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| Packungsgröße | SKU | Verfügbarkeit | Preis |
|---|
Über diesen Artikel
Specific activity:
≥2,500 units/mg protein
Biological source:
bovine
Preise und Verfügbarkeit sind derzeit nicht verfügbar.
Technischer Dienst
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Unterstützung erhaltenbiological 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)
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.[1]
Application
Biochem/physiol Actions
Calcineurin (CaN) activity is stimulated by nickel (Ni2+) and manganese (Mn2+) ions.[1] It participates in the coupling of Ca2+ signals.[1] CaN may regulate oocyte growth and meiotic maturation in porcine.[2] 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.
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.
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.
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Dieser Artikel | |||
|---|---|---|---|
| biological source bovine | biological source bovine brain | biological source mouse | biological source - |
| 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) | Gene Information - |
| form lyophilized powder | form lyophilized | form - | form liquid |
| mol wt dimer ~77 kDa, subunit mol wt 19-58 kDa | mol wt - | mol wt - | mol wt - |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −70°C |
Lagerklasse
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
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Verwandter Inhalt
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)
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| C1907-100UN | 04061833628997 |



