Upstream / Downstream
Explore pathways related to this product.
the purchase of 3 or more products
Find answers on our FAQs page.
- Additional protein information
- Analytical tools
Phospho-SHIP2 (Tyr1135) Antibody #2007
This product is discontinued
Gallery: Phospho-SHIP2 (Tyr1135) Antibody #2007
Phospho-SHIP2 (Tyr1135) Antibody detects endogenous levels of SHIP2 when phosphorylated at Tyr1135.
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1135 of human SHIP2. Antibodies are purified by protein A and peptide affinity chromatography.
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).
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). Tyr1135 is phosphorylated in human cancer cells (12-15).
For Research Use Only. Not For Use In Diagnostic Procedures. Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.