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AAT Bioquest

ReadiUse™ CL-APC [Cross linked-Allophycocyanin] *Ammonium Sulfate-Free*

Cross linked-Allophycocyanin (CL-APC) is a phycobiliprotein isolated from Spirulina sp., a blue-green alga. Like other phycobiliproteins, APC is strongly fluorescent, with an extremely high absorptivity and a high quantum efficiency. AAT Bioquest offers this ReadiUse™ APC that can be readily used for any labelings without any purifications required.
Cross linked-Allophycocyanin (CL-APC) is a phycobiliprotein isolated from Spirulina sp., a blue-green alga. Like other phycobiliproteins, APC is strongly fluorescent, with an extremely high absorptivity and a high quantum efficiency. AAT Bioquest offers this ReadiUse™ APC that can be readily used for any labelings without any purifications required.
Cross linked-Allophycocyanin (CL-APC) is a phycobiliprotein isolated from Spirulina sp., a blue-green alga. Like other phycobiliproteins, APC is strongly fluorescent, with an extremely high absorptivity and a high quantum efficiency. AAT Bioquest offers this ReadiUse™ APC that can be readily used for any labelings without any purifications required.
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Physical properties
Molecular weight~105000
SolventWater
Spectral properties
Correction Factor (280 nm)0.195
Extinction coefficient (cm -1 M -1)730000
Excitation (nm)651
Emission (nm)660
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageRefrigerated (2-8 °C); Minimize light exposure
UNSPSC12171501
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Show More (60)

OverviewpdfSDSpdfProtocol


Molecular weight
~105000
Correction Factor (280 nm)
0.195
Extinction coefficient (cm -1 M -1)
730000
Excitation (nm)
651
Emission (nm)
660
Cross linked-Allophycocyanin (CL-APC) is a phycobiliprotein isolated from Spirulina sp., a blue-green alga. Like other phycobiliproteins, APC is strongly fluorescent, with an extremely high absorptivity and a high quantum efficiency. It is a protein which can be easily linked to antibodies and other proteins by conventional protein cross-linking techniques without altering its spectral characteristics. APC is the least stable among the major phycobiliproteins, susceptible to dissociation at low concentrations including concentrations at which some assays are performed. CL-APC is chemically cross-linked between α and ß subunits, and is much more stable than APC. The crosslinked APC has improved stability in aqueous solution. However, all the commercial APC materials are sold in concentrated ammonium sulfate buffers. The commercial APC materials from other vendors require the tedious dialysis or other purifications performed before it can be used for labeling purposes. AAT Bioquest offers this ReadiUse™ APC that can be readily used for any labelings without any purifications required. Our highly purified ReadiUse™ APC facilitates the rapid APC conjugations to antibodies and other proteins such as streptavidin and other secondary reagents.

Spectrum


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spectrum

Spectral properties

Correction Factor (280 nm)0.195
Extinction coefficient (cm -1 M -1)730000
Excitation (nm)651
Emission (nm)660

Product Family


NameExcitation (nm)Emission (nm)Extinction coefficient (cm -1 M -1)Correction Factor (280 nm)
ReadiUse™ Preactivated APC6516607300000.195

Images


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