SensoLyte® AMC Calpain Activity Assay Kit

Catalog No. ABIN1882424

Product Details

Target: Calpain

Detection Method: Fluorometric

Application: Activation (Act), Fluorescence Resonance Energy Transfer Microscopy (FRET)

Brand: SensoLyte®

Characteristics: The SensoLyte® AMC Calpain Assay Kit is optimized for detecting calpain activities. This kit contains a fluorogenic peptide substrate, suc-LLVY-AMC. Upon calpain protease cleavage, suc-LLVY-AMC generates the AMC fluorophore emitting bright blue fluorescence and can be monitored at excitation/emission=354/442 nm. Increase in AMC fluorescence is proportional to calpain activity. The assay can detect both calpain 1 (µ) and 2 (m) activities and is ideal for kinetic study of these enzymes. The assays are performed in a convenient 96-well microplate format.

Application Details

Comment:

FRET-based Assay Kit

Restrictions: For Research Use only

Handling

Handling Advice: Aliquot as needed to avoid multiple freeze-thaw cycles. Protect Components A and B from light and moisture.

Storage: -80 °C

Storage Comment: Store all kit components, except Component D, at -20 °C. Store Component D at -80 °C. Component C can be stored at room temperature for convenience.

References

Lai, Riley, Cai, Leong, Herman: "Calpain mediates epithelial cell microvillar effacement by enterohemorrhagic Escherichia coli." in: Frontiers in microbiology, Vol. 2, pp. 222, (2011) (PubMed).

Wadosky, Li, Rodríguez, Min, Bogan, Gonzalez, Patterson, Kornegay, Willis: "Regulation of the calpain and ubiquitin-proteasome systems in a canine model of muscular dystrophy." in: Muscle & nerve, Vol. 44, Issue 4, pp. 553-62, (2011) (PubMed).

Gallery, Blank, Lin, Gutierrez, Pulido, Rappoli, Badola, Rolfe, Macbeth: "The JAMM motif of human deubiquitinase Poh1 is essential for cell viability." in: Molecular cancer therapeutics, Vol. 6, Issue 1, pp. 262-8, (2007) (PubMed).

Target Details

Target: Calpain

Abstract: Calpain Products

Background: The calpains are a family of intracellular Ca2+ supdependent cysteine proteases. The best-characterized calpains are isoforms 1 (m) and 2 (m). Calpains respond to Ca2+ signals by cleaving many specific proteins, thereby irreversibly modifying their function(s). They are implicated in a variety of Ca2+ regulated cellular processes as well as various pathological phenomena, such as ischemic injury, muscular dystrophy, diabetes, cataract, atherosclerosis, Alzheimer's disease, and cancer. Calpains represent potential therapeutic targets for drug discovery.