p53 Proteins, Antibodies, cDNA Clones, ELISA Kits Research Reagents

TP53 (Tumor Protein P53) is a protein coding gene located on human chromosome 17p13.1. TP53 is also known as P53, BCC7, LFS1, BMFS5, and TRP53. The human TP53 gene encodes a 43653 Da protein containing 393 amino acids. The TP53 protein is ubiquitously expressed in spleen, lymph node and other tissues. Among its related pathways are Apoptosis Modulation and Signaling and Regulation of TP53 Activity through Acetylation. TP53 is related to DNA-binding transcription factor activity and protein heterodimerization activity. TP63 is an important paralog of TP53 gene. TP53 is associated with some diseases, including Li-Fraumeni Syndrome and Osteogenic Sarcoma.

p53 Protein (1)

    p53 Antibody (7)

      p53 ELISA Kit & Match Antibody ELISA Pair Set (1)

      p53 cDNA Clone (47)

      NM_131327.2

      In expression vector

      NM_001328587.1

      In expression vector

      p53 Background

      p53, also known as Tp53, is a DNA-binding protein which belongs to the p53 family. It contains transcription activation, DNA-binding, and oligomerization domains. p53 protein is expressed at low level in normal cells and at a high level in a variety of transformed cell lines, where it's believed to contribute to transformation and malignancy. p53 (TP53) is a transcription factor whose protein levels and post-translational modification state alter in response to cellular stress (such as DNA damage, hypoxia, spindle damage). Activation of p53 begins through a number of mechanisms including phosphorylation by ATM, ATR, Chk1 and MAPKs. MDM2 is a ubiquitin ligase that binds p53 and targets p53 for proteasomal degradation. Phosphorylation, p14ARF and USP7 prevent MDM2-p53 interactions, leading to an increase in stable p53 tetramers in the cytoplasm. Further modifications such as methylation and acetylation lead to an increase in Tp53 binding to gene specific response elements. Tp53 regulates a large number of genes (>100 genes) that control a number of key tumor suppressing functions such as cell cycle arrest, DNA repair, senescence and apoptosis. Whilst the activation of p53 often leads to apoptosis, p53 inactivation facilitates tumor progression. It is postulated to bind to a p53-binding site and activate expression of downstream genes that inhibit growth and/or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Defects in TP53 are a cause of esophageal cancer, Li-Fraumeni syndrome, lung cancer and adrenocortical carcinoma.

      p53 References

      • Bakhrat A, et al. (2010) Drosophila Chk2 and p53 proteins induce stage-specific cell death independently during oogenesis. Apoptosis. 15(12):1425-34.
      • Kurzhals RL, et al. (2011) Chk2 and p53 are haploinsufficient with dependent and independent functions to eliminate cells after telomere loss. PLoS Genet. 7(6):e1002103.
      • Pardi N, et al. (2011) In vivo effects of abolishing the single canonical sumoylation site in the C-terminal region of Drosophila p53. Acta Biol Hung. 62(4):397-412.
      • Wells BS, et al. (2012) Maintenance of imaginal disc plasticity and regenerative potential in Drosophila by p53. Dev Biol. 361(2):263-76.

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