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     Western blot analysis of SHP1 in Human tonsil, Daudi, Jurkat and Raji lysates using SHP1 antibody.    

  
  

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     Immunoprecipitation analysis of SHP1 in Raji lysates using SHP1 antibody.    

  
  

SHP1 (Src homology region 2 domain-containing phosphatase-1), also known as PTPN6. is a protein tyrosine phosphatase predominantly expressed in hematopoietic cells. It plays a critical role in negatively regulating signaling pathways by dephosphorylating key tyrosine residues on target proteins. Structurally, SHP1 contains two N-terminal SH2 domains that mediate interactions with phosphorylated signaling molecules and a C-terminal catalytic domain responsible for its phosphatase activity. Its function is essential for modulating immune responses, cell differentiation, and apoptosis. Dysregulation of SHP1 has been implicated in autoimmune diseases, cancers (e.g., leukemia, lymphoma), and inflammatory disorders, where loss of function or reduced expression often correlates with hyperactive signaling in pathways like JAK/STAT, MAPK, or B-cell receptor signaling.

SHP1 antibodies are essential tools for studying its expression, localization, and activity in both physiological and pathological contexts. These antibodies are widely used in techniques such as Western blotting, immunohistochemistry, and flow cytometry to detect SHP1 in research models or clinical samples. Specific clones or epitope-targeted antibodies are validated for applications, ensuring accurate quantification of SHP1 levels or phosphorylation states. Given its therapeutic potential as a drug target, SHP1 antibodies also aid in screening inhibitors or evaluating therapeutic efficacy in preclinical studies. Proper antibody validation remains crucial due to cross-reactivity risks with homologous phosphatases like SHP2 (PTPN11).