Enhanced green fluorescence protein EGFP-mCherry Recombinant Protein

Recombinant Human Enhanced green fluorescence protein EGFP-mCherry

Cat. Num. AAA283703

• Applications: Western Blot, ELISA
• Purity: >95 % as determined by SDS-PAGE; Affinity purification
• Synonyms: Enhanced green fluorescence protein EGFP-mCherry; Recombinant Human Enhanced green fluorescence protein EGFP-mCherry; microtubule-associated protein 1 light chain 3 beta; Enhanced green fluorescence protein EGFP-mCherry recombinant protein

• Host: E Coli
• Purity/Purification: >95 % as determined by SDS-PAGE; Affinity purification
• Form/Format: Lyophilized Powder

• Applicable Applications for Enhanced green fluorescence protein EGFP-mCherry recombinant protein: Western Blot (WB), ELISA (EIA)
• Application Notes: Western blotting, ELISA, Albumin-bound fluorescence was used in serum of patients with chronic renal failure.
• Species of Origin: Human
• Tag: His
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Storage Buffer: Lyophilized from sterile 20mM PB, 240mM NaCl, PH6.0.
• Preparation and Storage: Store it under sterile conditions at -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.Samples are stable for up to twelve months from date of receipt at -81 degree C.

Related Product Information for Enhanced green fluorescence protein EGFP-mCherry recombinant protein

Fluorescence resonance energy transfer (FRET) between fluorescent proteins (FPs) is a powerful tool to investigate protein-protein interaction and even protein modifications in living cells. Here, we analyze the E(0)GFP-mCherry pair and show that it can yield a reproducible quantitative determination of the energy transfer efficiency both in vivo and in vitro. The photophysics of the two proteins is reported and shows good spectral overlap (Förster radius R(0) = 51 A), low crosstalk between acceptor and donor channels, and independence of the emission spectra from pH and halide ion concentration. Acceptor photobleaching (APB) and one- and two-photon fluorescence lifetime imaging microscopy (FLIM) are used to quantitatively determine FRET efficiency values. A FRET standard is introduced based on a tandem construct comprising donor and acceptor together with a 20 amino acid long cleavable peptidic linker. Reference values are obtained via enzymatic cleavage of the linker and are used as benchmarks for APB and FLIM data. E(0)GFP-mCherry shows ideal properties for FLIM detection of FRET and yields high accuracy both in vitro and in vivo. Furthermore, the recently introduced phasor approach to FLIM is shown to yield straightforward and accurate two-photon FRET efficiency data even in suboptimal experimental conditions. The consistence of these results with the reference method (both in vitro and in vivo) reveals that this new pair can be used for very effective quantitative FRET imaging