Two major intrinsic membrane polypeptides of molecular weights 22K and 26K have been isolated and antisera for each prepared against highly purified preparations. The lack of reactivity of these antibodes in several other tissues suggests that they are unique to the lens. These antisera were used for localization of these polypeptides in adult human lenses by indirect immunofluorescent staining. Neither of the polypeptides is found in the epithelial cells; however those cells commencing differentiation show some fluorescent staining. The elongating fiber cells of the bow region show cytoplasmic staining for both 22K and 26K. This may reflect their sites of synthesis. In this region the species of 22K studied showed no localization in the membrane; however, 26K is concentrated at the membrane as evidenced by the intense band of fluorescent staining in this region. In the lens inner cortical region, there is a loss of cytoplasmic staining and both polypeptides appear to be membrane bound. This redistribution of the membrane polypeptides occurring in the inner cortex is at the site of considerable lens fiber contour alterations.