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Human Calpain-1
Native whole molecule, biologically active
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Proteins Synonyms: mu-Calpain, u-Calpain, CAPN Biological Activity: ≥ 1, 000 units/mg protein Source: Human Erythrocytes Purity: ≥ 95% by SDS-PAGE Physical State: Frozen in 20 mM imidazole, 5mM β-mercaptoethanol, 1 mM EDTA, 1mM EGTA, 30% glycerol, pH 6.8 Manufacturer: |
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Athens Research & Technology
Produktdetails
Synonyms
mu-Calpain, u-Calpain, CAPN
Description of Human Calpain-1
Calpain-1 (µ-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 µM). 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 β-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-β1 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 PHLPP1β. Therapeutically, calpain-1-specific inhibitors (e.g., peptidyl α-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.
Source
Erythrocytes shown to be non reactive for HBsAg, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests.
Biological Activity
≥ 1, 000 units/mg protein. One unit is defined as the amount of enzyme that will hydrolyze 1 ρmol SucLLVY-AMC per minute at 25°C using a fluorogenic calpain activity assay kit
Storage
For long term, store Human Calpain-1 at ≤ -80°C.
Applications
Alzheimer's, Cardiovascular Disease, Ischemia, Brain Injury, In Vitro Diagnostic.
Citations/Publications
Li, J., et al., (2023), 'Structure of the Flight Muscle Thick Filament from the Bumble Bee, Bombus ignitus, at 6 Å Resolution', Int. J. Mol. Sci., 24: pp 377. Available at: https://doi.org/10.3390/ijms24010377
Shipped with dry ice
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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Payment Methods
Paying by bank transfer
