52412
R-Phycoerythrin
BioReagent, passes test for gel electrophoresis
Sinônimo(s):
R-PE, phycobiliprotein
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About This Item
Produtos recomendados
linha de produto
BioReagent
concentração
≥10.0 mg/mL (UV)
técnica(s)
electrophoresis: suitable
fluorescência
λex 542 nm; λem 575 nm in 0.1 M phosphate pH 7.2
adequação
passes test for gel electrophoresis
temperatura de armazenamento
2-8°C
Categorias relacionadas
Descrição geral
R-Phycoerythrin or R-PE is a fluorescent probe belonging to the group of phycobiliproteins obtained from macroalgae. R-Phycoerythrin (R-PE) is a protein acting as a photosynthetic accessory pigment in red algae (Rhodophyta). It is an oligomeric protein of 240 kDa, with 6 α (about 20 kDa), 6 β (about 20 kDa), and 1 γ (about 30 kDa) subunits. Phycobiliproteins are water-soluble light-harvesting proteins with a high fluorescent property.
Aplicação
R-Phycoerythrin (R-PE) is useful in the laboratory as a fluorescence-based indicator for the presence of cyanobacteria and a variety of immunofluorescence applications. R-PE is a useful fluoroprobe in various electrophoretic procedures. R-Phycoerythrin (R-PE) proteins detect mercury ions in soil and groundwater samples. Phycoerythrin has been widely used in food, cosmetics, immunodiagnostics, and analytical reagents.
Nota de análise
The product is suspended in 150 mM sodium phosphate, 60% ammonium sulfate, 1 mM EDTA, 1 mM sodium azide, pH 7.0 and must be dialyzed against conjugation buffer or PBS before conjugation.A566/A280 >4.6, A620/A566 <0.03, A566/A498 <1.5
Código de classe de armazenamento
12 - Non Combustible Liquids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves
Certificados de análise (COA)
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R Rossano et al.
Journal of biotechnology, 101(3), 289-293 (2003-03-05)
R-Phycoerythrin (R-PE) is a protein acting as a photosynthetic accessory pigment in red algae (Rodophyta). This protein has gained importance in many biotechnological applications in food science, immunodiagnostic, therapy, cosmetics, protein and cell labelling, and analytical processes. In this paper
Xiaobin Wang et al.
The Analyst, 144(12), 3892-3897 (2019-05-24)
Mercury, as one of the most prevalent toxic metals released by various natural and anthropogenic processes, causes severe pollution of soil and groundwater. In this work, R-phycoerythrin (R-PE) proteins encapsulated into ZIF-8 composite thin films were prepared via a solid-confinement
Hoda Hossein-Nejad et al.
The Journal of chemical physics, 136(2), 024112-024112 (2012-01-21)
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Justin D Cohen et al.
Chembiochem : a European journal of chemical biology, 13(6), 888-894 (2012-04-12)
A screen of Trp37 mutants of Escherichia coli lipoic acid ligase (LplA) revealed enzymes capable of ligating an aryl-aldehyde or aryl-hydrazine substrate to LplA's 13-residue acceptor peptide. Once site-specifically attached to recombinant proteins fused to this peptide, aryl-aldehydes could be
Lu-Ning Liu et al.
Journal of biotechnology, 116(1), 91-100 (2005-01-18)
Phycoerythrins have been widely used in food, cosmetics, immunodiagnostics and analytical reagents. An efficient one-step chromatography method for purification of R-phycoerythrins from Polysiphonia urceolata was described in this paper. Pure R-phycoerythrin was obtained with an absorbance ratio A(565)/A(280) of 5.6
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