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 PerCP
Peridinin-Chlorophyll-Protein (PerCP) is a red-emitting fluorescent protein isolated from algae that can be excited by the 488 nm blue laser and captured with a 670/30 nm bandpass filter. PerCP exhibits a large Stokes' Shift, with an excitation peak at 482 nm and an emission peak at 675 nm. PerCP is was historically used in flow cytometry, however it is highly susceptible to photobleaching and has poor stability. Alternatives like BB700, NovaFluor Blue 690 or PerCP-eFluor™ 710 are preferred. PerCP is a generic dye that has no sole manufacturer.