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     All lanes use the Antibody at 1:2K dilution for 1 hour at room temperature.    

  
  

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     Western blot analysis of SHIP1 expression in Daudi cell lysate.    

  
  

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     Immunohistochemical analysis of paraffin-embedded rat spleen, using SHIP Antibody.    

  
  

SHIP (Src homology 2 domain-containing inositol phosphatase) is a lipid phosphatase that plays a critical role in regulating immune cell signaling. Discovered in the mid-1990s, SHIP is primarily expressed in hematopoietic cells, including B cells, T cells, mast cells, and macrophages. Its structure includes an N-terminal SH2 domain, a central catalytic domain with inositol phosphatase activity, and C-terminal proline-rich regions for protein interactions.

Functionally, SHIP modulates phosphatidylinositol 3-kinase (PI3K) signaling by hydrolyzing phosphatidylinositol (3.4.5)-trisphosphate (PIP3) to phosphatidylinositol (3.4)-bisphosphate (PIP2), thereby limiting Akt activation and downstream pathways involved in cell survival, proliferation, and activation. This negative regulatory role makes SHIP crucial for maintaining immune homeostasis, preventing excessive inflammation, and controlling autoimmune responses.

SHIP antibodies are essential tools for studying its expression, localization, and activity in immune regulation. Dysregulation of SHIP has been linked to diseases like leukemia, allergies, and autoimmune disorders. Therapeutic strategies targeting SHIP (e.g., agonists or inhibitors) are under exploration to modulate immune responses in cancer or inflammatory conditions. Research on SHIP continues to uncover its broader roles in metabolism, apoptosis, and phagocytosis, highlighting its significance as a multifaceted regulator in immunity and disease.