Application
| WB, IHC, IP, ICC |
---|---|
Primary Accession | Q08209 |
Other Accession | Q08209 |
Host | Rabbit |
Reactivity | Human, Mouse, Rat, Rabbit, Dog |
Clonality | Polyclonal |
Description | Rabbit Anti-Human Calcineurin A Polyclonal |
Target/Specificity | Detects ~61kDa. |
Other Names | Alpha isoform formerly PPP2B Antibody, Calcineurin A alpha Antibody, Calcineurin A1 Antibody, CalcineurinA Antibody, Calmodulin dependent calcineurin A subunit alpha isoform Antibody, Calmodulin-dependent calcineurin A subunit alpha isoform Antibody, CALN Antibody, CALNA Antibody, CALNA 1 Antibody, CAM PRP catalytic subunit Antibody, CCN 1 Antibody, Protein phosphatase 2B catalytic subunitProtein phosphatase 3 (formerly 2B) catalytic subunit alpha isoform Antibody, Protein phosphatase 3 catalytic subunit alpha isoform PPP3CA Antibody, Protein phosphatase 3 catalytic subunit alpha isozyme Antibody, Serine/threonine protein phosphatase 2B catalytic subunit alpha isoform Antibody |
Immunogen | Human Calcineurin A peptide (AA 264-283) |
Purification | Peptide Affinity Purified |
Storage | -20ºC |
Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
Shipping Temperature | Blue Ice or 4ºC |
Certificate of Analysis | 1 µg/ml of SPC-175 was sufficient for detection of Calcineurin A in 20 µg of Heat shock Hela lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody. |
Cellular Localization | Nucleus |
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Provided below are standard protocols that you may find useful for product applications.
Background
Calcineurin is a heterodimeric phosphatase protein, also known as calcium-dependent serine-threonine phosphatase. The structure consists of a catalytic subunit alpha, Calcineurin A (57-59KDa) the active site and a Ca2+ binding unit, Calcineurin B (19-20KDa) the regulatory subunit(1). Calcineurin plays a key role in the T-cell response growth and differentiation mechanism, regulating the activation of the Nuclear factor of activated T-cells (NFATc) which are important in the expression of IL-2 genes. Calcineurin has been the target of inhibitors, the novel and structural immune-suppressants antifungal drugs(2). Genetic studies in yeast and fungi established the molecular basis of the inhibition mechanism by cyclosporine A and FK506 (3).
References
1. Rusnak F. and Mertz P. (2000) Physiol Rev. 80(4):1483-521.
2. Hemenway C.S. And Heitman J. (1999)Cell Biochem Biophys. 30(1):115-51.
3. Fox D.S. and Heitman J. (2002) Bioessays. 24(10):894-903.