Alpha-Crystallin is comprised of two polypeptides, alphaA-crystallin (alphaA) and alphaB-crystallin (alphaB), which share 55% amino acid sequence homology [1]. They are the most abundant proteins in lens fiber cells [2,3] and exist as heteroaggregates of approximately 800 kDa that can undergo inter-aggregate subunit exchange [4]. The expression of these two proteins in the lens epithelium, however, is not uniform throughout different regions of the anterior epithelium. AlphaB expression is detected in central epithelium and increases from the central to elongation zones, where epithelial cells differentiate into fiber cells. AlphaA, however, is not detected in the central epithelium. The relative proportion of alphaA and alphaB changes from a molar ratio of 1:3 in the pericentral and germative zones to a molar ratio of 3:1 in the elongation zone and fiber cells [2,3]. These differences in the relative proportions of alphaA and alphaB within the lens suggest different functions for the two subunits in the developing lens.