antibody

p53, phosphorylated (Ser15) (Tumor Suppressor Protein, Oncogene Protein) (AlexaFluor®488)

P1001-27D4

100 ul

monoclonal

mouse

AF488

phosphorylated

8A24(16G8)

p53, phosphorylated (Ser15) (Tumor Suppressor Protein, Oncogene Protein) (AlexaFluor®488)

mouse

Mab

AlexaFluor®488

Phosphorylated

Antibodies

100 ul

8A24(16G8)

IgG

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, oncoprotein MDM2 (4). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (6,7). p53 can apparently 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 (4,5). Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability and activity (8,9). p53 is phosphorylated at Ser392 in vivo (11,12) and by CAK in vitro (12). Phosphorylation of p53 at Ser392 is altered in human tumors (14) and has been reported to influence the growth suppressor function, DNA binding and transcriptional activation of p53 (10,11,13). p53 is phosphorylated at Ser6 and Ser9 by CK1δ and CK1ε both in vitro and in vivo (10,15). 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). Applications: Suitable for use in ELISA, Flow Cytometry. Other applications not tested. Recommended Dilution: Immunofluorescence (IF-IC) 1:10 Flow Cytometry 1:10. Direct flow cytometric analysis of human cells. Optimal dilutions to be determined by the researcher. Storage and Stability: Store at 2-8°C. Do Not Freeze. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer. AlexaFluor conjugates are sensitive to light.

Hu

Synthetic phosphopeptide corresponding to residues surrounding Ser15 of human p53 (KLH). Conjugated to Alexa Fluor® 488 under optimal conditions with an F/P ratio of 2-6.

Detects endogenous levels of human p53 only when phosphorylated at Ser15. The antibody does not cross-react with p53 phosphorylated at other sites.

Purified

Supplied as a liquid in PBS, pH 7.2, 2mg/ml BSA, 0.09% sodium azide.

Not determined

Product Type: Mab Isotype: IgG Clone No: 8A24(16G8) Host: mouse Source: human Concentration: Not determined Form: Supplied as a liquid in PBS, pH 7.2, 2mg/ml BSA, 0.09% sodium azide. Purity: Purified Immunogen: Synthetic phosphopeptide corresponding to residues surrounding Ser15 of human p53 (KLH). Conjugated to Alexa Fluor® 488 under optimal conditions with an F/P ratio of 2-6. Specificity: Detects endogenous levels of human p53 only when phosphorylated at Ser15. The antibody does not cross-react with p53 phosphorylated at other sites. Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

FC IF

4°C

(1) Levine, A.J. (1997) Cell 88, 323-331. (2) Meek, D.W. (1994) Semin. Cancer Biol. 5, 203-210. (3) Milczarek, G.J. et al. (1997) Life Sci. 60, 1-11. (4) Shieh, S.Y. et al. (1997) Cell 91, 325-334. (5) Tibbetts, R.S. et al. (1999) Genes Dev. 13, 152-157. (6) Chehab, N.H. et al. (1999) Proc. Natl. Acad. Sci. USA 96, 13777-13782. (7) Honda, R. et al. (1997) FEBS Lett. 420, 25-27. (8) Shieh, S.Y. et al. (1999) EMBO J. 18, 1815-1823. (9) Hirao, A. et al. (2000) Science 287, 1824-1827. (10) Kohn, K.W. (1999) Mol. Biol. Cell 10, 2703-2734. (11) Hao, M. et al. (1996) J. Biol. Chem. 271, 29380- 29385. (12) Lu, H. et al. (1997) Mol. Cell. Biol. 17, 5923-5934. (13) Lohrum, M. and Scheidtmann, K.H. (1996) Oncogene 13, 2527-2539. (14) Ulrich, S.J. et al. (1993) Proc. Natl. Acad. Sci. USA 90, 5954-5958. (15) Knippschild, U. et al. (1997) Oncogene 15, 1727-1736. (16) Oda, K. et al. (2000) Cell 102, 849-862. (17) Ito, A. et al. (2001) EMBO J. 20, 1331-1340. (18) Sakaguchi, K. et al. (1998) Genes Dev. 12, 2831-2841. (19) Solomon, J.M. et al. (2006) Mol. Cell. Biol. 26, 28-38.

https://usbio-images.r.worldssl.net/prodimages/1/P1001-27D4_1.jpg