antibody

p53, phosphorylated (Ser315)

P1001-25D

100 ul

polyclonal

domestic rabbit

nonconjugated

phosphorylated

p53, phosphorylated (Ser315)

rabbit

Pab

Phosphorylated

Antibodies

100 ul

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 reduced interaction of p53 with its negative regulator, oncoprotein MDM2 (4). MDM2 inhibits the accumulation of p53 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; the phosphorylations impair 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 ck1d and ck1e both in vitro and in vivo (10,15). Phosphorylation of p53 at Ser46 is important in regulating the ability of p53 to induce apoptosis (16). In vivo phosphorylation at Ser315 has been observed following UV-irradiation, and a Ser315Ala mutant p53 has reduced activity as a transcription factor (17). Aurora A phosphorylates p53 at Ser315 in a cell cycledependent manner leading to MDM2-mediated ubiquitination/ degradation of p53 (18). Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilution: Western Blot: 1:1000 Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot. Store at -20°C. Aliquots are stable for at least 12 months at -20°C. 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.

Hu

Synthetic phosphopeptide corresponding to residues surrounding Ser315 of human p53.

Detects endogenous levels of p53 only when phosphorylated at serine 315. Species Crossreactivity: Human

Purified by Protein A and peptide affinity chromatography.

Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol.

100ul (10 Western mini-blots)

Product Type: Pab Isotype: IgG Host: rabbit Source: human Concentration: 100ul (10 Western mini-blots) Form: Supplied as a liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 100ug/ml BSA, 50% glycerol. Purity: Purified by Protein A and peptide affinity chromatography. Immunogen: Synthetic phosphopeptide corresponding to residues surrounding Ser315 of human p53. Specificity: Detects endogenous levels of p53 only when phosphorylated at serine 315. Species Crossreactivity: Human 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.

WB

-20°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) Blaydes, J.P. et al. (2001) J. Biol. Chem. 276, 4699–4708. (18) Katayama, H. et al. (2004) Nat. Genet. 36, 55–63.

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