NIC Wiki

Table of Fluorescent Proteins

This page is no longer being maintained. The interactive graph of fluorescent protein properties and interactive graph of photoswitchable fluorescent protein properties pages should be viewed instead.

Blue/UV Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
TagBFP	402	457	52000	0.63	32.8	Monomer	2.7	Evrogen	aka mTagBFP; from [27]
mTagBFP2	399	454	50600	0.64	32.4	Monomer	2.7	[48]
Azurite	383	450	26200	0.55	14.4	Monomer	5.0	[28]
EBFP2	383	448	32000	0.56	18	Monomer	5.3	[29]
mKalama1	385	456	36000	0.45	16	Monomer	5.5	[29]
Sirius	355	424	15000	0.24	3.6	Monomer	<3.0	[37]
Sapphire	399	511	29000	0.64	18.6	Monomer		[8]	aka H9-40
T-Sapphire	399	511	44000	0.6	26.4	Monomer		[12]	faster folding than Sapphire

Cyan Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
ECFP	433	475	32500	0.4	13.0	Monomer	4.7
Cerulean	433	475	43000	0.62	26.7	Monomer	4.7	[13]	improved ECFP
SCFP3A	433	474	30000	0.56	16.8	Monomer	<4.5	[39]	improved Cerulean
mTurquoise	434	474	30000	0.84	25.2	Monomer		[36]	improved SCFP3A
mTurquoise2	434	474	30000	0.93	27.9	Monomer	3.1	[47]
monomeric Midoriishi-Cyan	470	496	22150	0.7	15.5	Monomer	7.0	MBL International	from [14]
TagCFP	458	480	37000	0.57	21.0	Monomer	4.7	Evrogen
mTFP1	462	492	64000	0.85	54.0	Monomer	4.3	Allele Biotech	from [24]

Green Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
EGFP	488	507	56000	0.6	33.6	Monomer
Emerald	487	509	57500	0.68	37.3	Monomer		[8]	EGFP derivative; 5-fold brighter at 37° C
Superfolder GFP	485	510	83300	0.65	54.1	Monomer		[38]	Fast folding, highly stable
Monomeric Azami Green	492	505	55000	0.74	40.7	Monomer	5.8	MBL International	from [11]
TagGFP2	483	506	56500	0.6	33.9	Monomer	4.7	Evrogen
mUKG	483	499	60000	0.72	43.2	Monomer	5.2	[26]
mWasabi	493	509	70000	0.80	56.0	Monomer	6.0	Allele Biotech
Clover	505	515	111000	0.76	84.4	Monomer	6.1	[46]
mNeonGreen	506	517	116000	0.80	92.8	Monomer	5.7	[49]	Allele Biotech

Yellow Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
EYFP	513	527	83400	0.61	50.9	Monomer
Citrine	516	529	77000	0.76	58.5	Monomer	5.7	[2]	EYFP derivative; Less Cl, pH sensitive
Venus	515	528	92200	0.57	52.5	Monomer	6.0	[9]	EYFP derivative; 30-fold brighter at 37° C
SYFP2	515	527	101000	0.68	68.7	Monomer	6.0	[39]	improved Venus
TagYFP	508	524	64000	0.62	39.7	Monomer	5.5	Evrogen

Orange Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
Monomeric Kusabira-Orange	548	559	51600	0.6	31.0	Monomer	5.0	MBL International	from [14]
mKOκ	551	563	105000	0.61	64.0	Monomer	4.2	[26]	faster maturing than mKO
mKO2	551	565	63800	0.62	39.6	Monomer	5.5	MBL International	fast maturing
mOrange	548	562	71000	0.69	49.0	Monomer	6.5	[16]	~2.5 hr maturation time
mOrange2	549	565	58000	0.60	34.8	Monomer	6.5	[33]	~25x more photostable than mOrange

Red Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
mRaspberry	598	625	86000	0.15	12.9	Monomer		[15]	~55 min maturation time
mCherry	587	610	72000	0.22	15.8	Monomer	<4.5	[16]	~15 min maturation time
mStrawberry	574	596	90000	0.29	26.1	Monomer	<4.5	[16]	~50 min maturation time
mTangerine	568	585	38000	0.3	11.4	Monomer	5.7	[16]
tdTomato	554	581	138000	0.69	95.2	Monomer	4.7	[16]	~1 hr maturation time
TagRFP	555	584	100000	0.48	49.0	Monomer	3.8	Evrogen	From [20]
TagRFP-T	555	584	81000	0.41	33.2	Monomer	4.6	[33]	~10x more photostable than TagRFP
mApple	568	592	75000	0.49	36.7	Monomer	6.5	[33]
mRuby	558	605	112000	0.35	39.2	Monomer	4.4	[35]
mRuby2	559	600	113000	0.38	43	Monomer	5.3	[46]

