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moxEos3.2

moxEos3.2 is a fluorescent protein published in 2017, derived from Lobophyllia hemprichii. It is reported to be a monomer.

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Oligomerization Organism Molecular Weight Cofactor
Monomer Lobophyllia hemprichii 25.7 kDa -

Attributes

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Photostability

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moxEos3.2 Sequence

moxEos3.2 was derived from mEos3.2 with the following mutations: M1_S2insV/C101A/C171A/C195A

MVSAIKPDMKIKLRMEGNVNGHHFVIDGDGTGKPFEGKQSMDLEVKEGGPLPFAFDILTTAFHYGNRVFAKYPDNIQDYFKQSFPKGYSWERSLTFEDGGIANARNDITMEGDTFYNKVRFYGTNFPANGPVMQKKTLKWEPSTEKMYVRDGVLTGDIEMALLLEGNAHYRADFRTTYKAKEKGVKLPGAHFVDHAIEILSHDKDYNKVKLYEHAVAHSGLPDNARR

Excerpts

The new “mox” (monomeric oxidation protected) PSFP, moxEos3.2, was resistant to inappropriate disulphide bond formation when expressed in the ER, while the parent “wt” mEos3.2 formed a ladder of covalent oligomers, with noticeably very little protein in the monomeric state. We also confirmed that the alanine mutations did not alter the monomericity of mEos3.2 by performing a CytERM assay for FP oligomerization. Despite these successful outcomes, we noticed that moxEos3.2 was visually much dimmer in the green and red states in comparably transfected and expressing cells. Furthermore, this mox form bleached substantially faster than the wt parent in both the green and red states. Taken together, the optimization of mEos3.2 for the secretory pathway had impaired the performance of the protein.

Kaberniuk et al. (2017)

Primary Reference

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

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