Date published: 2026-2-1

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Proteasome Inhibitor II

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Alternate Names:
Z-LLF-CHO
Application:
Proteasome Inhibitor II is a potent, cell-permeable, and reversible proteasome inhibitor
Purity:
≥95%
Molecular Weight:
509.7
Molecular Formula:
C29H39N3O5
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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Proteasome Inhibitor II has emerged as a crucial tool in scientific research, particularly within the field of proteasome biology and protein degradation studies. This compound operates by selectively targeting and inhibiting the activity of the proteasome, a multi-subunit protein complex responsible for the degradation of intracellular proteins. Its mechanism of action involves reversible binding to the catalytic sites of the proteasome, thereby preventing substrate recognition and degradation. Research utilizing Proteasome Inhibitor II has provided valuable insights into the regulation of protein turnover, cellular homeostasis, and various signaling pathways. Furthermore, this inhibitor has been instrumental in elucidating the role of the proteasome in cellular processes such as cell cycle progression, apoptosis, and immune responses. Additionally, Proteasome Inhibitor II has been employed in studies investigating the pathophysiology of diseases characterized by dysregulated proteasome function, including cancer, neurodegenerative disorders, and inflammatory diseases. Its specificity and efficacy in modulating proteasome activity make Proteasome Inhibitor II an indispensable tool for deciphering the complex mechanisms underlying protein degradation and for identifying novel targets for proteasome-related diseases.


Proteasome Inhibitor II References

  1. Tumor necrosis factor-related apoptosis inducing ligand expression and activity in hen granulosa cells.  |  Johnson, AL., et al. 2007. Reproduction. 133: 609-16. PMID: 17379655
  2. Inhibition of proteasome activity sensitizes human granulosa tumor cells to TRAIL-induced cell death.  |  Woods, DC., et al. 2008. Cancer Lett. 260: 20-7. PMID: 18031928
  3. NF-kappaB inhibitors induce lytic cytotoxicity in Epstein-Barr virus-positive nasopharyngeal carcinoma cells.  |  Liu, SF., et al. 2008. Cell Biol Int. 32: 1006-13. PMID: 18579417
  4. Profiling drug-induced cell death pathways in the zebrafish lateral line.  |  Coffin, AB., et al. 2013. Apoptosis. 18: 393-408. PMID: 23413197
  5. Cytotoxic effects of NF‑κB inhibitors in combination with anti‑herpes agents on Epstein‑Barr virus‑positive gastric carcinoma in vitro.  |  Ordonez, P., et al. 2016. Mol Med Rep. 14: 2359-67. PMID: 27430429
  6. Use of zebrafish larvae lateral line to study protection against cisplatin-induced ototoxicity: A scoping review.  |  Domarecka, E., et al. 2020. Int J Immunopathol Pharmacol. 34: 2058738420959554. PMID: 33084473
  7. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids.  |  Orlowski, M., et al. 1993. Biochemistry. 32: 1563-72. PMID: 8431436
  8. Reactions of [14C]-3,4-dichloroisocoumarin with subunits of pituitary and spleen multicatalytic proteinase complexes (proteasomes).  |  Orlowski, M., et al. 1997. Biochemistry. 36: 13946-53. PMID: 9374874
  9. Dominant signals leading to inhibitor kappaB protein degradation mediate CD40 ligand rescue of WEHI 231 immature B cells from receptor-mediated apoptosis.  |  Schauer, SL., et al. 1998. J Immunol. 160: 4398-405. PMID: 9574544
  10. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor.  |  Orlowski, RZ., et al. 1998. Cancer Res. 58: 4342-8. PMID: 9766662

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

Proteasome Inhibitor II, 1 mg

sc-301618
1 mg
$55.00

Proteasome Inhibitor II, 5 mg

sc-301618A
5 mg
$176.00