preventing its chaperone function and leading to client protein degradation. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
A derivative of Geldanamycin, also inhibits Hsp90 by disrupting its ATPase activity, destabilizing client proteins. | ||||||
Radicicol | 12772-57-5 | sc-200620 sc-200620A | 1 mg 5 mg | $92.00 $333.00 | 13 | |
Inhibits Hsp90 by binding to its N-terminal ATPase domain, preventing proper folding and function of client proteins. | ||||||
NVP-AUY922 | 747412-49-3 | sc-364551 sc-364551A sc-364551B sc-364551C sc-364551D sc-364551E | 5 mg 25 mg 100 mg 250 mg 1 g 5 g | $150.00 $263.00 $726.00 $1400.00 $2900.00 $11000.00 | 3 | |
Disrupts Hsp90 function by binding to the ATP-binding site, destabilizing client proteins leading to their degradation. | ||||||
17-DMAG, Hydrochloride Salt | 467214-21-7 | sc-396751 | 25 mg | $312.00 | ||
Inhibits Hsp90 by competing for the ATP-binding pocket, leading to the degradation of client proteins. | ||||||
5-Iodotubercidin | 24386-93-4 | sc-3531 sc-3531A | 1 mg 5 mg | $153.00 $464.00 | 20 | |
Inhibits CDK2 and CDK9, affecting cell cycle progression and transcription, potentially impacting Tid-1L function. | ||||||
BIIB 021 | 848695-25-0 | sc-364434 sc-364434A | 5 mg 25 mg | $128.00 $650.00 | ||
Binds to Hsp90, disrupting its chaperone function and leading to the degradation of client proteins in cancer cells. | ||||||
ZM-447439 | 331771-20-1 | sc-200696 sc-200696A | 1 mg 10 mg | $153.00 $356.00 | 15 | |
Targets Hsp90, inhibiting its ATPase activity, promoting client protein degradation, and impacting cellular processes. | ||||||
Debio 0932 | 1061318-81-7 | sc-507516 | 10 mg | $280.00 | ||
Affects Hsp90 function by binding to its ATP-binding site, causing client protein destabilization and degradation. | ||||||