β_L-Crystallin from bovine eye lens

β-Crystallin is the most heterogeneous of the crystallin classes, with at least six different gene products, at least ten different post-translational modifications, and quaternary structure variants from dimers to octamers. However, all sequences are highly conserved through evolution.

βL-Crystallin is one of the major lens proteins that aggregates under UV. A chaperone mixture of D-pathethine and N-acetyl carnosine has the ability to slow down the rate of photoaggregatin βL-Crystallin, and may be important in the prevention of cataract.