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 for Homo sapiens (Human)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA004490GA01HU | CAPN1 Antibody |
Human,Mouse,Rat | ELISA,WB |
CSB-PA004490ESR1HU | CAPN1 Antibody |
Human | ELISA, IHC |
CSB-PA004490ESR2HU | CAPN1 Antibody |
Human | ELISA, WB, IHC |
CSB-PA004490LA01HU | CAPN1 Antibody |
Human | ELISA, WB, IHC, IF |
CSB-PA182064 | CAPN1 Antibody |
Human,Mouse,Rat | ELISA,WB |
CSB-PA445743 | CAPN1 Antibody |
Human,Mouse,Rat | ELISA,WB,IHC |
CSB-PA004490EA01HU | CAPN1 Antibody |
Human | ELISA, WB, IHC |
CSB-PA004490EB01HU | CAPN1 Antibody, HRP conjugated |
Human | ELISA |
CSB-PA004490ED01HU | CAPN1 Antibody, Biotin conjugated |
Human | ELISA |
CAPN1 Antibodies for Mus musculus (Mouse)
Code | Product Name | Species Reactivity | Application |
---|---|---|---|
CSB-PA004490ZA01MO | Capn1 Antibody |
Mus musculus | ELISA, WB (ensure identification of antigen) |
CAPN1 Proteins for Sus scrofa (Pig)
Code | Product Name | Source |
---|---|---|
CSB-YP004490PI CSB-EP004490PI CSB-BP004490PI CSB-MP004490PI CSB-EP004490PI-B |
Recombinant Pig Calpain-1 catalytic subunit(CAPN1) ,partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CAPN1 Proteins for Oryctolagus cuniculus (Rabbit)
Code | Product Name | Source |
---|---|---|
CSB-YP004490RB CSB-EP004490RB CSB-BP004490RB CSB-MP004490RB CSB-EP004490RB-B |
Recombinant Rabbit Calpain-1 catalytic subunit(CAPN1) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CAPN1 Proteins for Homo sapiens (Human)
Code | Product Name | Source |
---|---|---|
CSB-YP004490HU CSB-BP004490HU CSB-MP004490HU CSB-EP004490HU-B |
Recombinant Human Calpain-1 catalytic subunit(CAPN1) |
Yeast Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CSB-EP004490HU | Recombinant Human Calpain-1 catalytic subunit(CAPN1) |
E.coli |
CAPN1 Proteins for Mus musculus (Mouse)
Code | Product Name | Source |
---|---|---|
CSB-YP004490MO CSB-BP004490MO CSB-MP004490MO CSB-EP004490MO-B |
Recombinant Mouse Calpain-1 catalytic subunit(Capn1) |
Yeast Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CSB-EP004490MO | Recombinant Mouse Calpain-1 catalytic subunit(Capn1) |
E.coli |
CAPN1 Proteins for Rattus norvegicus (Rat)
Code | Product Name | Source |
---|---|---|
CSB-YP004490RA CSB-EP004490RA CSB-BP004490RA CSB-MP004490RA CSB-EP004490RA-B |
Recombinant Rat Calpain-1 catalytic subunit(Capn1) |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CAPN1 Proteins for Bos taurus (Bovine)
Code | Product Name | Source |
---|---|---|
CSB-YP632942BO CSB-EP632942BO CSB-BP632942BO CSB-MP632942BO CSB-EP632942BO-B |
Recombinant Bovine Calpain-1 catalytic subunit(CAPN1) ,partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CAPN1 Proteins for Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Code | Product Name | Source |
---|---|---|
CSB-YP705940PYX CSB-EP705940PYX CSB-BP705940PYX CSB-MP705940PYX CSB-EP705940PYX-B |
Recombinant Pongo abelii Calpain-1 catalytic subunit(CAPN1) ,partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
CAPN1 Proteins for Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Code | Product Name | Source |
---|---|---|
CSB-YP875604MOV CSB-EP875604MOV CSB-BP875604MOV CSB-MP875604MOV CSB-EP875604MOV-B |
Recombinant Macaca fascicularis Calpain-1 catalytic subunit(CAPN1) ,partial |
Yeast E.coli Baculovirus Mammalian cell In Vivo Biotinylation in E.coli |
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.