Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb #2416

Arrestin-β  

No. Size Price
2416S 100 µl ( 10 western blots ) ¥3,900.00 现货查询 购买询价
2416 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 50 Mouse IgG1
IP 1:50

Species cross-reactivity is determined by western blot.

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

Specificity / Sensitivity

Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb detects endogenous levels of β-arrestin 1 only when phosphorylated at serine 412. The antibody does not cross-react with beta-arrestin 2.

Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb鼠单抗能检测内源性丝氨酸(412位点)磷酸化的β-arrestin 1蛋白水平。这种抗体不会与beta-arrestin 2蛋白发生交叉反应。

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser412 of human β-arrestin 1.

该单克隆抗体通过使用合成的与人源β-arrestin 1蛋白丝氨酸(412位点)周围残疾相一致的肽段免疫动物而获得。

Western Blotting

Western Blotting

Western blot analysis of extracts from HEK293 cells alone (-), expressing β-arrestin 1 (wt) or β-arrestin (Ser412Ala) mutant (Ala412), using Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb. Lanes 1 and 3 show endogenous levels of phosphorylated β-arrestin 1.western blot方法检测细胞提取物:只选用能表达β-arrestin 1 (wt) 和 β-arrestin (Ser412Ala)突变体(Ala412) 的HEK293细胞 (-),使用的抗体是Phospho-β-Arrestin 1 (Ser412) (6-24) Mouse mAb。1、3条带表示内源性磷酸化的 β-arrestin 1蛋白水平。

IP

IP

Immunoprecipitation of β-arrestin 1 from HEK293 cells using a polyclonal antibody to phospho-β-arrestin 1 (Ser412), followed by alkaline phosphaphatase (CIP) treatment. β-arrestin 1 was detected by Phospho-beta-Arrestin 1 (Ser412) (6-24) Mouse mAb. CIP treatment abolished the β-arrestin 1 signal, indicating that the monoclonal antibody is phospho-specific.免疫沉淀方法检测细胞提取物:HEK293 细胞中的β-arrestin 1 蛋白,使用的抗体是phospho-β-arrestin 1(Ser412)单克隆抗体,接着用碱性磷酸酶(CIP)处理。用Phospho-beta-Arrestin 1 (Ser412) (6-24) Mouse mAb检测β-arrestin 1蛋白。CIP处理后会使β-arrestin 1蛋白信号消除,表明该单抗是一种特异性磷酸根抗体。

Background

Arrestin proteins function as negative regulators of G protein coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (or X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (or β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestin proteins function as adapters and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in ERK activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestin proteins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).

Arrestin蛋白的作用是G蛋白偶联受体(GPCR)信号传导的负调节因子,同源配体的结合刺激了GPCR的磷酸化,随后Arrestin蛋白结合到磷酸化的GPCR上,导致受体的内化和GPCR信号传导的脱敏(1)。目前已在四种不同的哺乳动物体内发现了Arrestin蛋白,Arrestin1(也被称为S-arrestin)、arrestin 4 (或成为 X-arrestin) 分别存在于视网膜的视杆细胞和视锥细胞中。Arrestin 2 (也被称为β-arrestin 1) and arrestin 3 (或成为 β-arrestin 2) 广泛表达于各种组织,它们能结合到多数GPCR上(2)。β-arrestin 蛋白作为适配器和支架蛋白发挥作用,此外该蛋白也参与其他反应,如通过ERK活化途径将c-Src蛋白家族聚集到GPCRs上 (3,4)。β-arrestins蛋白也参与一些受体酪氨酸激酶信号传导途径(5-8)。其他证据暗示β-arrestin蛋白能转移到细胞核内,并通过结合到转录辅助因子上而调节转录(9,10)。

Erk1/2 constitutively phosphorylates β-arrestin 1 at carboxy-terminal Ser412, which promotes cytosolic localization of the scaffold protein (11). Agonist stimulation of β2-adrenergic receptors results in recruitment of β-arrestin 1 to the plasma membrane and rapid dephosphorylation of arrestin. Dephosphorylation is an essential step of β-arrestin 1-mediated receptor endocytosis, but it is not required for receptor desensitization (12).

Erk1/2结构性磷酸化β-arrestin 1蛋白羧端的丝氨酸(412位点),磷酸化促进了scaffold 蛋白的胞质定位(11)。β2-adrenergic 受体用受体激动剂刺激后导致β-arrestin 1蛋白集中到质膜上,以及arrestin蛋白快速去磷酸化。去磷酸化是β-arrestin 1调节的受体内吞作用中一个重要的环节,但不是受体脱敏所必需的(12)。

  1. Shenoy, S.K. and Lefkowitz, R.J. (2005) Sci STKE 2005, cm10.
  2. Lefkowitz, R.J. and Shenoy, S.K. (2005) Science 308, 512-7.
  3. Luttrell, L.M. et al. (1999) Science 283, 655-61.
  4. Luttrell, L.M. et al. (1999) Curr Opin Cell Biol 11, 177-83.
  5. Luttrell, L.M. and Lefkowitz, R.J. (2002) J Cell Sci 115, 455-65.
  6. Waters, C. et al. (2004) Semin Cell Dev Biol 15, 309-23.
  7. Lefkowitz, R.J. and Whalen, E.J. (2004) Curr Opin Cell Biol 16, 162-8.
  8. Waters, C.M. et al. (2005) Cell Signal 17, 263-77.
  9. Kang, J. et al. (2005) Cell 123, 833-47.
  10. Ma, L. and Pei, G. (2007) J Cell Sci 120, 213-8.
  11. Lin, F.T. et al. (1999) J Biol Chem 274, 15971-4.
  12. Lin, F.T. et al. (1997) J Biol Chem 272, 31051-7.

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