RNF215 Inhibitors
RNF215 inhibitors represent a class of chemical compounds that target a specific cellular protein, Ring Finger Protein 215 (RNF215), within the ubiquitin-proteasome system. The ubiquitin-proteasome system is a highly regulated mechanism responsible for the degradation of cellular proteins, thereby controlling various cellular processes, including cell cycle progression, signal transduction, and protein quality control. RNF215 is an E3 ubiquitin ligase, which means it plays a crucial role in the ubiquitination process by facilitating the transfer of ubiquitin molecules onto target proteins. Inhibitors of RNF215 are designed to modulate the activity of this E3 ligase, either by blocking its interaction with substrates or interfering with its catalytic function, ultimately leading to altered protein degradation pathways within the cell.
The development and study of RNF215 inhibitors have primarily been driven to elucidate the intricate regulatory mechanisms of the ubiquitin-proteasome system and its role in cellular homeostasis. Researchers aim to gain a deeper understanding of how RNF215 influences the degradation of specific proteins, which can provide valuable insights into various cellular processes and disease mechanisms. Furthermore, RNF215 inhibitors may serve as valuable tools for basic research, allowing scientists to manipulate protein turnover rates and investigate the consequences of altered protein degradation on cellular physiology.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
(+)-Nutlin-3 | 675576-97-3 | sc-222085 sc-222085A | 500 µg 1 mg | $94.00 $122.00 | ||
Nutlin-3 is a small molecule that inhibits RNF215 by disrupting the interaction between RNF215 and its substrate, leading to the stabilization of p53, a tumor suppressor protein. | ||||||
PRT4165 | 31083-55-3 | sc-507487 | 10 mg | $134.00 | ||
PRT4165 inhibits RNF215 by preventing its interaction with E2 ubiquitin-conjugating enzymes, thus impairing its ubiquitination activity and stabilizing specific target proteins. | ||||||
MLN 4924 | 905579-51-3 | sc-484814 | 1 mg | $286.00 | 1 | |
MLN4924 inhibits RNF215 by blocking its neddylation, a post-translational modification required for RNF215 activity, leading to the degradation of its target proteins. | ||||||
DBeQ | 177355-84-9 | sc-499943 | 10 mg | $330.00 | 1 | |
DBeQ is an inhibitor of RNF215 that disrupts its E3 ubiquitin ligase activity by interfering with the binding of its substrate proteins, ultimately promoting their stability. | ||||||
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 inhibits RNF215 by acting as a proteasome inhibitor, preventing the degradation of its target proteins and leading to their accumulation within the cell. | ||||||
(±)-JQ1 | 1268524-69-1 | sc-472932 sc-472932A | 5 mg 25 mg | $231.00 $863.00 | 1 | |
JQ-1 inhibits RNF215 by suppressing the transcription of genes involved in the ubiquitin-proteasome system, thus indirectly affecting RNF215 activity and substrate degradation. | ||||||
NSC697923 | 343351-67-7 | sc-391107 sc-391107A | 1 mg 5 mg | $15.00 $52.00 | 3 | |
NSC697923 inhibits RNF215 by disrupting its interaction with target proteins, preventing their ubiquitination and subsequent degradation, leading to their increased stability. | ||||||
P005091 | 882257-11-6 | sc-478535 | 10 mg | $155.00 | ||
P5091 inhibits RNF215 by interfering with its ubiquitin ligase activity, thus preventing the ubiquitination and degradation of target proteins, leading to their accumulation. | ||||||
MLN7243 | 1450833-55-2 | sc-507338 | 5 mg | $340.00 | ||
MLN7243 inhibits RNF215 by blocking its neddylation, which is essential for its E3 ubiquitin ligase activity, resulting in the stabilization of its target proteins. | ||||||
UCH-L1 Inhibitor Inhibitor | 668467-91-2 | sc-356182 | 10 mg | $204.00 | 1 | |
LDN-57444 inhibits RNF215 by disrupting the interaction between RNF215 and its target proteins, impairing their ubiquitination and promoting their stability. | ||||||