Fluorescent Proteins

Protein ex em Extinction Coeff QY Brightness Aggregation pKa Source Notes
Green Proteins
EGFP 488 507 56000 0.6 33.6 Monomer   Clontech  
Emerald 487 509 57500 0.68 37.3 Monomer   [8] EGFP derivative; 5-fold brighter at 37° C
CoralHue® Azami Green 492 505 72300 0.67 48.4 Tetramer <5.0 MBL International from [11]
CoralHue® Monomeric Azami Green 492 505 55000 0.74 40.7 Monomer 5.8 MBL International from [11]
CopGFP 482 502 70000 0.6 42.0 Monomer   Evrogen Faster folding, less pH sensitive than EGFP
AceGFP 480 505 50000 0.55 27.5 Monomer   Evrogen  
ZsGreen1 493 505 35600 0.63 22.4 Tetramer   Clontech from [1]
TagGFP 482 505 58200 0.59 34.3 Monomer 4.7 Evrogen  
TurboGFP 482 502 70000 0.53 37.1 Dimer 5.2 Evrogen  
mUKG 483 499 60000 0.72 43.2 Monomer 5.2 Evrogen from [26]

 

Blue/UV Proteins
EBFP 380 440 29000 0.31 9.0 Monomer   Clontech  
TagBFP 402 457 52000 0.63 32.8 Monomer 2.7 Evrogen aka mTagBFP; from [27]
Azurite 383 450 26200 0.55 14.4 Monomer 5.0 [28] Highly photostable compared to EBFP
EBFP2 383 448 32000 0.56 18 Monomer 5.3 [29] Highly photostable compared to EBFP
mKalama1 385 456 36000 0.45 16 Monomer 5.5 [29]  
GFPuv 395 509 30000 0.79 23.7 Monomer   Clontech  
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
ECFP 433 475 32500 0.4 13.0 Monomer 4.7 Clontech  
Cerulean 433 475 43000 0.62 26.7 Monomer 4.7   improved ECFP from [13]
AmCyan1 458 489 40000 0.24 9.6 Tetramer   Clontech more photostable than ECFP; from [1]
CoralHue® Midoriishi-Cyan 472 495 27250 0.9 24.5 Dimer 6.6 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]

 

Yellow Proteins
EYFP 513 527 83400 0.61 50.9 Monomer   Clontech  
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
PhiYFP 525 537 130000 0.4 52.0 Monomer 6.0 Evrogen  
TagYFP 508 524 64000 0.62 39.7 Monomer 5.5 Evrogen  
TurboYFP 525 538 105000 0.53 55.7 Dimer   Evrogen Fast maturing PhiYFP variant
ZsYellow1 529 539 20200 0.42 8.5 Tetramer   Clontech from [1]

 

Orange Proteins
CoralHue® Kusabira-Orange 548 561 73700 0.45 33.2 Dimer <5.0 MBL International from [14]
CoralHue® 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 faster maturing than mKO; from [26]
mOrange 548 562 71000 0.69 49.0 Monomer <6.5 [16] ~2.5 hr maturation time

 

Red Proteins
tdimer2(12) 552 579 120000 0.68 81.6 Monomer 4.8 [3] Tandem dimer; functional monomer
mRFP1 584 607 44000 0.25 11.0 Monomer 4.5 [3]  
DsRed-Express 557 579 31000 0.42 13.0 Tetramer   Clontech DsRed.T1 from [4]
DsRed2 563 582 43800 0.55 24.1 Tetramer   Clontech  
DsRed-Monomer 556 586       Monomer   Clontech  
HcRed1 588 618       Dimer   Clontech HcRed-2A from [5]
AsRed2 576 592 56200 0.05 2.8 Tetramer   Clontech asFP595 from [6]?
eqFP611 559 611 78000 0.45 35.1 Tetramer <4.0 [7] Tetramers dissociate at low concentration
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]
JRed 584 610 44000 0.2 8.8 Monomer? 5.0 Evrogen  
TurboFP602 574 602 74000 0.35 26 Dimer 4.7 Evrogen  

 

Far Red Proteins
mPlum 590 649   0.1   Monomer   [15] ~100 min maturation time
TurboFP635 588 635 65000 0.34 22.1 Dimer 5.5 Evrogen aka Katushka; From [21]
TagFP635 588 635 45000 0.33 14.9 Monomer 6.0 Evrogen aka mKate; From [21]
AQ143 595 655 90000 0.04 3.6 Tetramer   from [25]
HcRed-Tandem 590 637 160000 0.04 6.4 Monomer   Evrogen Tandem dimer; functional monomer

 

Large Stokes Shift Proteins

CoralHue® mKeima Red 440 620 14400 0.24 3.5 Monomer 6.5 MBL International From [22]
CoralHue® dKeima Red 440 616 24600 0.31 7.6 Dimer 6.5 MBL International From [22]
CoralHue® dKeima570 440 570 14400 0.15 2.2 Dimer 6.5 MBL International From [22]

 

