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2000
Volume 11, Issue 1
  • ISSN: 1389-2010
  • E-ISSN: 1873-4316

Abstract

p53, a tumor suppressor and a transcription factor, binds DNA in a sequence-specific manner. In more than half of human cancers, p53 has been found to be mutated with the loss of DNA-binding ability. In this review, we focus on the sensitive detection of interaction of tumor suppressor p53 with double-stranded DNA bearing the consensus sequence and proteins, such as monoclonal antibodies recognizing the p53 protein and metalloprotein. Relying on the specific binding of p53 to DNA and antibodies, quantitative determination of wild-type and mutant p53 proteins in normal and cancer cell lysates has been achieved.

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/content/journals/cpb/10.2174/138920110790725366
2010-01-01
2025-04-13
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/content/journals/cpb/10.2174/138920110790725366
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  • Article Type:
    Research Article
Keyword(s): cell lysates; consensus sequence; DNA; Interaction; metalloprotein; monoclonal antibodies; p53
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