GADS Recombinant Rabbit mAb (S-5667)

GADS (Grb2-related adaptor protein 2, also known as GRAP2, Mona, or Grf40) is an intracellular adaptor protein that plays a key role in T lymphocyte signal transduction. It is composed of an N-terminal SH3 domain and an SH2 domain, a central region connected by a long flexible amino acid sequence, and a C-terminal SH3 domain. The core function of GADS is that, following T cell receptor (TCR) engagement, it binds LAT through its SH2 domain while simultaneously binding SLP-76 through its C-terminal SH3 domain, thereby bridging these two adaptor proteins and assembling a multi-protein signaling complex that is essential for T cell activation. Studies have shown that thymocytes from GADS-deficient mice exhibit severe proliferative defects, and the association between SLP-76 and LAT is uncoupled, confirming that GADS is an indispensable adaptor protein in CD3 signaling. In addition, the C-terminal SH3 domain of GADS displays a unique homodimerization pattern when binding SLP-76 peptides, which may represent a regulatory mechanism that enhances the specificity of signal transduction. Structural studies have shown that, despite containing a putative flexible region, full-length GADS exists as a monomer in solution and adopts a relatively compact overall structure.