About ANK1
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 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.