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AAT Bioquest

PerCP [Peridinin-Chlorophyll-Protein Complex]

Peridinin chlorophyll (PerCP) is an apocarotenoid pigment that some organisms use in photosynthesis. Many photosynthetic dinoflagellates use peridinin, which absorbs blue-green light in the 470-550 nm range, outside the range accessible to chlorophyll molecules. The peridinin-chlorophyll-protein complex is a specialized molecular complex consisting of a boat-shaped protein molecule with a large central cavity that contains peridinin, chlorophyll, and lipid molecules, usually in a 4:1 ratio of peridinin to chlorophyll. PerCP is commonly used in immunoassays such as fluorescence-activated cell sorting (FACS) and flow cytometry. The fluorophore is covalently linked to proteins or antibodies for use in research applications.
Peridinin chlorophyll (PerCP) is an apocarotenoid pigment that some organisms use in photosynthesis. Many photosynthetic dinoflagellates use peridinin, which absorbs blue-green light in the 470-550 nm range, outside the range accessible to chlorophyll molecules. The peridinin-chlorophyll-protein complex is a specialized molecular complex consisting of a boat-shaped protein molecule with a large central cavity that contains peridinin, chlorophyll, and lipid molecules, usually in a 4:1 ratio of peridinin to chlorophyll. PerCP is commonly used in immunoassays such as fluorescence-activated cell sorting (FACS) and flow cytometry. The fluorophore is covalently linked to proteins or antibodies for use in research applications.
Peridinin chlorophyll (PerCP) is an apocarotenoid pigment that some organisms use in photosynthesis. Many photosynthetic dinoflagellates use peridinin, which absorbs blue-green light in the 470-550 nm range, outside the range accessible to chlorophyll molecules. The peridinin-chlorophyll-protein complex is a specialized molecular complex consisting of a boat-shaped protein molecule with a large central cavity that contains peridinin, chlorophyll, and lipid molecules, usually in a 4:1 ratio of peridinin to chlorophyll. PerCP is commonly used in immunoassays such as fluorescence-activated cell sorting (FACS) and flow cytometry. The fluorophore is covalently linked to proteins or antibodies for use in research applications.
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Physical properties
Molecular weight~35000
SolventWater
Spectral properties
Extinction coefficient (cm -1 M -1)350000
Excitation (nm)477
Emission (nm)678
Storage, safety and handling
Certificate of OriginDownload PDF
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageRefrigerated (2-8 °C); Minimize light exposure
UNSPSC12171501

OverviewpdfSDSpdfProtocol


Molecular weight
~35000
Extinction coefficient (cm -1 M -1)
350000
Excitation (nm)
477
Emission (nm)
678
PerCP (Peridinin-chlorophyll-protein complex) is isolated from Dinophyceae sp. It has an extremely high extinction coefficient, a high quantum efficiency and a large Stokes shift. It is well excited with the Argon laser at 488 nm with its maximum emission peak at 677nm. PerCP protein is commonly used for fluorescent immunolabeling, particularly in applications involving fluorescent-activated cell sorting (FACS). Its cyanine tandem conjugates (such as PerCP-Cy5.5 developed by BD) can be excited with a standard 488 nm laser and emits in the far red at a longer wavelength for multicolor flow cytometric analysis of cells. These multiple emission wavelengths make PerCP- Cyanine conjugates potentially useful fluorochromes for multicolor analysis with FITC, PE and other fluorochromes. PerCP tandem structure may make it more photostable than PerCP alone, which generally photobleaches rapidly with more powerful water-cooled gas lasers. AAT Bioquest offers iFluor protein labeling dyes that are generally brighter and more photostable than the corresponding cyanine dyes of similar wavelengths. iFluor protein labeling dyes are superior alternatives to the cyanine dyes.

Spectrum


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spectrum

Spectral properties

Extinction coefficient (cm -1 M -1)350000
Excitation (nm)477
Emission (nm)678

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Citations


View all 1 citations: Citation Explorer
Optimising biomass and peridinin production in the immobilised cultivation of the dinoflagellate Symbiodinium voratum
Authors: Langenbach, Dorothee
Journal: (2016)

References


View all 46 references: Citation Explorer
Chromophore attachment to phycobiliprotein beta-subunits: phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena Sp. PCC7120
Authors: Zhao KH, Su P, Li J, Tu JM, Zhou M, Bubenzer C, Scheer H.
Journal: J Biol Chem (2006): 8573
Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy
Authors: Petrasek Z, Schmitt FJ, Theiss C, Huyer J, Chen M, Larkum A, Eichler HJ, Kemnitz K, Eckert HJ.
Journal: Photochem Photobiol Sci (2005): 1016
Single-molecule spectroscopy selectively probes donor and acceptor chromophores in the phycobiliprotein allophycocyanin
Authors: Loos D, Cotlet M, De Schryver F, Habuchi S, Hofkens J.
Journal: Biophys J (2004): 2598
Isolation and characterisation of phycobiliprotein rich mutant of cyanobacterium Synechocystis sp
Authors: Prasanna R, Dhar DW, Dominic TK, Tiwari ON, Singh PK.
Journal: Acta Biol Hung (2003): 113
Evaluation of Tolypothrix germplasm for phycobiliprotein content
Authors: Prasanna R, Prasanna BM, Mohammadi SA, Singh PK.
Journal: Folia Microbiol (Praha) (2003): 59
Co-ordinated expression of phycobiliprotein operons in the chromatically adapting cyanobacterium Calothrix PCC 7601: a role for RcaD and RcaG
Authors: Noubir S, Luque I, Ochoa de Alda JA, Perewoska I, T and eau de Marsac N, Cobley JG, Houmard J.
Journal: Mol Microbiol (2002): 749
Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: evidence for rapid evolution of genetic heterogeneity
Authors: Ting CS, Rocap G, King J, Chisholm SW.
Journal: Microbiology (2001): 3171
Phycobiliprotein-Fab conjugates as probes for single particle fluorescence imaging
Authors: Triantafilou K, Triantafilou M, Wilson KM.
Journal: Cytometry (2000): 226
Novel activity of a phycobiliprotein lyase: both the attachment of phycocyanobilin and the isomerization to phycoviolobilin are catalyzed by the proteins PecE and PecF encoded by the phycoerythrocyanin operon
Authors: Zhao KH, Deng MG, Zheng M, Zhou M, Parbel A, Storf M, Meyer M, Strohmann B, Scheer H.
Journal: FEBS Lett (2000): 9
Phycobiliprotein and fluorescence immunological assay
Authors: Wu P., undefined
Journal: Sheng Li Ke Xue Jin Zhan (2000): 82