MONOCLONAL ANTI-MDM2 MOUSE

Monoclonal Anti-MDM2 antibody produced in mouse has been used in:

• immunoblotting
• immunoprecipitation (1 μg/ml)
• fluorescence-activated cell sorting (FACS)
• immunofluorescence (1:200)
• immunohistochemistry
• confocal immunofluorescence
• immunocytochemistry
• enzyme-linked immunosorbent assay (ELISA)

Monoclonal Anti-MDM2 (mouse IgG1 isotype) is derived from the SMP14 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a BALB/c mouse. The murine double minute (mdm2), an E3 ubiquitin ligase comprises an N-terminal p53 domain. The C-terminal domain encompasses the really interesting new gene (RING) domain,?nuclear localization signal (NLS), nucleolar localization signal (NoLS)?and a nuclear export signal?(NES). MDM2 is mapped to the human chromosome 12q15. It is expressed as different splice variants.

Murine double minute (mdm2) mediates the transactivation of the tumor suppressor p53. MDM2 binds to the histone acetyltransferase p300 transcriptional coactivator/histone acetylase to mediate the degradation of p53. The nuclear localization signal of MDM2 mediates its shuttling from the nucleus to the cytoplasm and mediates p53 degradation. In addition to its relationships with p53, MDM2 activates cell proliferation by stimulating the S-phase-inducing transcription factors, E2F1/dimerization partner 1 (DP1). The amplification of the MDM2 gene is detected in the esophagogastric, liver, colon, breast and lung carcinomas. A disturbance in the optimal levels of the MDM2/p53 axis may have an impact on premature aging. Monoclonal antibody reacting specifically with MDM2 is an essential tool in defining the interactions and distributions of MDM2, its function in signaling pathways and mutual regulation of p53.