Far-Red Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
mPlum	590	649		0.1		Monomer		[15]	~100 min maturation time
HcRed-Tandem	590	637	160000	0.04	6.4	Monomer			Tandem dimer; functional monomer
mKate2	588	633	62500	0.40	25	Monomer	5.4	Evrogen
mNeptune	600	650	67000	0.20	13.4	Monomer	5.4	[34]
NirFP	605	670	15700	0.06	0.9	Dimer	4.5	Evrogen

Near-IR Proteins

TagRFP657	611	657	34000	0.10	3.4	Monomer	5.0	[30]
IFP1.4	684	708	102000	0.077	7.8	Monomer	4.6	[31]	Bacterial phytochrome; requires biliverdin cofactor for fluorescence
iRFP	690	713	105000	0.059	6.2	Dimer	4.0	[43]	Bacterial phytochrome; requires biliverdin cofactor for fluorescence

Long Stokes Shift Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
mKeima Red	440	620	14400	0.24	3.5	Monomer	6.5	MBL International	From [22]
LSS-mKate1	463	624	31200	0.08	2.5	Monomer	3.2	[32]
LSS-mKate2	460	605	26000	0.17	4.4	Monomer	2.7	[32]
mBeRFP	446	611	65000	0.27	17.6	Monomer	5.6	[50]

Photoactivatible Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source
PA-GFP	504	517	17400	0.79	13.7	Monomer		[10]
PAmCherry1	564	595	18000	0.46	8.3	Monomer	6.3	[41]
PATagRFP	562	595	66000	0.38	25.1	Monomer	5.3	[40]

Photoconvertible Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
Kaede (green)	508	518	98800	0.88	86.9	Tetramer	5.6	MBL International
Kaede (red)	572	580	60400	0.33	19.9	Tetramer	5.6	MBL International	after photoconversion
KikGR1 (green)	507	517	53700	0.7	37.6	Tetramer	7.8	MBL International	from [23]
KikGR1 (red)	583	593	35100	0.65	22.8	Tetramer	5.5	MBL International	after photoconversion; from [23]
PS-CFP2	400	468	43000	0.2	8.6	Monomer		Evrogen	Before photoconversion
PS-CFP2	490	511	47000	0.23	10.8	Monomer		Evrogen	After photoconversion
mEos2 (green)	506	519	56000	0.84	47.0	Monomer	5.6	[42]
mEos2 (red)	573	584	46000	0.66	30.4	Monomer	6.4	[42]	After photoconversion
mEos3.2 (green)	507	516	63400	0.70	53	Monomer	5.4	[45]	Better folding, more monomeric than mEos2
mEos3.2 (red)	572	580	32200	0.55	18	Monomer	5.8	[45]	After photoconversion
PSmOrange	548	565	113300	0.51	57.8	Monomer	6.2	[44]	Before photoconversion
PSmOrange	634	662	32700	0.28	9.2	Monomer	5.6	[44]	After photoconversion

Photoswitchable Proteins

Protein	λ_ex	λ_em	Extinction coeff.	QY	Brightness	Aggregation	pKa	Source	Notes
Dronpa	503	518	95000	0.85	80.7	Monomer		MBL International	From [19]; Photoactivated form

Notes:

This is not a complete list of existing fluorescent proteins. In general I have included only those proteins that are commercially available or that are well characterized and represent a clear improvement over existing proteins. All values were taken from the manufacturers data or the indicated papers. I cannot vouch for their reliability. Brightness is the product of extinction coefficient and quantum yield, divided by 1000.

References:

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3. Campbell, R.E., et al., A monomeric red fluorescent protein. Proc Natl Acad Sci U S A, 2002. 99(12): p. 7877-82.

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21. Shcherbo, D. et al., Bright far-red fluorescent protein for whole-body imaging. Nat. Methods 2007. 4(9): p. 741-746.

22. Kogure, T. et al., A fluorescent variant of a protein from the stony coral Montipora facilitates dual-color single-laser fluorescence cross-correlation spectroscopy. Nat. Biotechnol. 2006. 24(5): p. 557-581.

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37. Tomosugi W. et al., An ultramarine fluorescent protein with increased photostability and pH insensitivity. Nat. Meth. 2009, 5: p. 351-353.

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40. Subach, FV. et al., Bright Monomeric Photoactivatable Red Fluorescent Protein for Two-Color Super-Resolution sptPALM of Live Cells. JACS 2010, 132: p. 6481 - 6491.

41. Subach, FV. et al., Photoactivatable mCherry for high-resolution two-color fluorescence microscopy. Nat. Meth. 2009, 6: p. 153-159.

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44. Subach, OM. et al., A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. Nat. Meth. 2011, 8: p. 771-777.

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