Cell Signaling Technology

Product Pathways - Phosphatases

PP2A C Subunit Antibody #2038

Applications Reactivity Sensitivity MW (kDa) Source
W IP IHC-P IF-IC F H M R Mk Dm (C) (Pg) Endogenous 36, 38 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  C=Chicken  Dm=D. melanogaster  Pg=Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

This antibody detects endogenous levels of PP2A catalytic subunit protein (both α and β isoforms). The antibody does not cross-react with other PP2A subunits.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino acids at the carboxy terminus of human PP2A catalytic subunit. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa, NIH/3T3, C6 and COS cells using PP2A C Subunit Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma using PP2A C Subunit Anitbody in the presence of control peptide (left) or PP2A C Subunit Blocking Peptide, #1067 (right).

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, showing cytoplasmic localization, using PP2A C Subunit Antibody.


IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma using PP2A C Subunit Antibody.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma using PP2A C Subunit Antibody in the presence of control peptide (left) or antigen-specific peptide, #1067 (right).

Flow Cytometry

Flow Cytometry

Flow cytometric analysis of NIH/3T3 cells using PP2A C Subunit Antibody (blue) compared to a non-specifc negative control antibody (red).


IF-IC

IF-IC

Immunofluorescent analysis of paraformaldehyde fixed HeLa cells using PP2A C Subunit Antibody.

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.

Application References

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

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