Bcl-2

Programmed cell death (apoptosis) is a normal physiologic process which occurs during embryonic development as well as in maintenence of tissue homeostasis. The apoptotic program is characterized by certain morphological features. These include changes in the plasma membrane such as loss of membrane asymmetry and attachment, a condensation of the cytoplasm and nucleus, and internucleosomal cleavage of DNA. In the final stages, the dying cells become fragmented into "apoptotic bodies" which are rapidly eliminated by phagocytic cells without eliciting significant inflammatory damage to surrounding cells. Members of the Bcl-2 family play a major role in regulating the cellular response to apoptotic signals. Bcl-2 is considered to be a novel proto-oncogene because it blocks apoptosis in many cell types. Bcl-2 is thought to provide selective survival advantage for cells by blocking apoptosis and thus may contribute to tumorigenesis. Bcl-2 is a 26 kD intracellular, integral membrane protein found primarily in the nuclear envelope, endoplasmic reticulum and outer mitochondrial membrane. Clone 3F11 reacts with mouse Bcl-2. It does not cross-react with human Bcl-2. Gel purified recombinant mouse Bcl-2 protein was used as immunogen. Clone A19-3 is an Armenian hamster IgG isotype control which is specific for the hapten trinitrophenol (TNP). This hapten is not expressed on human cells or human cell lines. The solutions are free of unconjugated antibody. The 3F11 and A19-3 FITC conjugates are matched in F/P ratios. The optimum F/P ratio was experimentally determined by flow cytometric analysis.

3F11

Intracellular staining (flow cytometry) (Routinely Tested), Immunofluorescence, Immunohistochemistry-frozen, Immunoprecipitation, Western blot (Reported)

Mouse (QC Testing)

Bcl-2

研发参考(9) 1. Alexander-Miller MA, Derby MA, Sarin A, Henkart PA, Berzofsky JA. Supraoptimal peptide-major histocompatibility complex causes a decrease in bc1-2 levels and allows tumor necrosis factor alpha receptor II-mediated apoptosis of cytotoxic T lymphocytes. J Exp Med. 1998; 188(8):1391-1399. (Clone-specific: Western blot). 2. Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 1993; 53(19):4701-4714. (Biology). 3. Novack DV, Korsmeyer SJ. Bcl-2 protein expression during murine development. Am J Pathol. 1994; 145(1):61-73. (Clone-specific: Immunohistochemistry, Western blot). 4. Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell. 1993; 74(4):609-619. (Clone-specific: Immunoprecipitation). 5. Reed JC, Tsujimoto Y, Alpers JD, Croce CM, Nowell PC. Regulation of bcl-2 proto-oncogene expression during normal human lymphocyte proliferation. Science. 1987; 236(4806):1295-1299. (Biology). 6. Veis DJ, Sentman CL, Bach EA, Korsmeyer SJ. Expression of the Bcl-2 protein in murine and human thymocytes and in peripheral T lymphocytes. J Immunol. 1993; 151(5):2546-2554. (Immunogen: Flow cytometry, Fluorescence microscopy, Immunohistochemistry, Western blot). 7. Veis DJ, Sorenson CM, Shutter JR, Korsmeyer SJ. Bcl-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell. 1993; 75(2):229-240. (Clone-specific: Western blot). 8. Williams GT. Programmed cell death: apoptosis and oncogenesis. Cell. 1991; 65(7):1097-1098. (Biology). 9. Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 1997; 275(5303):1129-1132. (Biology).