Cell Signaling Technology

Product Pathways - Lymphocyte Signaling

Phospho-SHIP2 (Tyr986/987) Antibody #2008

No. Size Price
2008S 100 µl ( 10 western blots ) ¥4,050.00 现货查询 购买询价 防伪查询
2008 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human, Endogenous 160 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,


Species predicted to react based on 100% sequence homology: Mouse, Rat,

Specificity / Sensitivity

Phospho-SHIP2 (Tyr986/987) Antibody detects endogenous levels of SHIP2 when phosphorylated at Tyr986 and Tyr987.

Phospho-SHIP2 (Tyr986/987) Antibody只能检测内源的在Tyr986和Tyr987位点磷酸化的SHIP2蛋白。

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr986 and Tyr987 of human SHIP2. Antibodies are purified by protein A and peptide affinity chromatography.

此多克隆抗体是通过合成人源对应的SHIP2 Tyr986和Tyr987位点周围的肽段来免疫动物而获得。抗体是通过protein A和多肽亲和层析纯化。

Western Blotting

Western Blotting

Western blot analysis of extracts from K562 cells, untreated or treated with λ phosphatase, using Phospho-SHIP2 (Tyr986/987) Antibody (upper) or total SHIP2 (C76A7) Rabbit mAb #2839 (lower).Western免疫印迹。用Phospho-SHIP2 (Tyr986/987) Antibody (上图) 或 total SHIP2 (C76A7) Rabbit mAb #2839 (下图)研究未经处理的和经λ磷酸酶处理的K562细胞的细胞提取液。


SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate (1). SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus (1,2). Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif (2), followed by tyrosine phosphorylation on the NPXY motif (2). The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1 (3-5). Its effect on calcium flux, cell survival, growth, cell cycle arrest and apoptosis is mediated through the PI3K and Akt pathways (3-5). Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function (6).

包含SH2的肌糖磷酸酶1(SHIP1)是造血组织中的磷酸酶,水解磷脂酰肌醇-3,4,5-三磷酸盐成磷脂酰肌醇-3,4-二磷酸盐(1)。SHIP1是细胞质磷酸酶在其N-末端有SH2区域 和C-末端的两个NPXY Shc结合区域(1,2)。受体交叉结合后, SHIP首先被招募到膜结合处,通过其SH2区域结合到ITIM域的磷酸化酪氨酸上(2),这在酪氨酸磷酸化NPXY域之后(2)。细胞膜的重新定位和NPXY域的磷酸化对SHIP1的调控功能非常重要(3-5)。它通过PI3K和Akt通路影响钙流,细胞的存活,生长,细胞周期和凋亡(3-5)。Tyr1021定位于SHIP1的一个NPXY域内, 而且其磷酸化对SHIP1功能是非常重要的(6)。

SHIP2, a homolog of SHIP1, is highly expressed in heart, skeletal muscle and placenta (7). SHIP2 negatively regulates insulin signaling (8) and polymorphisms in SHIP2 have been linked to hyperglycemia (9). Recent studies also suggest SHIP2 as a therapeutic target for the treatment of both obesity and type 2 diabetes (10,11). Tyr986 and Tyr987 are phosphorylated upon PDGF treatment of 3T3-L1 cells. Phosphorylation of these residues has also been observed in human cancer cells (12-15).

SHIP2是SHIP1的同源基因,在心脏,骨骼肌,胎盘中高表达(7)。SHIP2负调控胰岛素信号(8) ,SHIP2的多态性与高血糖症有关(9)。最近的研究也表明SHIP2作为肥胖症和2型糖尿病的治疗靶标(10,11)。经过PDGF处理的3T3-L1细胞中Tyr986和Tyr987位点被磷酸化。这些位点的磷酸化在人的癌细胞中也有发现(12-15)。

  1. Tridandapani, S. et al. (1997) Mol Cell Biol 17, 4305-11.
  2. Liu, L. et al. (1997) J Biol Chem 272, 8983-8.
  3. Malbec, O. et al. (2001) J Biol Chem 276, 30381-91.
  4. Carver, D.J. et al. (2000) Blood 96, 1449-56.
  5. Scharenberg, A.M. et al. (1998) EMBO J 17, 1961-72.
  6. Sattler, M. et al. (2001) J Biol Chem 276, 2451-8.
  7. Pesesse, X. et al. (1997) Biochem Biophys Res Commun 239, 697-700.
  8. Wada, T. et al. (2001) Mol Cell Biol 21, 1633-46.
  9. Ishida, S. et al. (2006) Pancreas 33, 63-7.
  10. Dyson, J.M. et al. (2005) Int J Biochem Cell Biol 37, 2260-5.
  11. Sasaoka, T. et al. (2006) Pharmacol Ther 112, 799-809.
  12. Artemenko, Y. et al. (2007) J Cell Physiol 211, 598-607.
  13. Goss, V.L. et al. (2006) Blood 107, 4888-97.
  14. Rikova, K. et al. (2007) Cell 131, 1190-203.
  15. Guo, A. et al. (2008) Proc Natl Acad Sci USA 105, 692-7.

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