The peridinin-chlorophyll-protein complex (PCP or PerCP) is a soluble molecular complex consisting of the peridinin-chlorophyll a-protein bound to peridinin, chlorophyll, and lipids. The peridinin molecules absorb light in the blue-green wavelengths (470 to 550 nm) and transfer energy to the chlorophyll molecules with extremely high efficiency.

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.

Peridinin-Chlorophyll-Protein (PerCP) is a 35.5 kDa fluorescent peridinin-chlorophyll-protein complex isolated from dinoflagellates. Jackson ImmunoResearch offers the form found in Dinophyceae sp. It has a broad spectrum of excitation with the main peak at 482 nm, and a long Stokes shift to an emission peak at 677 nm.

Peridinin-chlorophyll proteins (PerCP) are natural light-harvesting carotenoid-protein complexes derived from phytoplankton and first described well over 100 years ago.1 Modern studies have shown these proteins to be able to absorb light preferentially in the blue-green spectrum2 and to have a relatively large Stokes shift of emission.

Peridinin chlorophyll protein-Cyanine5.5 (PerCP-Cyanine5.5) is a photostable tandem dye excited from the 488 nm laser. It is stable in fixative, and stained cells can be stored overnight. Less-abundant intracellular antigens stained with PerCP-Cyanine5.5 can often be reliably detected in multicolor flow cytometry experiments.

Peridinin is a light-harvesting apocarotenoid, a pigment associated with chlorophyll and found in the peridinin-chlorophyll-protein (PCP) light-harvesting complex in dinoflagellates, best studied in Amphidinium carterae. [1]

Peridinin is a light-harvesting pigment associated with chlorophyll and found in the peridinin chlorophyll binding protein (PerCP); a light harvesting protein found in dinoflagellates.