PP2C-α (D18C10) XP Rabbit mA

3549:

Flow , IHC / Paraffin , Immunofluorescence , Immunoprecipitation , Western Blotting

PP2C-α (D18C10) XP^® Rabbit mAb detects endogenous levels of total PP2C-α protein.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser375 of human PP2C-α.

Western Blotting

Western blot analysis of extracts from various cell lines using PP2C-α (D18C10) XP^® Rabbit mAb.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma using PP2C-α (D18C10) XP^® Rabbit mAb.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma using PP2C-α (D18C10) XP^® Rabbit mAb.

Flow Cytometry

Flow cytometric analysis of HeLa cells using PP2C-α (D18C10) XP^® Rabbit mAb (blue) compared to a nonspecific negative control antibody (red).

IF-IC

Confocal immunofluorescent analysis of HeLa cells using PP2C-α (D18C10) XP^® Rabbit mAb (green). Actin filaments were labeled using DY-554 phalloidin (red).

The α isoform of protein phosphatase 2C (PP2C-α) is the catalytic subunit of a widely expressed serine/threonine phosphatase involved in regulation of the cell stress response (1,2). Also known as magnesium-dependent protein phosphatase (PPM1A), this monomeric phosphatase is a member of a conserved group of proteins that acts on many different substrates in numerous pathways. PP2C-α inhibits p38 MAPK and SAPK/JNK pathways activated in response to cell stress as seen in both in vivo and in vitro studies. Specifically, PP2C-α removes phosphates from MKK3 and MKK7, reducing activity of both proteins and inhibiting activation of the downstream kinases JNK and p38 MAPK, respectively (3). Another PP2C-α substrate is IKKβ, the critical regulator of NF-κB signaling. Dephosphorylation of IKKβ at Ser177/181 by PPM1A and PPM1B results in inactivation of IKKβ and inhibition of NF-κB signaling (4). PP2C-α is one of the phosphatases responsible for removing phosphate residues from cyclin dependent protein kinases. In a study using HeLa cell extracts, PP2C-α dephospohrylates CDK2 and CDK6, with a preference toward interacting with CDK2 phosphorylated at Thr160, a residue found in the activating T-loop of the kinase. Removal of phosphates from this site is thought to inactivate cyclin-associated kinases (5). PP2C-α induces cell cycle arrest and apoptosis, likely through activation of p53 though other pathways may also contribute to PP2C-α mediated cell death (6). Additional PP2C-α substrates include the Wnt signaling pathway protein axin (7) and CFTR, a chloride channel protein implicated in cystic fibrosis (8).

1. Marley, A.E. et al. (1998) FEBS Lett 431, 121-4.
2. Stern, A. et al. (2007) J Mol Evol 64, 61-70.
3. Takekawa, M. et al. (1998) EMBO J 17, 4744-52.
4. Sun, W. et al. (2009) Cell Signal 21, 95-102.
5. Cheng, A. et al. (2000) J Biol Chem 275, 34744-9.
6. Ofek, P. et al. (2003) J Biol Chem 278, 14299-305.
7. Strovel, E.T. et al. (2000) J Biol Chem 275, 2399-403.
8. Travis, S.M. et al. (1997) Proc Natl Acad Sci USA 94, 11055-60.

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For Research Use Only. Not For Use In Diagnostic Procedures.