CAPN1 Research Reagents

Calpain-1 catalytic subunit is a protein in humans that is encoded by CAPN1 gene. Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

The following CAPN1 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

CAPN1 Antibodies

CAPN1 Antibodies for Homo sapiens (Human)

CAPN1 Antibodies for Mus musculus (Mouse)

CAPN1 Proteins

CAPN1 Proteins for Sus scrofa (Pig)

CAPN1 Proteins for Oryctolagus cuniculus (Rabbit)

CAPN1 Proteins for Homo sapiens (Human)

CAPN1 Proteins for Mus musculus (Mouse)

CAPN1 Proteins for Rattus norvegicus (Rat)

CAPN1 Proteins for Bos taurus (Bovine)

CAPN1 Proteins for Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)

CAPN1 Proteins for Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)

CAPN1 Background

The CAPN1 encodes calpain-1, one isoform of calpains that are calcium-activated cytosolic cysteine proteases. CAPN1 is ubiquitously expressed in the central nervous system (CNS) of mammalian cells[1]. Calpain exists as an inactive proenzyme in the cytosol and migrates to membranes in response to the increase of cellular calcium ion concentration [2]. At the membrane, calpain is activated in the presence of calcium ion and phospholipids [3]. Calpain activation in apoptosis was first demonstrated in thymocytes, as measured by calpain autolysis [4]. Activated calpain leads to apoptosis by mediating the degradation of various proteins involved in maintaining neuronal structural integrity essential for normal cellular function and survival [5]. Calpain-1 is activated by micromolar concentrations of calcium. The activation of calpain-1 promotes neuronal survival (namely neuroprotection) [6] and synaptic plasticity [8][10]. Synaptic Nmethyl- D-asparate (NMDA) receptor-induced activation of calpain-1 degraded both PHLPP1α and PHLPP1β, leading to activation of the Akt & ERK pathways and neuroprotection [6][7]. Other findings also revealed the physiological role of calpain-1 in the regulation of calcium influx, apoptosis of primary neurons subjected to oxidative stress, and neuronal death following traumatic brain injury [14]. Targeted inhibition of calpain-1 offers a potential therapeutic approach against TBI and other neurodegenerative diseases [14]. Mutations in CAPN1 have recently been identified in a complicated form of Hereditary Spastic Paraplegia (HSP) with a combination of cerebellar ataxia and corticomotor tract disorder(SPG76) [9]. Overactivation of calpain-1 causes irreversible cell damage and contributes to the pathology of cerebral and cardiac ischemia, Alzheimer's disease, arthritis, and cataract formation [10][11]. Yoko Nabeshima et al. proposed that regulation of calpain-1 activity is a potential therapeutic target for drug development towards delaying onsets of aging-related syndromes caused by the abnormality of mineral homeostasis and reducing the complications of CKD [13].

[1] Ohno S, Minoshima S, et al. Four genes for the calpain family located on four distinct human chromosomes [J]. Cytogenet Cell Genet. 1990, 53 (4): 225-9.
[2] Wingrave JM, Schaecher KE, et al. Early induction of secondary injury factors causing activation of calpain and mitochondria-mediated neuronal apoptosis following spinal cord injury in rats [J]. J Neurosci Res. 2003 Jul 1; 73(1):95-104.
[3] Suzuki K, Sorimachi H. A novel aspect of calpain activation [J].FEBS Lett. 1998 Aug 14; 433(1-2):1-4.
[4] Squìer MK, Miller AC, et al. Calpain activation in apoptosis [J]. J Cell Physiol. 1994 May; 159(2):229-37.
[5] Springer JE, Azbill RD, et al. Rapid calpain I activation and cytoskeletal protein degradation following traumatic spinal cord injury: attenuation with riluzole pretreatment [J]. J Neurochem. 1997 Oct; 69 (4):1592-600.
[6] Wang Y, et al. Distinct roles for mu-calpain and m-calpain in synaptic NMDAR-mediated neuroprotection and extrasynaptic NMDAR-mediated neurodegeneration [J]. J Neurosci. 2013;33(48):18880-92.
[7] Averna M, Pellegrini M, et al. Physiological roles of calpain 1 associated to multiprotein NMDA receptor complex [J]. PLoS ONE. 2015, 10:e0139750.
[8] Liu J, Liu MC, et al. Calpain in the CNS: from synaptic function to neurotoxicity [J]. Sci Signal. 2008 Apr 8; 1(14):re1.
[9] Stefano Cotti Piccinelli, Maria T. Bassi, et al. A Novel CAPN1 Mutation Causes a Pure Hereditary Spastic Paraplegia in an Italian Family [J]. Front Neurol. 2019; 10: 580.
[10] Baudry M, Bi X. Calpain-1 and calpain-2: the Yin and Yang of synaptic plasticity and neurodegeneration [J]. Trends Neurosci. 2016, 39:235-45.
[11] Wang, K. K. & Yuen, P. W. Calpain inhibition: an overview of its therapeutic potential [J]. Trends Pharmacol. Sci. 15, 1994, 412-419.
[12] Lee, M. S. et al. Neurotoxicity induces cleavage of p35 to p25 by calpain [J]. Nature 405, 2000, 360-364.
[13]Yoko Nabeshima, Miwa Washida, et al. Calpain 1 inhibitor BDA-410 ameliorates α-klotho-deficiency phenotypes resembling human aging-related syndromes [J]. Scientific Reports volume 4, 2015, Article number: 5847.
[14] Kaori H. Yamada, Dorothy A. Kozlowski, et al. Targeted Gene Inactivation of Calpain-1 Suppresses Cortical Degeneration Due to Traumatic Brain Injury and Neuronal Apoptosis Induced by Oxidative Stress [J]. The Journal of Biological Chemistry, 2012, 287, 13182-13193.

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