About Alpha-crystallin protein FVRTVSLPV (Dextramer)
Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC). [provided by RefSeq, Jan 2014]

About PE
Phycoerythrin (PE, R-PE) is a red-emitting fluorescent protein-chromophore complex that can be excited the 488-nm blue, 532-nm green, or 561-nm yellow-green laser with increasing efficiency and captured with a 586/14 nm bandpass filter. PE has an excitation peak at 565 nm and an emission peak at 578 nm. PE is 240kD in size and has an extinction coefficient of ~2x10^6 which makes it one of the brightest fluorophores available and a potent donor upon which to build tandem fluorophores with longer Stoke's Shifts.