Render Target: STATIC
Render Timestamp: 2024-11-21T13:49:11.837Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-30 10:36:11.217
Product last modified at: 2024-10-24T14:15:12.512Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

p53 (DO-7) Mouse mAb (BSA and Azide Free) #46565

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  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 53
    Source/Isotype Mouse IgG2b
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    This product is the carrier free version of product #48818. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

    This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN, or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

    BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

    Formulation

    Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

    For standard formulation of this product see product #48818.

    Storage

    Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

    Specificity / Sensitivity

    p53 (DO-7) Mouse mAb (BSA and Azide Free) 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.
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