52412
R-Phycoerythrin
BioReagent, passes test for gel electrophoresis
Synonym(s):
R-PE, phycobiliprotein
product line
BioReagent
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
Quality Level
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
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves
Regulatory Information
动植物源性产品
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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
Avinash Kolli et al.
The Journal of chemical physics, 137(17), 174109-174109 (2012-11-14)
The influence of fast vibrations on energy transfer and conversion in natural molecular aggregates is an issue of central interest. This article shows the important role of high-energy quantized vibrations and their non-equilibrium dynamics for energy transfer in photosynthetic systems
Hoda Hossein-Nejad et al.
The Journal of chemical physics, 136(2), 024112-024112 (2012-01-21)
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
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