Download Data Sheet p53 mutant (R267W) (with N-terminal (His)10

Data Sheet
Version: 003-13.03.08
Page 1 of 2
p53 mutant (R267W) (with N-terminal (His)10-tag)
Recombinant human protein - unconjugated
Product Information
Catalogue-No.:
DIA P-5121, 5 µg
DIA P-5122, 10 µg
The product has been overfilled by at least 10%
to ensure total recovery of stated quantity.
Concentration:
See vial
Source:
Recombinant Human protein (aa 1 – 393) with
N-terminal (His)10-tag expressed in E. coli.
Characterization: On SDS-PAGE Coomassie Blue stained gel,
the purified recombinant protein shows a band
at 53 kDa.
Mutations:
Arginine 267 to Tryptophan (R267W)
Presentation:
Recombinant human p53 protein in 8M Urea,
100mM NaH2PO4, 10mM Tris pH 8,0.
The protein was purified from E.coli by nickel
chelate chromatography. Purity > 95% according to SDS-PAGE/ Coomassie Blue staining/
Western blot with anti-His-tag antibody. Without
additional proteins or stabilizers.
Applications
ELISA
Inhibition/Neutralization
Western Blot
The optimal dilution for a specific application should be
determined by the investigator.
Background
p53 is a tumor-suppressor gene expressed in a wide variety of tissue types and is involved in regulating cell growth, replication, and apoptosis. The p53 protein (393 aa, phosphoprotein) is a transcription factor, whose activity is regulated by phosphorylation. The normal function of p53 is to effect cell cycle arrest at the G1- and G2-checkpoints in response to DNA
damage. The current model postulates that p53 senses DNA damage and arrests the cell cycle to allow DNA repair to take
place. If repair is not successful, p53 initiates programmed cell death. In normal cells the p53 level is low. In response to
DNA damage or other cellular stress signals the checkpoint function is executed by accumulation of p53.
The control function of p53 includes the transcriptional regulation of several genes including the cell cycle inhibitor p21
WAF1/CIP1/SDI1 , DNA repair gene GADD45 and the apoptotic inducer Bax. p53 has also been shown to induce apoptosis
by means of a direct signaling pathway. p53 directly binds to and acts on several cellular proteins involved in various pathways, including c-Abl or basal transcription factors.
p53 can be functionally inactivated by mutation, most of them being amino acid substitutions. Inactivation can also be the
result of binding to DNA tumor virus encoded proteins such as SV40 large T antigen, adenovirus E1B- and papilloma Virus
E6-proteins or as a consequence of its interaction with the oncogene-encoded protein MDM2.
The p53 tumor suppressor gene has been found to contain mutation in over 50% of human cancers. Many mutations of the
p53 gene have been associated with malignant transformation in a wide variety of human tumors, including breast, ovarian,
bladder, colon, lung, and melanoma.
Storage and Stability
The protein is stable at 4°C during shipment and for short term storage of 2 – 3 weeks. For long term storage, the protein
should be kept frozen at -20°or -80°C. Without aliquoting the protein is stable for one or two cycles of freezing and thawing
only. To avoid repeated freezing and thawing, predilute the protein to not more than 1:10 and aliquot into small volumes,
not smaller than 20µl. For extended storage as a liquid, add an equal volume of glycerol (ACS or better grade) for a final
concentration of 50% followed by storage at -20°C. The protein is stable for up to 12 month when stored at the recommended temperature.
dianova GmbH
Warburgstr. 45 • 20354 Hamburg • Germany
Phone +49 40 45 06 70 • Fax +49 40 45 06 74 90 • www.dianova.de
Data Sheet
Version: 003-13.03.08
Page 2 of 2
References
1.
4.
Greenblatt MS, Bennett WP, Hollstein M, Harris CC.. Mutations in the p53 tumor suppressor gene: clues to cancer
etiology and molecular pathogenesis. Cancer Res. 54(18):4855-78. Review, 1994.
Hengstermann A, Whitaker NJ, Zimmer D, Zentgraf H, Scheffner M. Characterization of sequence elements involved in
p53 stability regulation reveals cell type dependence for p53 degradation. Oncogene 17(22):2933-41, 1998.
Kern SE, Pietenpol JA, Thiagalingam S, Seymour A, Kinzler KW, Vogelstein B. Oncogenic forms of p53 inhibit p53regulated gene expression. Science 256(5058):827-30, 1992.
Lane, D.P. p53 and human cancers. Br Med Bull. 50(3):582-99. Review, 1994.
5.
Lane, D.P. Cancer. p53, guardian of the genome. Nature. 358(6381):15-6, 1992.
6.
Malkin D, Li FP, Strong LC, Fraumeni JF Jr, Nelson CE, Kim DH, Kassel J, Gryka MA, Bischoff FZ, Tainsky MA, et al.
Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasms.
Science 250(4985):1233-8, 1990.
2.
3.
For research only. Not for diagnostic or therapeutic use.
dianova GmbH
Warburgstr. 45 • 20354 Hamburg • Germany
Phone +49 40 45 06 70 • Fax +49 40 45 06 74 90 • www.dianova.de