Photoconvertible Proteins
CoralHue® Kaede (green) 508 518 98800 0.88 86.9 Tetramer 5.6 MBL International Green to red photoconversion, green state
CoralHue® Kaede (red) 572 580 60400 0.33 19.9 Tetramer 5.6 MBL International Same protein as above, after photoconversion
CoralHue® KikGR1 (green) 507 517 53700 0.7 37.6 Tetramer 7.8 MBL International Green to red photoconversion, green state; from [23]
CoralHue® KikGR1 (red) 583 593 35100 0.65 22.8 Tetramer 5.5 MBL International Same protein as above, after photoconversion; from [23]
KFP-Red 580 600 59000 0.07 4.1 Tetramer   Evrogen This data is for photoactivated state
PA-GFP 504 517 17400 0.79 13.7 Monomer   [10] This data is for photoactivated state
PS-CFP 402 468 34000 0.16 5.44 Monomer 4.0 [17] Before photoconversion
PS-CFP 490 511 27000 0.19 5.13 Monomer 6.0 [17] After photoconversion
mEosFP 505 516 67200 0.64 43.0 Monomer 5.5 [18] Before photoconversion
mEosFP 569 581 37000 0.62 22.9 Monomer   [18] After photoconversion
CoralHue® 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:

  1. Matz, M.V., et al., Fluorescent proteins from nonbioluminescent Anthozoa species. Nat Biotechnol, 1999. 17: p. 969-973.
  2. Griesbeck, O., et al., Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications. J Biol Chem, 2001. 276(31): p. 29188-94.
  3. Campbell, R.E., et al., A monomeric red fluorescent protein. Proc Natl Acad Sci U S A, 2002. 99(12): p. 7877-82.
  4. Bevis, B.J. and B.S. Glick, Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nat Biotechnol, 2002. 20(1): p. 83-7.
  5. Gurskaya, N.G., et al., GFP-like chromoproteins as a source of far-red fluorescent proteins. FEBS Lett, 2001. 507(1): p. 16-20.
  6. Lukyanov, K.A., et al., Natural animal coloration can be determined by a nonfluorescent green fluorescent protein homolog. J Biol Chem, 2000. 275(34): p. 25879-82.
  7. Wiedenmann, J., et al., A far-red fluorescent protein with fast maturation and reduced oligomerization tendency from Entacmaea quadricolor (Anthozoa, Actinaria). Proc Natl Acad Sci U S A, 2002. 99(18): p. 11646-51.
  8. Cubitt, A.B., L.A. Woollenweber, and R. Heim, Understanding structure-function relationships in the Aequorea victoria green fluorescent protein. Meth Cell Biol, 1999. 58: p. 19-30.
  9. Nagai, T., et al., A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol, 2002. 20(1): p. 87-90.
  10. Patterson, G.H. and J. Lippincott-Schwartz, A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells. Science, 2002. 297(5588): p. 1873-7.
  11. Karasawa, S. et al., A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling. J Biol Chem, 2003.
    12. 278(36):p. 34167-71.
  12. Zapata-Hommer O. and Griesbeck O., Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP. BMC Biotechnol, 2003. 3(5).
  13. Rizzo, M.A., et al., An improved cyan fluorescent protein variant useful for FRET. Nat Biotechnol, 2004. 22(4):p. 445-449.
  14. Karasawa, S., et al., Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer. Biochem J, 2004. 381:p. 307-312
  15. Wang, L. et al., Evolution of new nonantibody proteins via iterative somatic hypermutation. Proc Natl Acad Sci, 2004. 101(48):p. 16745-16749.
  16. Shaner, N.C. et al., Improved monomeric red, orange, and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol, 2004.
  17. Chudakov, D.M. et al., Photoswitchable cyan fluorescent protein for protein tracking. Nat Biotechnol 2004. 22(11):p. 1435-1439.
  18. Wiedenmann, J. et al., EosFP, a fluorescent marker protein with UV-inducible green-to-red fluorescence conversion. Proc Natl Acad Sci 2004. 101(45): p.15905-15910
  19. Ando, R. et al., Regulated fast nucelocytoplasmic shuttling observed by reversible protein highlighting. Science 2004. 306: p. 1370-1373.
  20. Merzlyak, E.M. et al., Bright monomeric red fluorescent protein with an extended fluorescence lifetime. Nat. Methods 2007.4(7): p. 555-557.
  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.
  23. Tsutsui, H. et al. Semi-rational engineering of a coral fluorescent protein into an efficient highlighter. EMBO Rep. 2005. 6(3): p. 233-238.
  24. Ai HW, et al., Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging. Biochem J. 2006. 400(3): p. 531-540.
  25. Shkrob MA, et al., Far-red fluorescent proteins evolved from a blue chromoprotein from Actinia equina. Biochem J. 2005. 392(Pt 3): p. 649-654.
  26. Tsutsui H, et al., Improving membrane voltage measurements using FRET with new fluorescent proteins. Nat. Methods 2008. 5(8): p. 683-685.
  27. Subach OM et al., Conversion of Red Fluorescent Protein into a Bright Blue Probe. Chemistry & Biology. 2008. 15(10): p. 1116-1124.
  28. Mena, MA et al., Blue fluorescent proteins with enhanced brightness and photostability from a structurally targeted library. Nat Biotech. 2008. 24(12):p. 1569-1571.
  29. Ai, H, et al., Exploration of new chromophore structures leads to the identification of improved blue fluorescent proteins. Biochemistry 2007, 46: p. 5904-5910.

 
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