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E-64-d (CAS 88321-09-9)

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Alternate Names:
E-64-d is also known as Aloxistatin.
Application:
E-64-d is a potent lysosome and cell permeable inhibitor of thiol protease and cathepsin B, H, and L.
CAS Number:
88321-09-9
Purity:
≥98%
Molecular Weight:
342.43
Molecular Formula:
C17H30N2O5
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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E-64-d is a derivative of the membrane permeant E-64c (sc-201278) and acts as a potent inhibitor of thiol protease. It can permeate an intact cell and block the activity of calpain, which results in the protection of protein kinase C (PKC) from proteolysis. E-64-d is also a cathepsin B, cathepsin H, and cathepsin L inhibitor. Research shows that E-64-d can enhance compromised natural killer cells and bactericidal activity of leukocytes. In addition, it may act to induce cell cycle arrest during prophase and metaphase in Xenopus embryonic cells. E-64-d inhibits lysosomal proteases and interferes with autolysosomal digestion when used in combination with pepstatin A. E-64-d is also known as EST, (2S,3S)-trans-Epoxysuccinyl-L-leucylamido-3-methylbutane ethyl ester, Loxistatin, E-64d, Aloxistatin, E-64c ethyl ester, EP 453, NSC 694281, and 3-[[[(1S)-3-methyl-1[[(3S-methylbutyl)amino]carbonyl]butyl]amino]carbonyl]-2S-oxiranecarboxylic acid, ethyl ester.


E-64-d (CAS 88321-09-9) References

  1. Effects of proteasome inhibitor (lactacystin) and cysteine protease inhibitor (E-64-d) on processes of mitosis in Xenopus embryonic cells.  |  Sekiguchi, T., et al. 2002. Zoolog Sci. 19: 1251-5. PMID: 12499669
  2. Amelioration of experimental arthritis by a calpain-inhibitory compound: regulation of cytokine production by E-64-d in vivo and in vitro.  |  Yoshifuji, H., et al. 2005. Int Immunol. 17: 1327-36. PMID: 16176933
  3. Influence of oestradiol and tamoxifen on oestrogen receptors-alpha and -beta protein degradation and non-genomic signalling pathways in uterine and breast carcinoma cells.  |  Horner-Glister, E., et al. 2005. J Mol Endocrinol. 35: 421-32. PMID: 16326830
  4. Neurovascular and neuronal protection by E64d after focal cerebral ischemia in rats.  |  Tsubokawa, T., et al. 2006. J Neurosci Res. 84: 832-40. PMID: 16802320
  5. Effect of a thiol proteinase inhibitor, E-64-d, on susceptibility to infection with Staphylococcus aureus in Chediak-Higashi syndrome (beige) mice.  |  Morimoto, M., et al. 2007. Int Immunopharmacol. 7: 973-80. PMID: 17499200
  6. Improvement of deficient natural killer activity and delayed bactericidal activity by a thiol proteinase inhibitor, E-64-d, in leukocytes from Chediak-Higashi syndrome patients in vitro.  |  Tanabe, F., et al. 2009. Int Immunopharmacol. 9: 366-70. PMID: 19185618
  7. Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d.  |  McGowan, EB., et al. 1989. Biochem Biophys Res Commun. 158: 432-5. PMID: 2537073
  8. Cathepsin B is a New Drug Target for Traumatic Brain Injury Therapeutics: Evidence for E64d as a Promising Lead Drug Candidate.  |  Hook, G., et al. 2015. Front Neurol. 6: 178. PMID: 26388830
  9. The protease inhibitor E64d improves ox-LDL-induced endothelial dysfunction in human aortic endothelial cells.  |  Chen, M., et al. 2018. Can J Physiol Pharmacol. 96: 120-127. PMID: 28854341
  10. Identifying purine nucleoside phosphorylase as the target of quinine using cellular thermal shift assay.  |  Dziekan, JM., et al. 2019. Sci Transl Med. 11: PMID: 30602534
  11. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells.  |  Bestle, D., et al. 2020. Life Sci Alliance. 3: PMID: 32703818
  12. Swainsonine promotes apoptosis by impairing lysosomal function and inhibiting autophagic degradation in rat primary renal tubular epithelial cells.  |  Wang, S., et al. 2021. Chem Biol Interact. 336: 109319. PMID: 33186601
  13. Repurposing existing drugs for the treatment of COVID-19/SARS-CoV-2 infection: A review describing drug mechanisms of action.  |  Yousefi, H., et al. 2021. Biochem Pharmacol. 183: 114296. PMID: 33191206
  14. DEEMD: Drug Efficacy Estimation Against SARS-CoV-2 Based on Cell Morphology With Deep Multiple Instance Learning.  |  Saberian, MS., et al. 2022. IEEE Trans Med Imaging. 41: 3128-3145. PMID: 35622798
  15. E64d, a membrane-permeable cysteine protease inhibitor, attenuates the effects of parathyroid hormone on osteoblasts in vitro.  |  Murray, EJ., et al. 1997. Metabolism. 46: 1090-4. PMID: 9284902

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

E-64-d, 1 mg

sc-201280
1 mg
$70.00

E-64-d, 5 mg

sc-201280A
5 mg
$275.00

Hello. I am inquiring to see if the product below is available for shipping immediately upon ordering. If not, when is the expected shipping date? Thank you. E-64-d sc-201280A 5 mg

Asked by: John Ruedas
Thank you for your question. Please contact our Customer Care Department for current product availability.
Answered by: Technical Support
Date published: 2019-06-16

What is the appearance of the compound?

Asked by: two2igm05
Thank you for your question. E-64-d, sc-201280, is a white solid.
Answered by: Chemical Support 4
Date published: 2017-03-14

What is the solubility of this product?

Asked by: hawkeye11
Thank you for your question. E-64-d, sc-201280, sc-201280 is soluble in >10mg/ml in 100% ethanol and 20mg/ml in DMSO.
Answered by: TechService7
Date published: 2016-12-21
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Rated 5 out of 5 by from Worked great with cell linesWe used this product on cell lines, with and without other treatments. It worked exactly as expected.
Date published: 2022-11-21
Rated 5 out of 5 by from Intracellular inhibition of cystein proteaseIntracellular inhibition of cystein protease with 1, 10 and 100 M - Published data
Date published: 2016-05-06
Rated 5 out of 5 by from This drug exerts its function pretty wellThis drug exerts its function pretty well in autophagy induction. Published data
Date published: 2015-11-06
Rated 5 out of 5 by from HornerHorner-Glister, E. et al. (PubMed 16326830) used E-64-d, a calpain inhibitor, to determine if calpain protease is a possible degradation pathway of ER . Since degradation was still observed, calpain protease was eliminated as the cause of ER degradation. -SCBT Publication Review
Date published: 2015-03-20
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E-64-d is rated 5.0 out of 5 by 4.
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