HSPC196 Inhibitors
Certainly, inhibitors of HSPC196 function by disrupting the cellular processes that are crucial for the proper management of this protein. When we talk about compounds such as Geldanamycin, 17-AAG, or Alvespimycin, these are specifically designed to bind to HSP90. HSP90 is a chaperone that assists in the correct folding of various proteins, including HSPC196 if it is among its client proteins. By binding to the ATP-binding domain of HSP90, these inhibitors effectively halt the chaperone's activity. This cessation of function leads to the destabilization and eventual degradation of the proteins that rely on HSP90, which may include HSPC196.
Proteasome inhibitors also play a critical role in the regulation of protein levels within the cell. The proteasome is responsible for the degradation of proteins that are damaged, misfolded, or no longer needed, a process that is usually tagged by ubiquitin. When inhibitors interfere with the proteasome's activity, proteins that should be degraded begin to accumulate. This accumulation can be detrimental to cell health and can also affect the balance of functional HSPC196 within the cell.
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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 | |
Geldanamycin binds to HSP90, a chaperone protein. HSP90 is known to facilitate the correct folding of proteins, including those in the JAK/STAT signaling pathway. HSPC196, requiring proper folding for its activity, would be inhibited by geldanamycin's disruption of HSP90's function, leading to misfolded HSPC196 and reduced activity. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $67.00 $156.00 | 16 | |
17-AAG is an ansamycin antibiotic that also targets HSP90, impairing its chaperone activity. As HSP90 assists in the maturation of a wide array of signaling proteins, its inhibition by 17-AAG could result in the destabilization and degradation of immature HSPC196 proteins, leading to a decrease in functional HSPC196. | ||||||
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 is a steroidal lactone that has been shown to disrupt the function of proteasomes. Proteasomes are responsible for the degradation of misfolded proteins. By inhibiting proteasomes, Withaferin A can cause accumulation of misfolded proteins, which could include misfolded HSPC196, thus indirectly decreasing its functional activity. | ||||||
17-DMAG | 467214-20-6 | sc-202005 | 1 mg | $205.00 | 8 | |
Alvespimycin, another HSP90 inhibitor, works similarly to Geldanamycin and 17-AAG. By binding to HSP90, Alvespimycin prevents the proper folding of client proteins, which includes HSPC196, leading to its functional inhibition due to the lack of mature protein. | ||||||
Triptolide | 38748-32-2 | sc-200122 sc-200122A | 1 mg 5 mg | $90.00 $204.00 | 13 | |
Triptolide is a diterpene triepoxide that inhibits the transcription factor NF-κB. Given that NF-κB can regulate the expression of various genes including those involved in the stress response, Triptolide's action can lead to decreased expression of HSPC196 by limiting transcriptional activation of stress-responsive genes. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
EGCG is a polyphenol found in green tea that has been shown to modulate the activity of HSP70, a chaperone that works in conjunction with HSP90. By modulating HSP70, EGCG can indirectly lead to reduced chaperoning capacity for HSPC196, resulting in its decreased functional activity. | ||||||
Celastrol, Celastrus scandens | 34157-83-0 | sc-202534 | 10 mg | $158.00 | 6 | |
Celastrol is a quinone methide triterpene that disrupts the heat shock response by inhibiting HSP90. This inhibition can lead to a decrease in the folding and maturation of HSPC196, resulting in a reduction of its functional 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 | |
MG-132 is a peptide aldehyde that inhibits proteasomes. By preventing the degradation of ubiquitinated proteins, MG-132 can cause an accumulation of misfolded or damaged proteins, which can include HSPC196, thereby reducing the amount of functional HSPC196. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $110.00 $250.00 $936.00 $50.00 | 33 | |
Quercetin is a flavonoid that has been shown to inhibit the phosphorylation of various proteins. By inhibiting kinases responsible for phosphorylating HSPC196, Quercetin can reduce its functional activity, as proper phosphorylation is necessary for its function. | ||||||
Novobiocin | 303-81-1 | sc-362034 sc-362034A | 5 mg 25 mg | $128.00 $380.00 | ||
Novobiocin is a coumarin antibiotic known to bind to the C-terminal domain of HSP90, interfering with its chaperoning function. This can result in improperly folded HSPC196 proteins and a subsequent decrease in their functional activity. | ||||||