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  3. p53 (DO-7) & CO-0239-647 SignalStar® Oligo-Antibody Pair

p53 (DO-7) & CO-0239-647 SignalStar® Oligo-Antibody Pair #40297

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  • IHC

Order Information # 40297

This product is not sold separately. Please see the SignalStar® Multiplex IHC Panel Builder Tool for ordering information.

    Product Information

    Product Usage Information

    Application Dilution
    SignalStar™ Leica Bond 1:50 - 1:200
    SignalStar™ Manual 1:50 - 1:200

    Storage

    SignalStar conjugates are supplied in PBS (pH 7.2), less than 0.1% sodium azide, 2 mM EDTA, 0.05% Triton X-100, 2 mg/mL BSA, and 50% glycerol. Complementary oligos are supplied in nuclease-free water. Store at -20°C. Do not aliquot the antibody. All components in this kit are stable for at least 12 months when stored at the recommended temperature.

    Product Description

    SignalStar multiplex immunohistochemistry (IHC) is an advanced technology for labeling multiple proteins simultaneously in tissue samples using specific primary antibodies and fluorescent detection reagents. This technology offers accuracy and reliability in visualizing and analyzing protein expression while maintaining spatial context and tissue architecture.

    SignalStar Oligo-Antibody Pairs are compatible with the SignalStar Multiplex IHC Buffer Kits for use in fluorescent multiplex imaging experiments. This product includes the oligo-conjugated antibodies and complementary oligos required for labeling your target protein on up to 10 slides. SignalStar Multiplex IHC Buffer Kits are required to amplify and image the target signal. Multiple oligo-antibody pairs can be conveniently combined into a multiplex panel using the SignalStar Multiplex IHC Panel Builder. SignalStar Multiplex IHC Kits & Reagents are not compatible with all of Cell Signaling Technology® products and protocols that are recommended for use in immunohistochemical assays.

    Protocol

    Specificity / Sensitivity

    p53 (DO-7) Mouse mAb (SignalStar® Conjugate 0239) recognizes endogenous levels of total p53 protein.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant human p53 protein expressed in E. coli.

    Background

    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. Levine, A.J. (1997) Cell 88, 323-31.
    2. Meek, D.W. (1994) Semin Cancer Biol 5, 203-10.
    3. Milczarek, G.J. et al. (1997) Life Sci 60, 1-11.
    4. Shieh, S.Y. et al. (1997) Cell 91, 325-34.
    5. Chehab, N.H. et al. (1999) Proc Natl Acad Sci U S A 96, 13777-82.
    6. Honda, R. et al. (1997) FEBS Lett 420, 25-7.
    7. Tibbetts, R.S. et al. (1999) Genes Dev 13, 152-7.
    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.

    Database Links

    UniProt ID: P04637


    Entrez-Gene Id: 7157


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    For Research Use Only. Not for Use in Diagnostic Procedures.
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