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
Sign Into View Organizational & Contract Pricing
All Photos(1)
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)
Looking for similar products? Visit Product Comparison Guide
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
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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)
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
C X Gong et al.
Brain research, 741(1-2), 95-102 (1996-11-25)
Abnormally hyperphosphorylated tau is the major protein component of neurofibrillary tangles, the characteristic lesion of Alzheimer's disease (AD). Protein phosphatases (PP) type 1 (PP-1), type 2A (PP-2A) and type 2B (PP-2B) appear to be involved in the regulation of tau
Calmodulin binds to and regulates the activity of beta-secretase (BACE1)
Chavez SE and O?Day DH
Current research journal of biological sciences, 1, 37-47 (2007)
C B Klee et al.
Biochemistry, 17(1), 120-126 (1978-01-10)
The Ca2+-dependent, reversible, interaction of cyclic adenosine 3',5'-monophosphate (cAMP) phosphodiesterase with its activator has been used to purify the enzyme by affinity chromatography. Activator-dependent cAMP phosphodiesterase is only a minor component of the proteins specifically adsorbed in the presence of
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service