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. Author manuscript; available in PMC: 2012 Feb 1.
Published in final edited form as: Nat Biotechnol. 2011 Jul 17;29(8):757–761. doi: 10.1038/nbt.1918

Table 1.

In vitro properties of iRFP in comparison with IFP1.4.

Protein Absorbance
maximum
(nm)		 Excitation
maximum
(nm)		 Emission
maximum
(nm)		 Extinction coefficient
(M−1cm−1) (based on
protein
concentration)		 Extinction coefficient
(M−1cm−1) (based on
extinction coefficient
of BV)		 Quantum
yield (%)		 Molecular
brightness
relative to
IFP1.4 (%)		 Photostability,
τ50% (s)		 pKa Maturation
at 37°C,
50% (h)		 Conformational
stability in GndCl,
[D]50% (M)
iRFP 692 690 713 85,000 105,000 5.9 120 450 4.0 2.8 2.9
IFP1.4 684 684
(684)		 707
(708)		 54,700 102,000
(92,000)		 7.7
(7.0)		 100 50 4.6 1.9 1.7

IFP1.4 characteristics from the original paper9 are shown in parentheses. Spectroscopic parameters were determined in PBS at pH 7.5.