| 货号 | 5841T |
| 同种亚型 | Rabbit IgG |
| 反应种属 | Human,Mouse,Rat, |
| 来源宿主 | Rabbit IgG |
| 应用 | WB, ChIP |
| 目标/特异性 | Phospho-FRA1 (Ser265) (D22B1) Rabbit mAb recognizes endogenous levels of FRA1 protein only when phosphorylated at Ser265. This antibody may also cross-react with phospho-FRA2, but does not cross-react with phospho-c-Fos or phospho-FosB. |
| 使用方法 | WB(1:1000) ChIP (1:50) |
| 供应商 | CST |
| 灵敏度 | Endogenous |
| 背景 | The Fos family of nuclear oncogenes includes c-Fos, FosB, Fos-related antigen 1 (FRA1), and Fos-related antigen 2 (FRA2) (1). While most Fos proteins exist as a single isoform, the FosB protein exists as two isoforms: full-length FosB and a shorter form, FosB2 (Delta FosB), that lacks the carboxy-terminal 101 amino acids (1-3). The expression of Fos proteins is rapidly and transiently induced by a variety of extracellular stimuli including growth factors, cytokines, neurotransmitters, polypeptide hormones, and stress. Fos proteins dimerize with Jun proteins (c-Jun, JunB, and JunD) to form Activator Protein-1 (AP-1), a transcription factor that binds to TRE/AP-1 elements and activates transcription. Fos and Jun proteins contain the leucine-zipper motif that mediates dimerization and an adjacent basic domain that binds to DNA. The various Fos/Jun heterodimers differ in their ability to transactivate AP-1 dependent genes. In addition to increased expression, phosphorylation of Fos proteins by Erk kinases in response to extracellular stimuli may further increase transcriptional activity (4-6). Phosphorylation of c-Fos at Ser32 and Thr232 by Erk5 increases protein stability and nuclear localization (5). Phosphorylation of FRA1 at Ser252 and Ser265 by Erk1/2 increases protein stability and leads to overexpression of FRA1 in cancer cells (6). Following growth factor stimulation, expression of FosB and c-Fos in quiescent fibroblasts is immediate, but very short-lived, with protein levels dissipating after several hours (7). FRA1 and FRA2 expression persists longer and appreciable levels can be detected in asynchronously growing cells (8). Deregulated expression of c-Fos, FosB, or FRA2 can result in neoplastic cellular transformation; however, Delta FosB lacks the ability to transform cells (2,3). |
| 存放说明 | -20C |
| 计算分子量 | 40 |
| 参考文献 | 1 . Tulchinsky, E. (2000) Histol Histopathol 15, 921-8. 2 . Dobrazanski, P. et al. (1991) Mol Cell Biol 11, 5470-8. 3 . Nakabeppu, Y. and Nathans, D. (1991) Cell 64, 751-9. 4 . Rosenberger, S.F. et al. (1999) J Biol Chem 274, 1124-30. 5 . Sasaki, T. et al. (2006) Mol Cell 24, 63-75. 6 . Basbous, J. et al. (2007) Mol Cell Biol 27, 3936-50. 7 . Kovary, K. and Bravo, R. (1991) Mol Cell Biol 11, 2451-9. 8 . Kovary, K. and Bravo, R. (1992) Mol Cell Biol 12, 5015-23. |
Chromatin immunoprecipitations were performed with cross-linked chromatin from 4 x 106 PC-12 cells starved overnight and treated with β-NGF #5221 (50ng/ml) for 2h and either 10 μl of Phospho-FRA1 (Ser265) (D22B1) Rabbit mAb or 2 μl of Normal Rabbit IgG #2729 using SimpleChIP® Enzymatic Chromatin IP Kit (Magnetic Beads) #9003. The enriched DNA was quantified by real-time PCR SimpleChIP® Rat CCRN4L Promoter Primers #7983, rat DCLK1 promoter primers, and SimpleChIP® Rat GAPDH Promoter Primers #7964. The amount of immunoprecipitated DNA in each sample is represented as signal relative to the total amount of input chromatin, which is equivalent to one. | |
Western blot analysis of extracts from HeLa cells, serum-starved overnight, and either left untreated or treated with TPA #4174 for 4 hours, using Phospho-FRA1 (Ser265) (D22B1) Rabbit mAb #5841 (upper) and FRA1 (D80B4) Rabbit mAb #5281 (lower). Antibody phospho-specificity is shown by treating lysates with λ phosphatase. |
