Used as a homobifunctional crosslinking agent in biochemical and protein research. It reacts primarily with primary amines, such as lysine residues and N-termini of proteins, forming covalent bonds between closely spaced amino groups. The disulfide bridge in its structure allows for reversible crosslinking under reducing conditions, making it valuable in capturing and isolating protein complexes for analysis. Commonly applied in protein-protein interaction studies, affinity purification, and structural biology. Its water-soluble nature and cleavable linkage support controlled experiments where crosslinks need to be broken after complex stabilization.