PP2C-α (D18C10) XP® Rabbit mAb (BSA and Azide Free) #38317
- WB
- IHC
- IF
- F
Supporting Data
| REACTIVITY | H Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 43 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
Formulation
Storage
Specificity / Sensitivity
PP2C-α (D18C10) XP® Rabbit mAb (BSA and Azide Free) detects endogenous levels of total PP2C-α protein.
Species Reactivity:
Human, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser375 of human PP2C-α.
Background
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).
- Marley, A.E. et al. (1998) FEBS Lett 431, 121-4.
- Stern, A. et al. (2007) J Mol Evol 64, 61-70.
- Takekawa, M. et al. (1998) EMBO J 17, 4744-52.
- Sun, W. et al. (2009) Cell Signal 21, 95-102.
- Cheng, A. et al. (2000) J Biol Chem 275, 34744-9.
- Ofek, P. et al. (2003) J Biol Chem 278, 14299-305.
- Strovel, E.T. et al. (2000) J Biol Chem 275, 2399-403.
- Travis, S.M. et al. (1997) Proc Natl Acad Sci USA 94, 11055-60.
Limited Uses
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