IndraLab

Statements

KCNF1 binds GST. 4 / 4
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"An in vitro binding assay revealed that PCBP2 KH1 specifically interacted with the GST and L1 regions of EPRS (amino acids 1–196) but not with the GST-like domain alone (amino acids 1–168) ( xref and Supplementary Fig. 6a,b ), which further supported the finding that EPRS L1 was essential for interaction with PCBP2."
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"The anti-KCNF1 staining was specific as incubation of the antibody with recombinant GST-KCNF1, but not GST, completely removed the IF signals (Fig. xref )."
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"In in vitro translation assays, both GST-KH1 and GST-KH2 fusion proteins exhibited significant p53/p21 translational induction efficiency similar to or higher than that of the full-length hnRNP E1 protein ( xref , J and K ), demonstrating the independent and contextual functional capability of KH1 and KH2 domains."
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"Both GST-KH1 and GST-KH2 fusion proteins showed strong interactions with the 3′-UTRs of p53 and p21, whereas the GST-KH3 fusion protein showed a weak, tentative interaction with the p21 3′-UTR under the specified experimental settings ( xref , H and I )."
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