About CRYBB1
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]

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.