Date published: 2025-10-19

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ALLM (Calpain Inhibitor) (CAS 136632-32-1)

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Alternate Names:
N-Acetyl-L-leucyl-L-leucyl-L-methioninal; Calpain inhibitor II
Application:
ALLM (Calpain Inhibitor) is a cell-permeable, peptide aldehyde inhibitor of calpains and cathepsins
CAS Number:
136632-32-1
Purity:
≥95%
Molecular Weight:
401.56
Molecular Formula:
C19H35N3O4S
For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.
* Refer to Certificate of Analysis for lot specific data.

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ALLM (Calpain Inhibitor) is a synthetic peptide aldehyde that acts as an inhibitor of calpain, a family of calcium-dependent cysteine proteases involved in a variety of cellular processes, including cytoskeletal remodeling, cell proliferation, and apoptosis. The inhibitory action of ALLM (Calpain Inhibitor) is for research into the regulation of calpain activity and its role in cellular homeostasis and pathophysiology. By preventing the proteolytic activity of calpain, ALLM (Calpain Inhibitor) helps to elucidate the pathways through which calpain contributes to certain health conditions. It is particularly valuable in studies aiming to understand the calcium-regulated signals that lead to calpain activation and the subsequent effects on substrate proteins. Research with ALLM (Calpain Inhibitor) also extends to the investigation of other calpain-related regulatory mechanisms and their implications for cell function and survival.


ALLM (Calpain Inhibitor) (CAS 136632-32-1) References

  1. Purification and characterization of a Ca(2+)-activated thiol protease from Drosophila melanogaster.  |  Pintér, M., et al. 1992. Biochemistry. 31: 8201-6. PMID: 1525160
  2. Calpain inhibitors prevent neuronal cell death and ameliorate motor disturbances after compression-induced spinal cord injury in rats.  |  Arataki, S., et al. 2005. J Neurotrauma. 22: 398-406. PMID: 15785234
  3. Calpain inhibition and insulin action in cultured human muscle cells.  |  Logie, LJ., et al. 2005. Mol Genet Metab. 85: 54-60. PMID: 15862281
  4. The role of Ca(2+)-dependent proteases (calpains) in post mortem proteolysis and meat tenderness.  |  Koohmaraie, M. 1992. Biochimie. 74: 239-45. PMID: 1610937
  5. Effects of detergents on Ca(2+)-activated neural proteinase activity (calpain) in neural and non-neural tissue: a comparative study.  |  Banik, NL., et al. 1992. Neurochem Res. 17: 797-802. PMID: 1641062
  6. [Calpain I inhibition prevents pacing-induced structural remodeling for atrial fibrillation in canine].  |  Li, WM., et al. 2007. Zhonghua Xin Xue Guan Bing Za Zhi. 35: 132-6. PMID: 17445406
  7. Calpain I inhibition prevents atrial structural remodeling in a canine model with atrial fibrillation.  |  Xue, HJ., et al. 2008. Chin Med J (Engl). 121: 32-7. PMID: 18208663
  8. Inhibition of the calpain-mediated proteolysis of protein kinase C enhances lytic activity in human NK cells.  |  Shenoy, AM. and Brahmi, Z. 1991. Cell Immunol. 138: 24-34. PMID: 1913839
  9. Intermittent hypoxia degrades HIF-2alpha via calpains resulting in oxidative stress: implications for recurrent apnea-induced morbidities.  |  Nanduri, J., et al. 2009. Proc Natl Acad Sci U S A. 106: 1199-204. PMID: 19147445
  10. m-Calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions.  |  Miyazaki, T., et al. 2010. Cardiovasc Res. 85: 530-41. PMID: 19752040
  11. Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins.  |  Sasaki, T., et al. 1990. J Enzyme Inhib. 3: 195-201. PMID: 2079636
  12. Calpain inhibitors stimulate phagocyte functions via activation of human formyl peptide receptors.  |  Fujita, H., et al. 2011. Arch Biochem Biophys. 513: 51-60. PMID: 21723247
  13. Calpain inhibitors exhibit matrix metalloproteinase-2 inhibitory activity.  |  Ali, MA., et al. 2012. Biochem Biophys Res Commun. 423: 1-5. PMID: 22575511
  14. Calcium-calpain Dependent Pathways Regulate Vesiculation in Malignant Breast Cells.  |  Taylor, J., et al. 2017. Curr Cancer Drug Targets. 17: 486-494. PMID: 27799031
  15. Rapid production method with increased yield of high-purity extracellular vesicles obtained using extended mitochondrial targeting domain peptide.  |  Lim, KM., et al. 2022. J Extracell Vesicles. 11: e12274. PMID: 36239712

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

ALLM (Calpain Inhibitor), 5 mg

sc-201268
5 mg
$140.00

ALLM (Calpain Inhibitor), 25 mg

sc-201268A
25 mg
$380.00