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
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
SHIP1 (M1014) polyclonal antibody detects endogenous levels of SHIP1 protein.
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