|Other Names||Apoptosis-stimulating of p53 protein 2, Bcl2-binding protein, Bbp, Renal carcinoma antigen NY-REN-51, Tumor suppressor p53-binding protein 2, 53BP2, p53-binding protein 2, p53BP2, TP53BP2, ASPP2, BBP|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-stimulating activity is inhibited by its interaction with DDX42.|
|Cellular Location||Cytoplasm, perinuclear region. Nucleus. Note=Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42|
|Tissue Location||Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocyte. Reduced expression in breast carcinomas expressing a wild-type TP53 protein. Overexpressed in lung cancer cell lines.|
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Provided below are standard protocols that you may find useful for product applications.
TP53BP2 is a member of the ASPP(apoptosis-stimulating protein of p53) family of p53 interactingproteins. The protein contains four ankyrin repeats and an SH3domain involved in protein-protein interactions. It is localized tothe perinuclear region of the cytoplasm, and regulates apoptosisand cell growth through interactions with other regulatorymolecules including members of the p53 family. Multiple transcriptvariants encoding different isoforms have been found for this gene.
Rose, J. Phd, et al. Mol. Med. (2010) In press :Zhao, J., et al. Hepatology 51(1):142-153(2010)Hirata, H., et al. J. Urol. 182(2):721-727(2009)Kweekel, D.M., et al. Br. J. Cancer 101(2):357-362(2009)Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)
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