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      Purified Mouse Anti-Human p53
      Purified Mouse Anti-Human p53
      Western blot analysis of p53. A SV-40 transformed rat granulosa cell lysate was probed with anti-human p53 (clone G59-12, Cat. No. 554157) at concentrations of 2.0 (lane 1), 1.0 (lane 2), and 0.5 µg/ml (lane 3). Clone G59-12 identifies p53 at 53 kDa.
      Purified Mouse Anti-Human p53
      Western blot analysis of p53. A SV-40 transformed rat granulosa cell lysate was probed with anti-human p53 (clone G59-12, Cat. No. 554157) at concentrations of 2.0 (lane 1), 1.0 (lane 2), and 0.5 µg/ml (lane 3). Clone G59-12 identifies p53 at 53 kDa.
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      BD Pharmingen™
      Human, Non-Human Primate (QC Testing), Mouse, Rat (Tested in Development)
      Mouse IgG1
      Recombinant full-length human p53
      Intracellular staining (flow cytometry), Western blot (Routinely Tested), Immunohistochemistry-formalin (antigen retrieval required), Immunohistochemistry-frozen (Tested During Development), Immunoprecipitation (Reported)
      53 kDa
      0.5 mg/ml
      AB_395276
      Aqueous buffered solution containing ≤0.09% sodium azide.
      RUO


      Preparation And Storage

      Store undiluted at 4°C. The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
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      Recommended Assay Procedures

      Clone G59-12 conjugated to R-Phycoerythrin (PE) is suggested for flow cytometric analysis of p53 (Cat. No. 557027). Positive control cell lines include SKBR-3 human breast carcinoma cells (ATCC HTB-30) and A431 human vulval carcinoma cells (ATCC CRL-1555). Jurkat T cells (ATCC TIB-152) or MCF-7 human breast carcinoma cells (ATCC HTB-22) are suggested as negative controls. Positive immunostaining is seen in a high proportion of breast and colon carcinomas. p53 staining is not typically detected in normal skin, brain, kidney, lung, stomach, or breast tissue.

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      Product Notices

      1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
      2. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
      3. Sodium azide is a reversible inhibitor of oxidative metabolism; therefore, antibody preparations containing this preservative agent must not be used in cell cultures nor injected into animals. Sodium azide may be removed by washing stained cells or plate-bound antibody or dialyzing soluble antibody in sodium azide-free buffer. Since endotoxin may also affect the results of functional studies, we recommend the NA/LE (No Azide/Low Endotoxin) antibody format, if available, for in vitro and in vivo use.
      4. Species cross-reactivity detected in product development may not have been confirmed on every format and/or application.
      5. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
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      554157 Rev. 8
      Antibody Details
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      G59-12

      p53 is a 53 kD nuclear phosphoprotein that acts as a tumor suppressor protein, and is involved in inhibiting cell proliferation when DNA damage occurs. The gene for p53 is the most commonly mutated gene yet identified in human cancers. Missense mutations occur in tumors of the colon, lung, breast, ovary, bladder and several other organs. The mutant p53 is overexpressed in a variety of transformed cells and the wildtype p53 forms specific complexes with several viral oncogenes including SV40 large T, E1B from adenovirus and E6 from human papilloma virus. Wildtype p53 plays a role as a checkpoint protein for DNA damage during the S-phase of the cell cycle. p53 migrates at a reduced molecular weight of 53 kDa.

      Clone G59-12 recognizes mutant and wild type human, rat and mouse p53 tumor suppressor protein. Recombinant full-length human p53 was used as immunogen. The G59-12 clone was originally characterized by western blot analysis, immunoprecipitation and immunohistochemical staining.

      554157 Rev. 8
      Format Details
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      Purified
      Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
      Purified
      554157 Rev.8
      Citations & References
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      Development References (11)

      1. Cheng J, Yee JK, Yeargin J, Friedmann T, Haas M. Suppression of acute lymphoblastic leukemia by the human wild-type p53 gene. Cancer Res. 1992; 52(1):222-226. (Clone-specific: Immunoprecipitation). View Reference
      2. Gjerset RA, Arya J, Volkman S, Haas M. Association of induction of a fully tumorigenic phenotype in murine radiation-induced T-lymphoma cells with loss of differentiation antigens, gain of CD44, and alterations in p53 protein levels. Mol Carcinog. 1992; 5(3):190-198. (Clone-specific: Immunoprecipitation). View Reference
      3. Jacquemier J, Moles JP, Penault-Llorca F, et al. p53 immunohistochemical analysis in breast cancer with four monoclonal antibodies: comparison of staining and PCR-SSCP results. Br J Cancer. 1994; 69(5):846-852. (Biology). View Reference
      4. Morkve O, Halvorsen OJ, Stangeland L, Gulsvik A, Laerum OD. Quantitation of biological tumor markers (p53, c-myc, Ki-67 and DNA ploidy) by multiparameter flow cytometry in non-small-cell lung cancer. Int J Cancer. 1992; 52(6):851-855. (Biology). View Reference
      5. Stein LS, Stoica G, Tilley R, Burghardt RC. Rat ovarian granulosa cell culture: a model system for the study of cell-cell communication during multistep transformation. Cancer Res. 1991; 51(2):696-706. (Clone-specific). View Reference
      6. Van Meir EG, Roemer K, Diserens AC, et al. Single cell monitoring of growth arrest and morphological changes induced by transfer of wild-type p53 alleles to glioblastoma cells. Proc Natl Acad Sci U S A. 1995; 92(4):1008-1012. (Clone-specific: Immunoprecipitation). View Reference
      7. Vogelstein B. Cancer. A deadly inheritance. Nature. 1990; 348(6303):681-682. (Biology). View Reference
      8. Vojtesek B, Bartek J, Midgley CA, Lane DP. An immunochemical analysis of the human nuclear phosphoprotein p53. New monoclonal antibodies and epitope mapping using recombinant p53. J Immunol Methods. 1992; 151(1-2):237-244. (Biology). View Reference
      9. Yeargin J, Cheng J, Haas M. Role of the p53 tumor suppressor gene in the pathogenesis and in the suppression of acute lymphoblastic T-cell leukemia. Leukemia. 1992; 6(3):85S-91S. (Clone-specific: Immunoprecipitation). View Reference
      10. Yeargin J, Cheng J, Yu AL, Gjerset R, Bogart M, Haas M. P53 mutation in acute T cell lymphoblastic leukemia is of somatic origin and is stable during establishment of T cell acute lymphoblastic leukemia cell lines. J Clin Invest. 1993; 91(5):2111-2117. (Clone-specific: Immunoprecipitation). View Reference
      11. van den Berg FM, Baas IO, Polak MM, Offerhaus GJ. Detection of p53 overexpression in routinely paraffin-embedded tissue of human carcinomas using a novel target unmasking fluid. Am J Pathol. 1993; 142(2):381-385. (Biology). View Reference
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      554157 Rev. 8

      Please refer to Support Documents for Quality Certificates


      Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described


      Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

      For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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