(R)-MG132 is a potent, reversible, and cell-permeable proteasome inhibitor. After treatment for one hour at 100 nM, it inhibits 50% and 31% of proteasome activity in lysates of J558L multiple myeloma cells and EMT6 breast cancer cells, respectively.
CAT No: R1874
CAS No:1211877-36-9
Synonyms/Alias:(R)-MG132;1211877-36-9;(R)-MG-132;Benzyl n-[(2s)-4-methyl-1-[[(2r)-4-methyl-1-[[(2s)-4-methyl-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]carbamate;MFCD28580122;Cbz-L-leu-D-leu-L-leu-H;CHEMBL1090713;SCHEMBL14579851;CHEBI:191090;EX-A7448;HY-13259C;s8410;AKOS030210983;CID 45103781;DA-65432;CS-0021842;MG-132(R), >=95% (HPLC);D-leucinamide, n-[(phenylmethoxy)carbonyl]-l-leucyl-n-[(1s)-1-formyl-3-methylbutyl]-;benzyl N-[(1S)-3-methyl-1-{[(1R)-3-methyl-1-{[(2S)-4-methyl-1-oxopentan-2-yl]carbamoyl}butyl]carbamoyl}butyl]carbamate;Benzyl N-[(2S)-4-methyl-1-[[(2R)-4-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]carbamate; (R)-MG-132;
Chemical Name:benzyl N-[(2S)-4-methyl-1-[[(2R)-4-methyl-1-[[(2S)-4-methyl-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]carbamate
(R)-MG132 is a synthetic peptide aldehyde that functions as a potent, reversible, and cell-permeable proteasome inhibitor. Structurally characterized as the (R)-enantiomer of the well-studied MG132 molecule, it selectively targets the chymotrypsin-like activity of the 26S proteasome complex, a critical component of the ubiquitin-proteasome pathway responsible for regulated protein degradation in eukaryotic cells. The unique stereochemistry of (R)-MG132 imparts distinct biochemical properties, making it a valuable tool for dissecting enantioselective aspects of proteasomal inhibition and protein turnover. Its use in laboratory settings enables researchers to investigate fundamental mechanisms of protein homeostasis, signal transduction, and cellular stress responses, as well as to explore the consequences of impaired proteasome function in various biological systems.
Proteasome inhibition: In biochemical research, (R)-MG132 is widely employed to inhibit the proteolytic activity of the 26S proteasome in cell-based and in vitro assays. By selectively blocking the chymotrypsin-like protease sites, it facilitates the accumulation of ubiquitinated proteins, thereby enabling the study of protein degradation pathways under controlled conditions. This approach is particularly useful for elucidating the role of the proteasome in regulating protein quality control, cell cycle progression, and the turnover of key regulatory proteins.
Ubiquitin-proteasome pathway studies: The compound serves as a critical reagent for dissecting the dynamics of the ubiquitin-proteasome system. By inhibiting proteasomal degradation, researchers can monitor the fate of ubiquitinated substrates, assess the efficiency of ubiquitin ligases, and map the temporal sequence of protein ubiquitination and removal. This application is essential for understanding how cells maintain proteostasis and respond to misfolded or damaged proteins, as well as for identifying novel components or modulators of the pathway.
Cell signaling research: (R)-MG132 is instrumental in probing signal transduction cascades that are regulated by proteasomal degradation of signaling intermediates. Inhibition of the proteasome can stabilize labile transcription factors, kinases, or inhibitors that are otherwise rapidly degraded, thus allowing detailed analysis of their function, regulation, and downstream effects. This application is particularly relevant for studies involving NF-κB signaling, p53 regulation, and other pathways where proteasome-mediated turnover is a key regulatory mechanism.
Apoptosis and stress response analysis: Utilization of (R)-MG132 in cellular models enables the investigation of apoptosis, autophagy, and other stress response pathways that are influenced by impaired protein degradation. By inducing proteotoxic stress and altering the balance of pro- and anti-apoptotic factors, the compound helps researchers delineate the molecular events that underlie cell fate decisions. This is especially valuable in studies of neurodegeneration, cancer biology, and cellular adaptation to environmental stressors.
Enantioselectivity and stereochemical studies: The (R)-enantiomer of MG132 provides a unique opportunity to examine the stereochemical requirements for proteasome inhibition and to compare the biological activities of different enantiomers. Researchers can use (R)-MG132 alongside its (S)-counterpart to assess differential potency, selectivity, and off-target effects, thereby gaining insights into the structure-activity relationships governing proteasome inhibitor function. Such studies are important for the rational design of next-generation proteasome-targeting molecules with improved specificity and reduced side effects.
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