Monoclonal antibody specifically recognizing modification...

Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of... – Animal cell – per se – expressing immunoglobulin – antibody – or...

Reexamination Certificate

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C435S331000, C435S344000, C435S344100, C530S300000, C530S327000, C530S350000, C530S387700, C530S387900, C530S388250, C530S388800, C530S388850

Reexamination Certificate

active

08062887

ABSTRACT:
The present invention provides a monoclonal antibody recognizing modification after translation of p53 in a manner specific to a modification site, an antibody microarray comprising the antibody immobilized on a substrate, etc. Disclosed is a monoclonal antibody which reacts specifically with a peptide consisting of an amino acid sequence of at least 6 consecutive amino acids containing a predetermined amino acid residue of the amino acid sequence represented by SEQ ID NO: 1, wherein the amino acid residue is phosphorylated or acetylated, or with a peptide having one to several arbitrary amino acids added to the above peptide, but does not react with the above peptide which is not phosphorylated or acetylated.

REFERENCES:
patent: 6441140 (2002-08-01), Comb et al.
patent: 6884597 (2005-04-01), Taya et al.
patent: 2005/0023912 (2005-02-01), Lin et al.
patent: 2006/0035296 (2006-02-01), Taya et al.
patent: 1050581 (2000-11-01), None
patent: 1184665 (2002-03-01), None
patent: 2000-325086 (2000-11-01), None
patent: 2001-161398 (2001-06-01), None
patent: 2003-093056 (2003-04-01), None
patent: WO-9936532 (1999-07-01), None
patent: WO-9946574 (1999-09-01), None
patent: WO-0072011 (2000-11-01), None
patent: WO 2004/29622 (2004-04-01), None
Craig et al., “Novel phosphorylation sites of human tumour suppressor protein p53 at Ser20 and Thr18 that disrupt the binding of mdm2 (mouse double minute 2) protein are modified in human cancers”, Biochem J., Aug. 15, 1999; 133-141, vol. 342(Pt 1).
Otvos et al., “A monoclonal antibody to a multiphosphorylated, conformational epitope at the carboxy-terminus of p53”, Biochim Biophys Acta., Sep. 16, 1998, 457-74, vol. 1404(3).
Sakaguchi et al., “DNA damage activates p53 through a phosphorylation-acetylation cascade”, Genes Dev., Sep. 15, 1998, 2831-2841, vol. 12(18).
Taya, 53 no aphosphorylation to acetylation ni yoru Saibo Kino no Seigyo', Cell Technology, 2003, 29-33, vol. 22(1).
Wang et al., “Identification and Characterization of a Novel p300-mediated p53 Acetylation Site, Lysine 305”, J. Biol. Chem., 25568-25576, 2003, vol. 278 (28).
International Preliminary Report on Patentability issued Oct. 3, 2007 during the Prosecution of International Application No. PCT/JP2006/306921.
Written Opinion issued Oct. 3, 2007 during the Prosecution of International Application No. PCT/JP2006/306921.
Banin et al., “Enhanced phosphorylation of p53 by ATM in response to DNA damage”; Science; Sep. 11, 1998; 1674-7; vol. 281 (5383).
Bulavin et al,. “Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation”; The EMBO Journal; 1999; 6845-6854; vol. 18.
Chehab et al., “Chk2/hCds1 functions as a DNA damage checkpoint in G1 by stabilizing p53”; Genes Dev.; Feb. 1, 2000; 278-288; vol. 14(3).
Dumaz et al., “Serine 15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2”; The EMBO Journal; 1999; 7002-7010; vol. 18.
Gu et al., “Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain.”; Cell.; Aug. 22, 1997; 595-606; vol. 90(4).
Higashimoto et al., “Human p53 Is Phosphorylated on Serines 6 and 9 in Response to DNA Damage-inducing Agents”; J. Biol. Chem.; Jul. 28, 2000; 23199-23203, vol. 275(30).
Lambert et al., “Phosphorylation of p53 Serine 15 Increases Interaction with CBP”; J Biol Chem; Dec. 4, 1998; 33048-33053; vol. 273(49).
Oda et al., “p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53”; Cell; Sep. 15, 2000; 849-62; vol. 102(6).
Saito et al., “ATM mediates phosphorylation at multiple p53 sites, including Ser(46), in response to ionizing radiation”; J Biol Chem.; Apr. 12, 2002; 12491-4; vol. 277(15).
Sanchez-Prie et al., “A Role for the p38 Mitogen-activated Protein Kinase Pathway in the Transcriptional Activation of p53 on Genotoxic Stress by Chemotherapeutic Agents1”; Cancer Research; May 1, 2000; 2464-2472; vol. 60.
Shieh et al., “The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites”; Genes Dev.; Feb. 1, 2000; 289-300; vol. 14(3).
Tanaka et al., “A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage”; Nature; 2000; 42-49; vol. 404.
Tibbetts et al., “A role for ATR in the DNA damage-induced phosphorylation of p53”; Genes Dev.; Jan. 15, 1999; 152-157; vol. 13(2).
Waterman et al., “ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins”; Nature Genetics; 1998; 175-178; vol. 19.
Yoichi Taya; “Structure of p53 and Sites for its Phosphorylation and Acetylation”; Experimental Medicine; 2001; 1050-1084; vol. 19(9), with English Translation thereof.
Office Action issued in Japanese Application No. 2007-511193 (and English translation theref), mailed May 27, 2011.

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