| 货号 | 57220S |
| 反应种属 | Mouse |
| 来源宿主 | Rabbit |
| 应用 | WB |
| 目标/特异性 | Phospho-RIP3 (Thr231/Ser232) Antibody (Mouse Specific) recognizes endogenous levels of RIP3 protein only when phosphorylated at Thr231/Ser232. This antibody may not react with single phosphorylation at either site. |
| 使用方法 | Western Blotting (1:1000) |
| 供应商 | CST |
| 灵敏度 | Endogenous |
| 背景 | The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8). Receptor-interacting protein 3 (RIP3) was originally found to interact with RIP and the TNF receptor complex to induce apoptosis and activation of NF-κB (9,10). It has subsequently been shown that the association between RIP and RIP3 is a key component of a signaling pathway that results in programmed necrosis (necroptosis), a necrotic-like cell death induced by TNF in the presence of caspase inhibitors (11-13). RIP3 is phosphorylated at Ser227 and targets the phosphorylation of mixed lineage kinase domain-like protein (MLKL), which is critical for necroptosis (14). In mice, RIP3 is phosphorylated at Thr231 and Ser232, leading to association with MLKL and necroptosis (15). |
| 存放说明 | -20C |
| 计算分子量 | 46-62 |
| 参考文献 | 1 . Meylan, E. and Tschopp, J. (2005) Trends Biochem Sci 30, 151-9. 2 . Hsu, H. et al. (1996) Immunity 4, 387-96. 3 . Stanger, B.Z. et al. (1995) Cell 81, 513-23. 4 . Ting, A.T. et al. (1996) EMBO J 15, 6189-96. 5 . Kelliher, M.A. et al. (1998) Immunity 8, 297-303. 6 . Devin, A. et al. (2000) Immunity 12, 419-29. 7 . Zhang, S.Q. et al. (2000) Immunity 12, 301-11. 8 . Lin, Y. et al. (1999) Genes Dev 13, 2514-26. 9 . Chen, W. et al. (2013) J Biol Chem 288, 16247-61. 10 . Yu, P.W. et al. (1999) Curr Biol 9, 539-42. 11 . Sun, X. et al. (1999) J Biol Chem 274, 16871-5. 12 . Zhang, D.W. et al. (2009) Science 325, 332-6. 13 . He, S. et al. (2009) Cell 137, 1100-11. 14 . Cho, Y.S. et al. (2009) Cell 137, 1112-23. 15 . Sun, L. et al. (2012) Cell 148, 213-27. |
Western blot analysis of L-929 cells, untreated (-), or treated with combinations of the following treatments as indicated: Z-VAD (20 μM, added 30 min prior to other compounds; +), mouse TNF-α (20 ng/ml, 4 hr; +), and SM-164 (100 nM, 4 hr; +), using Phospho-RIP3 (Thr231/Ser232) Antibody (Mouse Specific) (upper) or RIP3 (D8J3L) Rabbit mAb #15828 (lower). | |
Western blot analysis of L-929 cells, untreated (-), or treated with combinations of the following treatments as indicated: Z-VAD (20 μM, added 30 min prior to other compounds; +), mouse TNF-α (20 ng/ml, 2 hr; +), SM-164 (100 nM, 2 hr; +), and necrostatin-1 (Nec-1, 50 μM, 2 hr; +), using Phospho-RIP3 (Thr231/Ser232) Antibody (Mouse Specific) (upper) or RIP3 (D8J3L) Rabbit mAb #15828 (lower). |
