IndraLab

Statements

USP13 binds GST. 8 / 8
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"To detect the direct interaction between USP13 and cyclin D1, we performed GST-pulldown assays with the recombinant GST-USP13 protein."
37311811
sparser
"Moreover, we found that GST-USP13 mainly interacted with the full length (FL) and the 169–202 amino acid fragment (Twist1 WR domain) of GFP-Twist1 rather than with other Twist1 fragments (Fig.  xref )."
36732432
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"Meanwhile, the results from the pull-down assay showed that purified GST-USP13 directly interacted with endogenous Raf1 in 46C ESC lysates ( xref E )."
34688658
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"The recombinant GST or GST-USP13 full-length was expressed from E. coli BL21 and immobilized on glutathione-Sepharose beads."
36612196
sparser
"In vitro kinase assays were performed directly on the GST or GST-USP13 beads with active CK2 enzyme and ATP."
36612196
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"Western blotting with an anti-pT122 antibody showed that CK2 phosphorylated GST-USP13 protein but not GST, indicating that USP13 is a substrate of CK2 in vitro ( xref D), suggesting that USP13 is a substrate for CK2."
36612196
sparser
"The results showed that cyclin D1 can be pulled down by purified GST-USP13 protein (Fig. xref )."
37311811
sparser
"Using GST-pulldown assays, we found that Flag-Twist1 co-precipitated with GST-USP13, but not with GST (Fig.  xref )."
36732432