| 货号 | 56343S |
| 同种亚型 | Rabbit IgG |
| 反应种属 | Human\Mouse\Rat |
| 来源宿主 | Rabbit IgG |
| 应用 | WB, IP |
| 目标/特异性 | FLIP (D5J1E) Rabbit mAb recognizes endogenous levels of total FLIP protein. This antibody recognizes both the long and short isoforms of FLIP. |
| 使用方法 | W IP |
| 供应商 | CST |
| 灵敏度 | Endogenous |
| 背景 | Cellular FLIP (FLICE inhibitory protein) is a regulator of apoptosis that has various names, such as c-FLIP (1), Casper (2), CLARP (3), FLAME (4), I-FLICE (5), MRIT (6), CASH (7), and Usurpin (8). FLIP is expressed as two alternative splice isoforms, FLIP short (FLIPS) and FLIP long (FLIPL). FLIPS contains two death effector domains (DEDs) like those found on the death receptor adaptor protein FADD and the pro-domain of caspase-8. FLIPL shares significant homology with caspase-8 (FLICE), and contains an additional death effector domain, but FLIPL lacks the catalytic active site of the caspases and does not have protease activity. Both FLIP isoforms have been reported to interact with FADD and pro-caspase-8. The role of FLIP in apoptosis is controversial as some research studies have reported it to be anti-apoptotic, while others claim that it is pro-apoptotic. Overexpression of FLIPL can lead to caspase-8 heterodimers that produce an active protease, resulting in apoptosis. However, at physiological levels, it is thought that the binding of FLIP to the DED of FADD results in inhibition of caspase-8 processing. Reduction of FLIP by siRNA or gene targeting sensitizes cells to death receptor-mediated apoptosis. FLIP has also been implicated in the resistance of cancer cells to apoptosis and is upregulated in some cancer types including Hodgkins lymphoma and ovarian and colon carcinomas (9). |
| 存放说明 | -20C |
| 计算分子量 | 55, 25 |
| 参考文献 | 1 . Irmler, M. et al. (1997) Nature 388, 190-5. 2 . Shu, H.B. et al. (1997) Immunity 6, 751-63. 3 . Inohara, N. et al. (1997) Proc Natl Acad Sci U S A 94, 10717-22. 4 . Srinivasula, S.M. et al. (1997) J Biol Chem 272, 18542-5. 5 . Hu, S. et al. (1997) J Biol Chem 272, 17255-7. 6 . Han, D.K. et al. (1997) Proc Natl Acad Sci U S A 94, 11333-8. 7 . Rasper, D.M. et al. (1998) Cell Death Differ 5, 271-88. 8 . Goltsev, Y.V. et al. (1997) J Biol Chem 272, 19641-4. 9 . Kataoka, T. (2005) Crit Rev Immunol 25, 31-58. |
Western blot analysis of extracts from various cell lines using FLIP (D5J1E) Rabbit mAb (upper) or β-Actin (D6A8) Rabbit mAb #8457 (lower). KARPAS cell line source: Dr. Abraham Karpas at the University of Cambridge. | |
Western blot analysis of extracts from A549 cells, transfected with 100 nM SignalSilence® Control siRNA (Unconjugated) #6568 (-), SignalSilence® FLIP siRNA I #12372 (+), or SignalSilence® FLIP siRNA II #12407 (+), using FLIP (D5J1E) Rabbit mAb (upper) or β-Actin (D6A8) #8457 (lower). The FLIP (D5J1E) Rabbit mAb confirms silencing of FLIP expression, while the β-Actin (D6A8) Rabbit mAb is used as a loading control. | |
Immunoprecipitation of FLIP from KARPAS-299 cell extracts. Lane 1 represents 10% input, lane 2 is precipitated with Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is FLIP (D5J1E) Rabbit mAb. Western blot was performed using FLIP (D5J1E) Rabbit mAb. A conformation specific secondary antibody was used to avoid cross reactivity with IgG. KARPAS cell line source: Dr. Abraham Karpas at the University of Cambridge. | |
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with a construct expressing full-length human FLIP (hFLIP; +), using FLIP (D5J1E) Rabbit mAb. |
