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PhosphoSitePlus® Resource

  • Additional protein information
  • Analytical tools

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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-p53 (Ser6) Antibody 9285 40 µl
Western Blotting Immunoprecipitation
H Mk 53 Rabbit 
Phospho-p53 (Ser9) Antibody 9288 40 µl
Western Blotting Immunoprecipitation
H Mk 53 Rabbit 
Phospho-p53 (Ser15) (16G8) Mouse mAb 9286 40 µl
Western Blotting Immunofluorescence Flow Cytometry
H 53 Mouse IgG1
Phospho-p53 (Thr18) Antibody 2529 40 µl
Western Blotting
H 53 Rabbit 
Phospho-p53 (Ser20) Antibody 9287 40 µl
Western Blotting
H Mk 53 Rabbit 
Phospho-p53 (Ser46) Antibody 2521 40 µl
Western Blotting Immunoprecipitation Immunofluorescence Flow Cytometry
H Mk 53 Rabbit 
Phospho-p53 (Thr81) Antibody 2676 40 µl
Western Blotting Immunohistochemistry
H Mk 53 Rabbit 
Phospho-p53 (Ser392) Antibody 9281 40 µl
Western Blotting
H M Mi 53 Rabbit 
p53 (7F5) Rabbit mAb 2527 40 µl
Western Blotting Immunohistochemistry Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H Mk 53 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
Goat 

Product Description

The Phospho-p53 Antibody Sampler Kit provides a fast and economical means of evaluating multiple phosphorylation sites of p53 protein. The kit contains enough primary and secondary antibodies to perform four Western blot experiments.


Specificity / Sensitivity

Phospho-p53 (Ser6), (Ser9), (Ser15), (Ser20), (Thr18), (Thr81), and (Ser392) Antibodies detect p53 only when phosphorylated at the indicated sites and do not cross-react with p53 phosphorylated at other sites.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide and are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with recombinant human proteins or synthetic peptides.

The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro (2,3). DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 (4). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (5,6). p53 can be phosphorylated by ATM, ATR, and DNA-PK at Ser15 and Ser37. Phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and activation of p53 in response to DNA damage (4,7). Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability, and activity (8,9). p53 is phosphorylated at Ser392 in vivo (10,11) and by CAK in vitro (11). Phosphorylation of p53 at Ser392 is increased in human tumors (12) and has been reported to influence the growth suppressor function, DNA binding, and transcriptional activation of p53 (10,13,14). p53 is phosphorylated at Ser6 and Ser9 by CK1δ and CK1ε both in vitro and in vivo (13,15). Phosphorylation of p53 at Ser46 regulates the ability of p53 to induce apoptosis (16). Acetylation of p53 is mediated by p300 and CBP acetyltransferases. Inhibition of deacetylation suppressing MDM2 from recruiting HDAC1 complex by p19 (ARF) stabilizes p53. Acetylation appears to play a positive role in the accumulation of p53 protein in stress response (17). Following DNA damage, human p53 becomes acetylated at Lys382 (Lys379 in mouse) in vivo to enhance p53-DNA binding (18). Deacetylation of p53 occurs through interaction with the SIRT1 protein, a deacetylase that may be involved in cellular aging and the DNA damage response (19).


1.  Chehab NH et al. (1999) Proc Natl Acad Sci U S A 96, 13777–82

2.  Levine, A.J. (1997) Cell 88, 323-31.

3.  Meek, D.W. (1994) Semin Cancer Biol 5, 203-10.

4.  Milczarek, G.J. et al. (1997) Life Sci 60, 1-11.

5.  Shieh, S.Y. et al. (1997) Cell 91, 325-34.

6.  Tibbetts, R.S. et al. (1999) Genes Dev 13, 152-7.

7.  Honda, R. et al. (1997) FEBS Lett 420, 25-7.

8.  Shieh, S.Y. et al. (1999) EMBO J 18, 1815-23.

9.  Hirao, A. et al. (2000) Science 287, 1824-7.

10.  Hao, M. et al. (1996) J Biol Chem 271, 29380-5.

11.  Lu, H. et al. (1997) Mol Cell Biol 17, 5923-34.

12.  Ullrich, S.J. et al. (1993) Proc Natl Acad Sci U S A 90, 5954-8.

13.  Kohn, K.W. (1999) Mol Biol Cell 10, 2703-34.

14.  Lohrum, M. and Scheidtmann, K.H. (1996) Oncogene 13, 2527-39.

15.  Knippschild, U. et al. (1997) Oncogene 15, 1727-36.

16.  Oda, K. et al. (2000) Cell 102, 849-62.

17.  Ito, A. et al. (2001) EMBO J 20, 1331-40.

18.  Sakaguchi, K. et al. (1998) Genes Dev 12, 2831-41.

19.  Solomon, J.M. et al. (2006) Mol Cell Biol 26, 28-38.



For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.

9919
Phospho-p53 Antibody Sampler Kit