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Merck

C1907

Calcineurin from bovine brain

lyophilized powder, ≥2,500 units/mg protein

Sinónimos:

Calcium/Calmodulin-Activated Protein Phosphatase, Calmodulin binding protein, Modulator binding protein, PP2B, Phosphoprotein Phosphohydrolase, Protein phosphatase 2B

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508,00 €

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Número CAS:
UNSPSC Code:
51111800
NACRES:
NA.32
MDL number:

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Nombre del producto

Calcineurin from bovine brain, lyophilized powder, ≥2,500 units/mg protein

biological source

bovine

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

Quality Level

Gene Information

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1 of 4

Este artículo
208694SAB4200816539568
specific activity

≥2,500 units/mg protein

specific activity

≥250,000 units/mg protein

specific activity

-

specific activity

≥300,000 U/mg, ≥50,000 units/mL

Gene Information

cow ... PPP3CA(286852)

Gene Information

bovine ... Calm(32659)

Gene Information

bovine ... PPP3CA(286852)
human ... CALNA(5530)
rat ... Caln1(363909)

Gene Information

-

biological source

bovine

biological source

bovine brain

biological source

mouse

biological source

-

form

lyophilized powder

form

lyophilized

form

-

form

liquid

UniProt accession no.

P48452

UniProt accession no.

-

UniProt accession no.

Q08209

UniProt accession no.

-

solubility

H2O: soluble

solubility

aqueous buffer: soluble, water: soluble

solubility

-

solubility

-

Analysis Note

Sigma tests activity in 80 mM Tris, pH 7.5 with 65 mM KCl, 8 mM MgSO4 and 0.3% albumin.

Application

Calcineurin from bovine brain has been used:
  • as a positive control in western blot analysis of oocytes and cumulus cells proteome[1]
  • as a positive control in calmodulin (CaM)-agarose binding assay[2]
  • to test its phosphatase activity in the presence of okadaic acid[3]

Biochem/physiol Actions

Calcineurin (CaN) activity is stimulated by nickel (Ni2+) and manganese (Mn2+) ions.[4] It participates in the coupling of Ca2+ signals.[4] CaN may regulate oocyte growth and meiotic maturation in porcine.[1] It also participates in gene regulation, cell survival, and death.[3]
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.
The major calmodulin-binding protein found in the brain. A key enzyme involved in T-cell activation and hyperphosphorylation of tau protein in Alzheimer′s disease.

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.[4]

Other Notes

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.

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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
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
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
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
T D Batiuk et al.
The Journal of clinical investigation, 100(7), 1894-1901 (1997-10-06)
Cyclosporine (CsA) is both a clinical immunosuppressive drug and a probe to dissect intracellular signaling pathways. In vitro, CsA inhibits lymphocyte gene activation by inhibiting the phosphatase activity of calcineurin (CN). In clinical use, CsA treatment inhibits 50-75% of CN

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