DUB2A Inhibitors
Usp17ld, a thiol-dependent deubiquitinase, is a key player in cellular processes involving protein deubiquitination within the endoplasmic reticulum (ER) membrane. This enzyme, orthologous to human genes such as USP17L2, exhibits a versatile subcellular localization, being active in both the cytosol and nucleus. Its predicted involvement in the regulation of apoptotic processes further underscores its significance in fundamental biological pathways. The enzymatic function of Usp17ld primarily revolves around its ability to cleave ubiquitin molecules from proteins, particularly within the ER membrane. This process of deubiquitination is crucial for maintaining cellular homeostasis by regulating the degradation and stability of proteins involved in various cellular functions. Usp17ld's participation in protein deubiquitination within the ER membrane positions it at the crossroads of essential cellular processes, influencing the fate of key proteins and, consequently, impacting cellular homeostasis. The predicted involvement in apoptotic regulation suggests a broader role in cell fate decisions, linking Usp17ld to processes fundamental for cell survival and death.
Inhibition of Usp17ld encompasses a diverse set of mechanisms, as indicated by the array of inhibitors outlined in the table. These inhibitors target the thiol-dependent deubiquitinase activity of Usp17ld, disrupting its enzymatic function and impeding the cleavage of ubiquitin from target proteins within the ER membrane. Some inhibitors act directly on Usp17ld, preventing its catalytic activity and thereby altering cellular processes related to protein homeostasis and apoptotic regulation. Others, classified as indirect inhibitors, impact cellular processes downstream of Usp17ld, such as autophagy or specific signaling pathways, indirectly influencing its thiol-dependent deubiquitinase activity. This multi-faceted approach to inhibition highlights the intricacies of Usp17ld's regulatory role in cellular functions and offers avenues for further exploration into its biological significance.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
WP1130 | 856243-80-6 | sc-364650 sc-364650A | 10 mg 50 mg | $480.00 $1455.00 | 1 | |
Thiol-dependent deubiquitinase inhibitor impacting Usp17ld. WP1130 disrupts the function of Usp17ld, preventing thiol-dependent deubiquitination. This inhibition hampers the enzymatic activity essential for protein deubiquitination within the endoplasmic reticulum membrane and potentially influences apoptotic processes. | ||||||
P005091 | 882257-11-6 | sc-478535 | 10 mg | $155.00 | ||
Usp inhibitor affecting protein deubiquitination. P5091 inhibits Usp17ld, disrupting its thiol-dependent deubiquitinase activity. The inhibition impedes Usp17ld's role in deubiquitinating proteins, potentially influencing cellular processes related to protein homeostasis within the endoplasmic reticulum membrane and apoptotic regulation. | ||||||
NSC697923 | 343351-67-7 | sc-391107 sc-391107A | 1 mg 5 mg | $15.00 $51.00 | 3 | |
Deubiquitinase inhibitor influencing Usp17ld. NSC697923 disrupts thiol-dependent deubiquitination, inhibiting Usp17ld and preventing its enzymatic activity. This inhibition impacts protein deubiquitination processes within the endoplasmic reticulum membrane, potentially altering cellular homeostasis and apoptotic regulation. | ||||||
IU1 | 314245-33-5 | sc-361215 sc-361215A sc-361215B | 10 mg 50 mg 100 mg | $138.00 $607.00 $866.00 | 2 | |
Ubiquitin-specific protease inhibitor affecting Usp17ld. IU1 inhibits Usp17ld, preventing its thiol-dependent deubiquitinase activity. This inhibition hampers the enzymatic processes crucial for protein deubiquitination within the endoplasmic reticulum membrane, potentially influencing apoptotic processes. | ||||||
Spautin-1 | 1262888-28-7 | sc-507306 | 10 mg | $165.00 | ||
Autophagy inhibitor affecting Usp17ld. Spautin-1 disrupts autophagy processes regulated by Usp17ld, indirectly influencing its thiol-dependent deubiquitination activity. This disruption potentially impacts protein deubiquitination within the endoplasmic reticulum membrane, altering cellular homeostasis and apoptotic regulation. | ||||||
UCH-L1 Inhibitor Inhibitor | 668467-91-2 | sc-356182 | 10 mg | $200.00 | 1 | |
Deubiquitinase inhibitor impacting Usp17ld. LDN-57444 disrupts the thiol-dependent deubiquitination activity of Usp17ld, inhibiting its enzymatic function. This inhibition potentially influences protein deubiquitination processes within the endoplasmic reticulum membrane, altering cellular homeostasis and apoptotic regulation. | ||||||
Glucocorticoid Receptor Modulator, CpdA | 14593-25-0 | sc-221677 | 25 mg | $150.00 | 2 | |
Deubiquitinase inhibitor affecting Usp17ld. CpdA disrupts the thiol-dependent deubiquitination activity of Usp17ld, inhibiting its enzymatic function. This inhibition potentially influences protein deubiquitination processes within the endoplasmic reticulum membrane, altering cellular homeostasis and apoptotic regulation. | ||||||
PR 619 | 2645-32-1 | sc-476324 sc-476324A sc-476324B | 1 mg 5 mg 25 mg | $75.00 $184.00 $423.00 | 1 | |
Broad-spectrum deubiquitinase inhibitor affecting Usp17ld. PR-619 disrupts the enzymatic activity of Usp17ld, preventing thiol-dependent deubiquitination. This inhibition potentially alters protein deubiquitination processes within the endoplasmic reticulum membrane, influencing cellular homeostasis and apoptotic regulation. | ||||||
Tyrphostin B42 | 133550-30-8 | sc-3556 | 5 mg | $26.00 | 4 | |
HB-EGF inhibitor impacting cellular processes downstream of Usp17ld. This compound indirectly influences Usp17ld by disrupting HB-EGF signaling, potentially altering protein deubiquitination processes within the endoplasmic reticulum membrane and cellular homeostasis, thus affecting apoptotic regulation. | ||||||