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Merck
CN

PC461

Sigma-Aldrich

PhosphoDetect Anti-p53 (pSer¹⁵) (Ab-6) Rabbit pAb

liquid, Calbiochem®, from rabbit

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About This Item

UNSPSC Code:
12352203
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biological source

rabbit

Quality Level

antibody product type

primary antibodies

form

liquid

does not contain

preservative

species reactivity

human

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

isotype

IgG

shipped in

wet ice

storage temp.

−20°C

General description

Rabbit polyclonal antibody supplied as undiluted serum. Recognizes the ~53 kDa p53 phoshorylated at Ser15.
This PhosphoDetect Anti-p53 (pSer¹⁵) (Ab-6) Rabbit pAb is validated for use in Immunoblotting, Paraffin Sections for the detection of p53 (pSer¹⁵) (Ab-6).
This product has been discontinued.


Recognizes the ~53 kDa p53 protein phosphorylated at Ser15. Does not recognizes unphosphorylated p53.

Immunogen

Human
a synthetic phosphopeptide [VEPPLpSQETFS(C)] corresponding to amino acids 10-20 surrounding the Ser¹⁵ phosphorylation site of human p53

Application


Immunoblotting (1:5000-1:10,000)
Paraffin Sections (1:1000-1:3000, heat pre-treatment required)

Physical form

Undiluted serum.

Preparation Note

Following initial thaw, aliquot and freeze (-20°C).

Analysis Note

Positive Control
MCF7 cells or prostate carcinoma tissue

Other Notes

Does not recognizes unphosphorylated p53. Antibody should be titrated for optimal results in individual systems.
Levine, A.J. 1997. Cell88, 323.
Meek, D.W. 1997. Pathol. Biol. Paris45, 804.
Miller, S.D., et al. 1997. Mol. Cell. Biol.17, 2194.
Pellegata, N.S., et al. 1996. Proc. Natl. Acad. Sci. USA93, 15209.
Sturzbecher, H.-W., et al. 1996. EMBO J.15, 1992.
Argarwal, M.L., et al. 1995. Proc. Natl. Acad. Sci. USA92, 8493.
Götz, C. and Montenarh, M. 1995. Int. J. Oncology6, 1129.
Reed, M. et al. 1995. Proc. Natl. Acad. Sci. USA92, 9455.
Waldman, T., et al. 1995. Cancer Res.55, 5187.
Cho, Y., et al. 1994. Science265, 346.
Clarke, A.R., et al. 1994. Oncogene9, 1767.
El-Deiry, W.S., et al. 1994. Cancer Res.54, 1169.
Greenblatt, M.S., et al. 1994. Cancer Res.54, 4855.
Lane, D.P. 1992. Nature358, 15.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Standard Handling (A)

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Storage Class Code

10-13 - German Storage Class 10 to 13

Regulatory Information

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Rajashree A Deshpande et al.
Nucleic acids research, 45(9), 5255-5268 (2017-04-04)
The Mre11-Rad50-Nbs1(Xrs2) (MRN/X) complex is critical for the repair and signaling of DNA double strand breaks. The catalytic core of MRN/X comprised of the Mre11 nuclease and Rad50 adenosine triphosphatase (ATPase) active sites dimerizes through association between the Rad50 ATPase
Cai Bowen et al.
Cell reports, 4(3), 516-529 (2013-07-31)
The prostate tumor suppressor NKX3.1 augments response to DNA damage and enhances survival after DNA damage. Within minutes of DNA damage, NKX3.1 undergoes phosphorylation at tyrosine 222, which is required for a functional interaction with ataxia telangiectasia mutated (ATM) kinase.
Zhi Guo et al.
Cell cycle (Georgetown, Tex.), 9(24), 4805-4811 (2010-12-15)
The Ataxia-Telangiectasia mutated (ATM) kinase is regarded as the major regulator of the cellular response to DNA double strand breaks (DSBs). In response to DSBs, ATM dimers dissociate into active monomers in a process promoted by the Mre11-Rad50-Nbs1 (MRN) complex.
Gary G Chiang et al.
Methods in molecular biology (Clifton, N.J.), 281, 125-141 (2004-06-29)
Members of the phosphoinositide-3-kinase-related kinase (PIKK) family, which includes mTOR, ATM, ATR, and hSMG-1, play important roles in regulating the cellular response to environmental stimuli. Despite the similarity of their catalytic domain to that of phosphoinositide-3-kinase, these extremely large (>250
Ji-Hoon Lee et al.
The Journal of biological chemistry, 288(18), 12840-12851 (2013-03-26)
The Ataxia Telangiectasia-Mutated (ATM) protein kinase is recruited to sites of double-strand DNA breaks by the Mre11/Rad50/Nbs1 (MRN) complex, which also facilitates ATM monomerization and activation. MRN exists in at least two distinct conformational states, dependent on ATP binding and

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