Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-EphA2 (Tyr594) Antibody #3970

No. Size Price
3970S 100 µl ( 10 western blots ) ¥4,050.00 现货查询 购买询价 防伪查询
3970 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human, Transfected Only 135 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,

Specificity / Sensitivity

Phospho-EphA2 (Tyr594) Antibody detects transfected levels of EphA2 proteins only when phosphorylated on Tyr594. This antibody does not cross-reacted with other activated protein tyrosine kinases.

磷酸化EphA2 (Tyr594)的抗体仅在EphA2蛋白的Tyr594位点磷酸化时能检测到转染的EphA2蛋白的表达。本抗体不与其它激活的酪氨酸蛋白激酶发生交叉反应。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr594 of human EphA2. Antibodies are purified by protein A and peptide affinity chromatography.

多克隆抗体通过用多肽免疫动物得到,该磷酸化多肽是根据人的EphA2蛋白Tyr594附近的氨基酸序列合成的。抗体经过protein A和亲和层析纯化。

Western Blotting

Western Blotting

Western blot analysis of cell extracts from 293-T cells, transfected with human EphA2 expression construct, untreated or stimulated with B61-Fc ligand, using Phospho-EphA2 (Tyr594) Antibody (upper) or EphA2 Antibody #3974 (lower). 用抗磷酸化EphA2 (Tyr594)的抗体(上)或抗EphA2的抗体 #3974(下)对经过或未经B61-Fc配体刺激的转染了人EphA2表达组件的293-T细胞的裂解液进行免疫印迹检测。


The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, the ephrins stimulate the kinase activity of the Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyrosines 324/327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

Eph受体是研究的最为清楚的酪氨酸激酶受体家族(RTKs)。根据其序列的相似性和一子集配体的倾向性可将它们分为两组:结合基磷脂酰肌醇锚定的麻黄素A配体的EphA受体; 结合具有跨膜区和胞内区的麻黄素B蛋白的EphB 受体(1,2)。Eph 受体及其配体与多种疾病相关,包括肿瘤(3)。Eph A 和B配体都有双重功能。作为RTK配体,麻黄素激活Eph受体的激酶活性以及激活表达该受体细胞的信号通路。麻黄素的胞外区的聚集足以完成这项功能(4)。麻黄素的第二项功能称为“反向信号调节”,凭借胞内区的酪氨酸磷酸化,能够与表达配体的细胞中许多激活信号通路的其它蛋白相互作用(5)。许多刺激都能使麻黄素B的酪氨酸位点磷酸化,包括与麻黄素B受体结合、Src激酶的激活以及受PDGF和 FGF刺激 (6)。酪氨酸 324/327的磷酸化被认为是体内麻黄素 B1的主要磷酸化位点(7)。

Phosphorylation of Tyr594 was identified in several tumor cell lines (8,9). It was demonstrated that phosphorylated Tyr588 and Tyr594 of EphA2 provide binding sites for guanine nucleotide exchange factors Vav2 and Vav3, which may be involved in regulation of cell migration (10).

Tyr594位点的磷酸化在许多肿瘤细胞系中存在(8, 9)。有证据显示EphA2的Tyr588 和Tyr594位点的磷酸化为鸟苷酸交换因子Vav2 和 Vav3提供了结合位点,这可能与细胞的迁移调控有关(10)。

  1. Wilkinson, D.G. (2000) Int Rev Cytol 196, 177-244.
  2. Klein, R. (2001) Curr Opin Cell Biol 13, 196-203.
  3. Dodelet, V.C. and Pasquale, E.B. (2000) Oncogene 19, 5614-9.
  4. Holder, N. and Klein, R. (1999) Development 126, 2033-44.
  5. Brückner, K. et al. (1997) Science 275, 1640-3.
  6. Palmer, A. et al. (2002) Mol Cell 9, 725-37.
  7. Kalo, M.S. et al. (2001) J Biol Chem 276, 38940-8.
  8. Guo, A. et al. (2008) Proc Natl Acad Sci USA 105, 692-697.
  9. Rikova, K. et al. (2007) Cell 131, 1190-1203.
  10. Fang, W.B. et al. (2008) J. Biol. Chem. 283, 16017-16026.

Application References

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