Calpain-1, Porcine

Athens Research

Calpain-1, Porcine

9

Alzheimer's, Cardiovascular Disease, Ischemia, Brain Injury, In Vitro Diagnostic

Research Use Only

≥95% by SDS-PAGE

Calpain-1 (u-Calpain) is a calcium-dependent cysteine protease composed of an 80 kDa catalytic subunit (CAPN1) and a 30 kDa regulatory subunit (CAPNS1), forming a heterodimer stabilized by domain interactions. The catalytic subunit contains four domains: domain II harbors the protease active site, while domain IV binds calcium, enabling activation at micromolar concentrations (EC₅₀ ≈ 50 uM). The regulatory subunit’s domain VI facilitates membrane association and modulates calcium sensitivity. Calpain-1 regulates cellular processes including cytoskeletal remodeling, signal transduction, and synaptic plasticity by cleaving substrates like protein kinase C (PKC), focal adhesion kinase, and bèta-spectrin, often altering their activity or localization. Dysregulated calpain-1 activity is implicated in neurodegenerative diseases such as Alzheimer’s, where excessive cleavage of tau and amyloid precursor protein exacerbates neurofibrillary tangle formation. In cardiovascular pathologies, calpain-1 promotes vascular smooth muscle calcification via matrix metalloproteinase-2 activation and transforming growth factor-bèta1 signaling, contributing to atherosclerosis. Renal proximal tubule injury involves calpain-1-mediated degradation of cytoskeletal proteins (paxillin, talin), leading to cell necrosis. Conversely, calpain-1 activation during long-term potentiation (LTP) supports synaptic plasticity and neuroprotection by degrading inhibitors of ERK signaling, such as PHLPP1bèta. Therapeutically, calpain-1-specific inhibitors (e.g., peptidyl alfa-ketoamides) are under investigation for traumatic brain injury and ischemia, aiming to mitigate calcium-induced proteolysis. Recombinant calpain-1 expression systems enable structural studies to refine drug design. Additionally, calpain-1 activity serves as a biomarker for disease progression in Alzheimer’s and cardiovascular disorders, with elevated levels correlating with tissue damage. These dual roles-as a mediator of physiological plasticity and pathological degradation-underscore its potential as a therapeutic target across diverse conditions.

more then 1 year

Porcine erythrocyte was obtained from healthy animals of US origin and under the care of a registered veterinarian.

≤ -80° C

12352202