CLPX Inhibitors
Chemical inhibitors of CLPX can exert their inhibitory effects through various mechanisms that interfere with the protein's functional pathways. Hsp70 inhibitors such as pifithrin-μ and Ver-155008 disrupt the collaboration between CLPX and the Hsp70 family of proteins, which is essential for proper protein degradation. Since CLPX works closely with Hsp70 proteins, the inhibition of these chaperones results in a downstream inhibition of CLPX's role in protein processing. Proteasome inhibitors like MG132 and Lactacystin cause an accumulation of polyubiquitinated proteins, which burdens the protein degradation pathways and indirectly prevents CLPX from performing its function effectively. This is because the proteostasis network, which includes the proteasome system, is interconnected, and dysregulation of one component can affect the others.
Other inhibitors, such as Concanamycin A and Bafilomycin A1, disrupt cellular compartments by inhibiting V-ATPases, impairing the acidic environment required for lysosomal and proteasomal degradation. Since the functional integrity of CLPX is dependent on these cellular processes, their disruption can lead to a reduction in CLPX activity. Lastly, inhibitors like EerI and Epoxomicin interfere with specific degradation pathways such as ER-associated degradation (ERAD) and the ubiquitin-proteasome system, respectively. By doing so, they indirectly hinder the role of CLPX within these pathways, leading to its functional inhibition.
Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Pifithrin-μ | 64984-31-2 | sc-203195 sc-203195A | 10 mg 50 mg | $127.00 $372.00 | 4 | |
Pifithrin-μ is known to inhibit Hsp70 family protein activity. As CLPX works in conjunction with Hsp70 family proteins in protein degradation pathways, inhibition of Hsp70 can indirectly inhibit the functional activity of CLPX. | ||||||
17-AAG | 75747-14-7 | sc-200641 sc-200641A | 1 mg 5 mg | $66.00 $153.00 | 16 | |
17-AAG is an Hsp90 inhibitor, and by destabilizing Hsp90 client proteins, it can indirectly inhibit CLPX function by disrupting the protein degradation pathways that CLPX is involved in. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc pyrithione can inhibit the function of multiple chaperone proteins. CLPX, being a chaperone-associated protein, may be indirectly inhibited due to disruption of the chaperone-mediated protein folding and degradation processes. | ||||||
VER 155008 | 1134156-31-2 | sc-358808 sc-358808A | 10 mg 50 mg | $199.00 $825.00 | 9 | |
This is an inhibitor of Hsp70 family proteins. By inhibiting these proteins, the associated functioning of CLPX, which relies on Hsp70 for its chaperone-mediated activities, would be indirectly inhibited. | ||||||
Concanamycin A | 80890-47-7 | sc-202111 sc-202111A sc-202111B sc-202111C | 50 µg 200 µg 1 mg 5 mg | $65.00 $162.00 $650.00 $2550.00 | 109 | |
As an inhibitor of V-ATPases, Concanamycin A disrupts proton gradients across membranes, affecting cellular compartments and processes, including those involving CLPX, which relies on proper cellular compartmentalization for its function. | ||||||
Oligomycin A | 579-13-5 | sc-201551 sc-201551A sc-201551B sc-201551C sc-201551D | 5 mg 25 mg 100 mg 500 mg 1 g | $175.00 $600.00 $1179.00 $5100.00 $9180.00 | 26 | |
By inhibiting ATP synthase, Oligomycin A decreases the availability of ATP within the cell. Because CLPX requires ATP for its function, this reduction in ATP can indirectly inhibit CLPX activity. | ||||||
Bafilomycin A1 | 88899-55-2 | sc-201550 sc-201550A sc-201550B sc-201550C | 100 µg 1 mg 5 mg 10 mg | $96.00 $250.00 $750.00 $1428.00 | 280 | |
This inhibitor of V-ATPases can disrupt cellular proton gradients and acidification essential for lysosomal and proteasomal degradation, processes that are interconnected with the function of CLPX. | ||||||
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 | |
This proteasome inhibitor can lead to the accumulation of polyubiquitinated proteins, which can saturate the protein degradation pathways and indirectly inhibit the function of chaperone proteins like CLPX. | ||||||
Eeyarestatin I | 412960-54-4 | sc-358130B sc-358130 sc-358130A sc-358130C sc-358130D sc-358130E | 5 mg 10 mg 25 mg 50 mg 100 mg 500 mg | $112.00 $199.00 $347.00 $683.00 $1336.00 $5722.00 | 12 | |
EerI inhibits ER-associated degradation (ERAD) by disrupting p97 ATPase, which is involved in the retrotranslocation of proteins from the ER. As CLPX is associated with protein degradation, inhibiting ERAD can indirectly affect CLPX's function. | ||||||
Epoxomicin | 134381-21-8 | sc-201298C sc-201298 sc-201298A sc-201298B | 50 µg 100 µg 250 µg 500 µg | $134.00 $215.00 $440.00 $496.00 | 19 | |
A specific proteasome inhibitor that can lead to an accumulation of proteins meant for degradation, indirectly affecting the functionality of CLPX by overwhelming the protein degradation pathways it is part of. | ||||||