Hi All,
I have a simple question about the complex formation between macromolecular complex and antibody. My protein is stable in the presence of the 5mM DTT and under these conditions the reducing environment is too strong for the antibody to survive. I am also now trying to check the stability of the protein in lower molar concentration of DTT, but as DTT being a strong reducing agent it might still pose a threat to the disintegrate the antibody. Does anybody have experience in handling protein-antibody complexes using other reducing agents? Your answers and help in this regard will be highly appreciated. Thanks, Jan
