Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

EWS Antibody #11910

sc-28327   sc-28865   sc-48404  

No. Size Price
11910S 100 µl ( 10 western blots ) ¥3,100.00 现货查询 购买询价
11910 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat, Endogenous 85 Rabbit
IP 1:50

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,

Specificity / Sensitivity

EWS Antibody recognizes endogenous levels of total EWS protein.

EWS Antibody能够检测内源性EWS总蛋白水平。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly142 of human EWS protein. Antibodies are purified by protein A and peptide affinity chromatography.

该多克隆抗体是采用合成的与人源EWS蛋白 Gly142残基周围序列相对应的肽段免疫动物而生产的。并经过Protein A和多肽亲和层析纯化。

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using EWS Antibody.Western blot方法检测不同细胞系的提取物,使用的抗体为EWS Antibody。

IP

IP

Immunoprecipitation of EWS from HeLa cell extracts using Normal Rabbit IgG #2729 (lane 2) or EWS Antibody (lane 3). Lane 1 is 10% input. Western blot analysis was performed using EWS Antibody.从 HeLa细胞提取物中免疫沉淀EWS,使用的抗体为Normal Rabbit IgG #2729 (lane 2) 或 EWS Antibody (Mouse Specific) (lane 3)。Lane 1为10% input。 使用EWS Antibody进行Western blot检测。

Background

The Ewing sarcoma (EWS) protein is a member of the multifunctional FET (FUS, EWS, and TAF15) family of proteins (1,2). These proteins are RNA and DNA binding proteins that are thought to be important for both transcriptional regulation and RNA processing. EWS can be found as part of a fusion protein with various E-twenty six (ETS) family transcription factors, most commonly Fli-1, in the Ewing sarcoma family of tumors (1-4). The amino terminus of the EWS protein, containing the transcriptional activation domain, is fused to the DNA binding domain of the ETS transcription factor, causing aberrant expression of target genes (1-5). EWS interacts with the transcription initiation complex via TFIID and RNA polymerase II subunits, as well as transcriptional regulators, such as Brn3A and CBP/p300, which suggests a role for EWS in transcriptional regulation (1,6-9). EWS also interacts with multiple components of the splicing machinery, implicating a role for EWS in RNA processing (1,10-12). EWS regulates the expression of cyclin D1, which controls G1-S phase transition during the cell cycle, at the level of transcriptional activation and mRNA splicing. The EWS-Fli-1 fusion protein has been shown to promote the expression of the cyclin D1b splice variant in Ewing sarcoma cells (13). In addition, EWS regulates the DNA damage-induced alternative splicing of genes involved in DNA repair and stress response and is required for cell viability upon DNA damage (14). Consistent with these results, EWS knockout mice display hypersensitivity to ionizing radiation and premature cellular senescence, suggesting a role for EWS in homologous recombination and maintenance of genomic stability (15).

尤文氏肉瘤(EWS)蛋白是多功能FET(FUS、 EWS和TAF15)蛋白家族的成员(1,2)。这些蛋白是RNA和DNA结合蛋白,被认为对转录调控和RNA加工都有重要作用。在尤文氏肉瘤肿瘤家族中发现,EWS可以与多种E-twenty six (ETS)家族转录因子,最常见的是Fli-1形成融合蛋白(1-4)。EWS的氨基末端含有一个转录激活结构域,与ETS转录因子的DNA结合结构域融合在一起,从而引起目的基因的异常表达(1-5)。EWS可以通过TFIID以及RNA聚合酶II 亚单位与转录起始复合物相互作用,与Brn3A 和 CBP/p300等转录因子也是一样的,这都暗示着EWS在转录调控中的作用(1,6-9)。此外EWS还能与剪接机器中的多种成分产生相互作用,参与RNA 加工(1,10-12)。EWS能够从转录激活和mRNA加工水平上调控Cyclin D1的表达,而Cyclin D1可以控制细胞周期中G1-S期转换。EWS-Fli-1融合蛋白已经被证明能够促进尤文氏肉瘤细胞中cyclin D1b 剪接异构体的表达(13)。另外,EWS可调控基因中DNA损伤诱导的选择性剪接作用从而参与DNA修复以及应激反应,并且是DNA损伤后细胞生存所需要的。(14)。与这些结果一致的是,EWS敲除小鼠会呈现出对电离辐射过敏和过早细胞衰老,这些都暗示着,EWS在同源重组和基因组稳定性维持中的作用(15)。

  1. Law, W.J. et al. (2006) Brief Funct Genomic Proteomic 5, 8-14.
  2. Kovar, H. (2011) Sarcoma 2011, 837474.
  3. Delattre, O. et al. (1992) Nature 359, 162-5.
  4. May, W.A. et al. (1993) Mol Cell Biol 13, 7393-8.
  5. Sorensen, P.H. et al. (1994) Nat Genet 6, 146-51.
  6. Bertolotti, A. et al. (1996) EMBO J 15, 5022-31.
  7. Bertolotti, A. et al. (1998) Mol Cell Biol 18, 1489-97.
  8. Araya, N. et al. (2003) J Biol Chem 278, 5427-32.
  9. Thomas, G.R. and Latchman, D.S. Cancer Biol Ther 1, 428-32.
  10. Chansky, H.A. et al. (2001) Cancer Res 61, 3586-90.
  11. Yang, L. et al. (2000) J Biol Chem 275, 37612-8.
  12. Knoop, L.L. and Baker, S.J. (2001) J Biol Chem 276, 22317-22.
  13. Sanchez, G. et al. (2008) Proc Natl Acad Sci U S A 105, 6004-9.
  14. Paronetto, M.P. et al. (2011) Mol Cell 43, 353-68.
  15. Li, H. et al. (2007) J Clin Invest 117, 1314-23.

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