mKate2.5 is a monomeric fluorescent protein published in 2012, derived from Entacmaea quadricolor. It was an intermediate protein in the evolution of FusionRed from mKate2, and has significantly reduced maturation rate, fluorescence brightness and pH stability relative to mKate2.
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mKate2.5 was derived from mKate2 with the following mutations: A46V/T74P/S129A/R158A/A159C/K176E/Y195N/K208N/C223_R232delinsSTGGAGDGGKA45V/T73P/S128A/R157A/A158C/K175E/Y194N/K207N/C222_R231delinsSTGGAGDGGK
amino acid numbers relative to mKate2eqFP578. show relative to eqFP578show relative to mKate2
mKate2.5 is characterized by monomeric behavior at 10 mg ml−1 concentrations on HPLC... Maturation rate, fluorescence brightness and pH stability of mKate2.5 were significantly reduced compared with mKate2 (data not shown).