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Active Human Calpain 1 (µ-Calpain), Human Erythrocyte

based on 7 citations in multiple journalsActive Human Calpain 1 (µ-Calpain), Human Erythrocyte74.1 4
A cysteine protease involved in apoptosis activation
Catalog #: 1134
$455.00

Product Details

Cat # +Size 1134-100
Size 100 μg
Alternate Name CANP; muCL; CANP1; SPG76; CANPL1; muCANP; Calpain mu-type; calcium-activated neutral proteinase 1; calpain-1 catalytic subunit; calpain-1 large subunit; cell proliferation-inducing gene 30 protein; micromolar-calpain
Gene Symbol CAPN1
Gene ID 823
Accession # P07384
Source Human Erythrocyte
Appearance Liquid
Physical Form Description In 20 mM imidazole-HCl, 5 mM β-mercaptoethanol, 1 mM EDTA, 1 mM EGTA, 30% glycerol, pH 6.8.
Molecular Weight 110 kDa (migrates as two subunits of 80 kDa and 30 kDa)
Purity by SDS-PAGE ≥95%
Handling Centrifuge the vial prior to opening.
Storage Conditions -70°C
Shipping Conditions Dry Ice
USAGE For Research Use Only! Not to be used in humans

Details

Calpain 1 is a calcium activated neutral cysteine protease. It is a heterodimer of a catalytic 80 kDa subunit and a 30 kDa subunit, which requires 50 µM of Ca²ᶧ for half-maximal activity in vitro. Calpain 1 has been implicated in processes such as in cell division, signal transduction, and long term potentiation, as well as in various pathological processes associated with altered metabolism and altered calcium homeostasis.


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Sirui Jiang, Dynamin‐like protein 1 cleavage by calpain in Alzheimer’s disease. Aging Cell, Feb 2019;  30767411.
Wang et al., MFN2 Couples Glutamate Excitotoxicity and Mitochondrial Dysfunction in Motor Neurons. J. Biol. Chem., Jan 2015; 290: 168 - 182.
Chen et al., Effects of isoproterenol on aquaporin 5 levels in the parotid gland of mice in vivo. Am J Physiol Endocrinol Metab, Jan 2014; 306: E100 - E108.
Mitchell and Samulski. Mechanistic Insights into the Enhancement of Adeno-Associated Virus Transduction by Proteasome Inhibitors. J. Virol., Dec 2013; 87: 13035 - 13041.
Alison L. Müller et al., Activation of proteases and changes in Na+-K+-ATPase subunits in hearts subjected to ischemia-reperfusion. J Appl Physiol, Feb 2013; 114: 351 - 360.
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