Rabbit polyclonal antibody to SHIP1 (M1014)

The major translational product of the v~Fms oncogene, originally isolated from the McDonough strain of feline sarcoma virus, has been identified as a 170 kDa glycoprotein with intrinsic tyrosine kinase activity. The v~Fms human cellular homolog, c~Fms, has been molecularly cloned and mapped to band q34 on chromosome 5, and identified as the receptor for hematopoietic ligand, CSF~1. Ligand~induced activation of the intrinsic CSF~1R protein tyrosine kinase triggers its interaction with cytoplasmic effector molecules. One such effector molecule, SHIP~1 p145 (SH2~containing~inositol phosphatase), associates with activated Fms. SHIP~1 contains two phosphotyrosine~binding domains (PTB), a unique amino terminal SH2 domain, a proline~rich region, and two highly conserved motifs found among inositol phosphate 5~phosphatases. SHIP~1 displays both phosphatidylinositol 3,4,5~triphosphate and inositol 1, 3, 4, 5 ~tetrakisphosphate polyphosphate 5~phosphatase activity. Evidence suggests that SHIP~1 may modulate Ras signaling in addition to inositol signaling pathways