52412
R-Phycoerythrin
BioReagent, passes test for gel electrophoresis
Synonym(s):
R-PE, phycobiliprotein
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About This Item
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product line
BioReagent
Quality Level
concentration
≥10.0 mg/mL (UV)
technique(s)
electrophoresis: suitable
fluorescence
λex 542 nm; λem 575 nm in 0.1 M phosphate pH 7.2
suitability
passes test for gel electrophoresis
storage temp.
2-8°C
Related Categories
General description
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.
Application
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.
Analysis Note
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
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (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
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
Hoda Hossein-Nejad et al.
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We present a formalism to quantify the contribution of path-interference in phonon-mediated electronic energy transfer. The transfer rate between two molecules is computed by considering the quantum mechanical amplitudes associated with pathways connecting the initial and final sites. This includes
Yu-Rong Chen et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(21), 8310-8315 (2012-05-09)
The red/far-red light photoreceptor phytochrome mediates photomorphological responses in plants. For light sensing and signaling, phytochromes need to associate with open-chain tetrapyrrole molecules as the chromophore. Biosynthesis of tetrapyrrole chromophores requires members of ferredoxin-dependent bilin reductases (FDBRs). It was shown
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