Cell Signaling Technology

Product Pathways - Phosphatases

SG2NA (S68) Mouse mAb #4956

Applications Reactivity MW (kDa) Source Isotype
W IP H M R Mk 95 Mouse IgG1

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

SG2NA (S68) Mouse mAb detects endogenous levels of total SG2NA protein. This antibody does not cross-react with striatin or other PP2A subunits.

Source / Purification

Monoclonal antibody is produced by immunizing mice with a synthetic peptide corresponding to residues around Ser240 of human SG2NA.

Western Blotting

Western Blotting

Western blot analysis of extracts from PL45, C2C12, C6 and COS cells, using SG2NA (S68) Mouse mAb.

Background

Protein phosphatase type 2A (PP2A) is an essential protein serine/threonine phosphatase that is conserved in all eukaryotes. PP2A is a key enzyme within various signal transduction pathways as it regulates fundamental cellular activities such as DNA replication, transcription, translation, metabolism, cell cycle progression, cell division, apoptosis and development (1-3). The core enzyme consists of catalytic C and regulatory A (or PR65) subunits, with each subunit represented by α and β isoforms (1). Additional regulatory subunits belong to four different families of unrelated proteins. Both the B (or PR55) and B' regulatory protein families contain α, β, γ and δ isoforms, with the B' family also including an ε protein. B'' family proteins include PR72, PR130, PR59 and PR48 isoforms, while striatin (PR110) and SG2NA (PR93) are both members of the B''' regulatory protein family. These B subunits competitively bind to a shared binding site on the core A subunit (1). This variable array of holoenzyme components, particularly regulatory B subunits, allows PP2A to act in a diverse set of functions. PP2A function is regulated by expression, localization, holoenzyme composition and post-translational modification. Phosphorylation of PP2A at Tyr307 by Src occurs in response to EGF or insulin and results in a substantial reduction of PP2A activity (4). Reversible methylation on the carboxyl group of Leu309 of PP2A has been observed (5,6). Methylation alters the conformation of PP2A, as well as its localization and association with B regulatory subunits (6-8).

  1. Janssens, V. and Goris, J. (2001) Biochem. J. 353, 417-439.
  2. Zolnierowicz, S. (2000) Biochem. Pharmacol. 60, 1225-1235.
  3. Milward, T.A. et al. (1999) Trends Biochem. Sci. 24, 186-191.
  4. Chen, J. et al. (1992) Science 257, 1261-1264.
  5. Turowski, P. et al. (1995) J. Cell. Biol. 129, 397-410.
  6. Lee, J. et al. (1996) Proc. Natl. Acad. Sci. USA 93, 6043-6047.
  7. Tolstykh, T. et al. (2000) EMBO J. 19, 5682-5691.
  8. Yu, X.X. et al. (2001) Mol. Biol. Cell 12, 185-199.

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