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Dendra2

Dendra2 is a photoconvertible green fluorescent protein published in 2006, derived from Dendronephthya sp.. It has high acid sensitivity.
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Oligomerization Organism Molecular Weight Cofactor
Monomer Dendronephthya sp. 26.1 kDa -

FPbase ID: GE6KO

Attributes

State Ex λ Em λ EC (M-1 cm-1) QY Brightness pKa Maturation (min) Lifetime (ns)
Green 490 507 45,000 0.5 22.5 6.6   3.3
Red 553 573 35,000 0.55 19.25 6.9   4.4
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Transitions

From To Switch λ
Green Red 405
Green Red 480
Edit state transitions

Photostability

State t1/2 (s) Power Light Mode In Cell Fusion ˚C Reference
Green 30.0 4.4 (mW/cm2) Arc-lamp Widefield Kaberniuk et al. (2017)
Red 1050.0 4.4 (mw/cm2) Arc-lamp Widefield Kaberniuk et al. (2017)
A caution on interpretation of photostability measurements
Add photostability info

Dendra2 Sequence

BLAST

Dendra2 was derived from Dendra with the following mutations: M1_N2insNTPGI/A224V

MNTPGINLIKEDMRVKVHMEGNVNGHAFVIEGEGKGKPYEGTQTANLTVKEGAPLPFSYDILTTAVHYGNRVFTKYPEDIPDYFKQSFPEGYSWERTMTFEDKGICTIRSDISLEGDCFFQNVRFKGTNFPPNGPVMQKKTLKWEPSTEKLHVRDGLLVGNINMALLLEGGGHYLCDFKTTYKAKKVVQLPDAHFVDHRIEILGNDSDYNKVKLYEHAVARYSPLPSQVW

Structure

Deposited: ,
Chromophore:

Excerpts

PS-CFP2 can be effectively photoactivated by UV-laser line only. Dendra2, on the other hand, can be photoactivated using either violet or blue light, through either arc lamp or laser light irradiation.

Chudakov et al. (2007)

PS-CFP2 can be used in combination with red or far-red fluorescent protein for dual color labeling. Dendra2 cannot be combined with green or red fluorescent proteins, since it occupies both green and red channels. It cannot be combined with blue fluorescent proteins either, since they require violet light excitation, which causes photoactivation of Dendra2.

Chudakov et al. (2007)

Primary Reference

Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light

Gurskaya Ng, Verkhusha Vv, Shcheglov As, Staroverov Db, Chepurnykh Tv, Fradkov Af, Lukyanov S, Lukyanov Ka

(2006). Nature Biotechnology, 24(4) , 461-465. doi: 10.1038/nbt1191. Article   Pubmed

Additional References

  1. The Photoconvertible Fluorescent Protein Dendra2 Tag as a Tool to Investigate Intracellular Protein Dynamics

    Lešková A, Kusá Z, Labajová M, Krausko M, Jásik J

    (2019). Methods in Molecular Biology, 1992, 201-214. doi: 10.1007/978-1-4939-9469-4_13. Article   Pubmed

  2. moxDendra2: an inert photoswitchable protein for oxidizing environments

    Kaberniuk Aa, Morano Nc, Verkhusha Vv, Snapp El

    (2017). Chemical Communications, 53(13) , 2106-2109. doi: 10.1039/c6cc09997a. Article   Pubmed

  3. Single-molecule evaluation of fluorescent protein photoactivation efficiency using an in vivo nanotemplate

    Durisic N, Laparra-Cuervo L, Sandoval-Álvarez , Borbely Js, Lakadamyali M

    (2014). Nature Methods, 11(2) , 156-162. doi: 10.1038/nmeth.2784. Article   Pubmed

  4. Revealing the Excited-State Dynamics of the Fluorescent Protein Dendra2

    Fron E, Van Der Auweraer M, Moeyaert B, Michiels J, Mizuno H, Hofkens J, Adam V

    (2013). The Journal of Physical Chemistry B, 117(8) , 2300-2313. doi: 10.1021/jp309219m. Article   Pubmed

  5. Rational Design of Photoconvertible and Biphotochromic Fluorescent Proteins for Advanced Microscopy Applications

    Adam V, Moeyaert B, David Cc, Mizuno H, Lelimousin M, Dedecker P, Ando R, Miyawaki A, Michiels J, Engelborghs Y, Hofkens J

    (2011). Chemistry & Biology, 18(10) , 1241-1251. doi: 10.1016/j.chembiol.2011.08.007. Article   Pubmed

  6. Tracking intracellular protein movements using photoswitchable fluorescent proteins PS-CFP2 and Dendra2

    Chudakov Dm, Lukyanov S, Lukyanov Ka

    (2007). Nature Protocols, 2(8) , 2024-2032. doi: 10.1038/nprot.2007.291. Article   Pubmed

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