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Transcription of c-KIT and both SCF splice variants was active in normoxic controls and cells subjected to hypoxia followed by a 24 hour recovery while maintained in medium with or without recombinant rat (rr) SCF (100 ng/ml) (figure 6C).
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In addition, the same variants were active against both Heliothis zea and S. exigua [ 20].
All of the labeled variants were active, inhibiting bovine trypsin with an SI of 1.1 similar to that of the wild-type.
Here, we demonstrate that the potentiated Hsp104 variants are active against a broad range of disease-linked TDP-43, FUS and α-syn mutants.
Taken together with the localization analyses these results suggest that the truncated Ilv2 versions as well as the Ilv5ΔN48 and the Ilv3ΔN19 variants are active enzymes even outside the mitochondrial matrix.
However, data for the LB03 H229andnd LB03 E73A mutants suggest that these enzyme variants are active and aqueous-soluble in the periplasm, albeit at slightly less abundance than the enzyme from their parent strain LB03.
Of these 24 variants only one (1 13) was active after heat-treatment.
As the results show, all three Flp variants tested are active on their respective genomic FRT-like sequences in mammalian cells (Figure 2B).
Thus, all CAM1 truncated variants that are active, most likely fold as a complete 8 barrels.
Under these less stringent conditions we found three additional variants that were active (1 2, 1 6 and 1 12).
To this end we have shown that all cysteine variants are enzymatically active.
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