C1907
Calcineurin from bovine brain
lyophilized powder, ≥2,500 units/mg protein
Synonym(s):
Calcium/Calmodulin-Activated Protein Phosphatase, Calmodulin binding protein, Modulator binding protein, PP2B, Phosphoprotein Phosphohydrolase, Protein phosphatase 2B
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About This Item
Recommended Products
biological source
bovine
Quality Level
form
lyophilized powder
specific activity
≥2,500 units/mg protein
mol wt
dimer ~77 kDa
subunit mol wt 19-58 kDa
composition
Protein, 0.3-1.7% Lowry
solubility
H2O: soluble
UniProt accession no.
storage temp.
−20°C
Gene Information
cow ... PPP3CA(286852)
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General description
Calcineurin (CaN) comprises CaN A and CaN B subunits. It exists as a heterodimer with a calmodulin-binding domain, catalytic site, a CaN B binding domain, and an autoinhibitory domain.
Application
Calcineurin from bovine brain has been used:
- as a positive control in western blot analysis of oocytes and cumulus cells proteome
- as a positive control in calmodulin (CaM)-agarose binding assay
- to test its phosphatase activity in the presence of okadaic acid
Biochem/physiol Actions
Calcineurin (CaN) activity is stimulated by nickel (Ni2+) and manganese (Mn2+) ions. It participates in the coupling of Ca2+ signals. CaN may regulate oocyte growth and meiotic maturation in porcine. It also participates in gene regulation, cell survival, and death.
Calcineurin is a cyclosporin-sensitive, calcium-regulated, serine-threonine protein phosphatase with broad substrate specificity. It is the major calmodulin-binding protein found in the brain. First identified as an inhibitor of the calmodulin activation of phosphodiesterase 3′:5′ cyclic nucleotide (PDE), calcineurin has similar effects on adenylate cyclase. Serves as a key enzyme involved in T-cell activation. Also involved in the hyperphosphorylation of tau protein in Alzheimer′s disease and has been shown to prevent calpain-mediated proteolysis of tau in differentiated PC12 cells.
Unit Definition
One unit will cause a 50% inhibition of the activated phosphodiesterase, 3′:5′-cyclic nucleotide (P 9529) activity when assayed with two units of activator (P 2277) and 0.1 mM Ca2+ in an enzyme coupled system at pH 7.5 at 30 °C.
Physical form
Lyophilized powder containing 0.5% EGTA, buffer salts and stabilizers.
Analysis Note
Sigma tests activity in 80 mM Tris, pH 7.5 with 65 mM KCl, 8 mM MgSO4 and 0.3% albumin.
Storage Class Code
11 - Combustible Solids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Felicia Ranta et al.
Cellular signalling, 20(10), 1780-1786 (2008-07-10)
Previously, we described that apoptotic cell death induced by the synthetic glucocorticoid dexamethasone (dex) is inhibited by calcineurin inhibitors, FK506 and deltamethrin, in insulin-secreting cells. The aim of the present study was to examine the mechanism of dex-dependent activation of
Lenka Tůmová et al.
Animal reproduction science, 141(3-4), 154-163 (2013-08-27)
The processes of oocyte growth, acquisition of meiotic competence and meiotic maturation are regulated by a large number of molecules. One of them could be calcineurin consisting of catalytic subunit A (Aα, Aβ, Aγ isoforms) and regulatory subunit B (B1
H Q Xie et al.
Journal of neuroscience research, 53(2), 153-164 (1998-07-22)
The effects of calcium influx on tau levels and phosphorylation were examined in differentiated PC12 cells. Maitotoxin-induced calcium influx resulted in time- and concentration-dependent tau dephosphorylation and degradation. Incubation of PC12 cells with a membrane-permeable calpain inhibitor blocked maitotoxin-induced tau
Ashakumary Lakshmikuttyamma et al.
Neurochemical research, 29(10), 1913-1921 (2004-11-10)
A major cause of neuronal dysfunction is due to altered Ca2+ regulation. An increase in Ca2+ influx can activate Ca2+-dependent enzymes including calpains, causing the proteolysis of its specific substrates. In the present study, calcineurin (CaN) was found to be
Modulator binding protein. Bovine brain protein exhibiting the Ca2+-dependent association with the protein modulator of cyclic nucleotide phosphodiesterase.
J H Wang et al.
The Journal of biological chemistry, 252(12), 4175-4184 (1977-06-25)
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