Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected insect cells.

Both spz proprotein and processed spz protein form disulfide-linked dimers.

spz was purified from conditioned medium. N-terminal sequencing determined the extent of the processed, 12 kDa monomer. Proteins were subjected to SDS-PAGE under non-reducing conditions.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 cells.

Both spz proprotein and processed spz protein form disulfide-linked dimers.

spz was purified from conditioned medium. Proteins were subjected to SDS-PAGE under non-reducing conditions.

spz was collected from bacterial inclusion bodies and refolded, then subjected to size exclusion chromatography.

spz refolded in vitro can form homodimers.

Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.

spz was collected from bacterial inclusion bodies and refolded, then subjected to mass spectrometry for size determination.

Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.

spz refolded in vitro can form homodimers.

spz was collected from bacterial inclusion bodies, refolded and trypsin digested to give an activated, 24 kDa spz dimer.

Interaction in vitro; protein produced as a recombinant fusion protein in bacterial system.

spz forms a disulfide-linked homodimer.

Interaction in vitro; proteins produced as a recombinant fusion proteins in baculovirus and Sf9 cell system.

The spz prodomain fragment binds to the spz C-106 domain

Bait protein was fused to a transmembrane domain, which targets the chimera to the cell surface. The ability of this chimera to recruit prey protein to the cell surface was taken as evidence of direct physical interaction.

Source was live HeLa cells; bait produced from transfected construct; prey secreted from transfected S2 cells.