FGR antibodies target the FGR protein, a member of the Src family of non-receptor tyrosine kinases encoded by the *FGR* gene. Initially identified in the 1980s, FGR (p55-Fgr) shares structural homology with other Src kinases, containing SH3. SH2. and catalytic tyrosine kinase domains. It is predominantly expressed in myeloid cells, B lymphocytes, and monocytes, playing roles in immune cell signaling, adhesion, and phagocytosis. FGR activation is linked to integrin-mediated signaling pathways, regulating cellular responses such as migration, cytokine release, and oxidative burst.
Dysregulation of FGR has been implicated in pathological conditions. Overexpression or hyperactivation of FGR is associated with chronic inflammation, autoimmune disorders, and hematological malignancies, including leukemia and lymphoma. Studies suggest its involvement in rheumatoid arthritis and atherosclerosis due to its role in leukocyte activation and tissue infiltration. Conversely, FGR deficiency may impair immune responses, highlighting its dual regulatory functions.
FGR antibodies are essential tools in biomedical research, enabling the study of FGR expression, phosphorylation status, and interaction networks. They are also explored for diagnostic applications, such as detecting FGR overexpression in tumors, and therapeutic potential, including blocking FGR activity in inflammatory diseases. Challenges remain in understanding tissue-specific FGR functions and developing targeted therapies with minimal off-effects. Ongoing research aims to clarify its precise mechanisms and clinical relevance.