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     The image is immunohistochemistry of paraffin-embedded Human brain tissue using P06089(SFR1 Antibody) at dilution 1/30. (Original magnification: ×200)    

  
  

SFR1 (also known as C12orf4 or SWIM8) is a protein involved in DNA repair and homologous recombination, primarily through its interaction with the SWI5-SFR1 complex. This complex plays a critical role in stabilizing RAD51. a key recombinase essential for repairing DNA double-strand breaks (DSBs) by homologous recombination repair (HRR). SFR1 acts as a mediator, facilitating RAD51 filament formation on single-stranded DNA, thereby enhancing the efficiency and accuracy of DSB repair. Dysregulation of SFR1 has been linked to genomic instability, which is associated with cancer progression and chemoresistance.

SFR1 antibodies are valuable tools for studying DNA repair mechanisms, particularly in cancer research and reproductive biology. They enable the detection and quantification of SFR1 protein levels in cells or tissues via techniques like Western blotting, immunofluorescence, or immunohistochemistry. These antibodies also aid in exploring SFR1’s interaction partners (e.g., SWI5. RAD51) and its role in maintaining genome integrity. Additionally, SFR1 expression patterns have been investigated in germ cells, where homologous recombination is crucial during meiosis. Research using SFR1 antibodies has contributed to understanding how defects in HRR pathways influence infertility, cancer susceptibility, and responses to DNA-damaging therapies like PARP inhibitors. Commercial SFR1 antibodies are typically developed in rabbits or mice, targeting specific epitopes within its N-terminal or C-terminal regions.