I am working with a purchased product called Jacalin lectin (catalog no. L-1150-25), got that lectin in powder or precipitated form, so I dissolved that lectin in the buffer as the company recommended (10mM HEPES buffered saline, 0.1mM CaCl2 pH 8.5) and dissolved it in 5ml buffer to make the final concentration of 5mg/ml. Sir,  I am using this lectin for conjugation with gold-nanoparticle in order to develop a diagnostic kit, but, somehow, lectin forms oligomers with itself (dimerization), and it is creating a problem in the conjugation experiment. I looked for the reason behind this, and I found that the protein forms dimers because of high concentration, the hydrophobic interaction occurs between protein molecules. Now, I want to know how to resolve this problem to get protein back in monomeric form to perform conjugation experiments.