IndraLab

Statements

BAP1 binds MBP. 7 / 7
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"The results illustrated the ability of TNPO1 to dissociate homodimeric MBP-BAP1 CTD to form a heterodimeric TNPO1:MBP-BAP1 CTD complex with a 1:1 binding stoichiometry."
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"Preincubation of MBP-BAP1 CTD with TNPO1 showed an increased apparent mol wt of 136.2 ± 8.1 kD for the main elution peak, which corresponded to a 1:1 binary complex ( xref )."
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"Recombinant importin-αs and TNPO1 were expressed in Escherichia coli and purified to homogeneity to investigate their interactions with the CTD of BAP1 (residues 596–729) fused with a maltose-binding protein (MBP) tag (hereafter MBP-BAP1 CTD ) by size-exclusion chromatography (SEC; xref )."
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"In the presence of two-fold excess karyopherins, MBP-BAP1 CTD formed stable complexes with individual karyopherins and coeluted at earlier elution volumes than did isolated proteins ( xref )."
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"The formation of the binary complexes was confirmed by SDS-PAGE, which showed distinct protein bands of the early elution peaks, corresponding to MBP-BAP1 CTD and individual karyopherins ( xref )."
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"MBP-BAP1 CTD by itself displayed protein concentration–dependent oligomerization with an apparent mol wt of 92.0–109.8 kD on increasing protein concentration ≤60 µM ( xref )."
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sparser
"As the theoretical mol wt of an MBP-BAP1 CTD monomer is 59 kD, the results suggested a dynamic monomer-dimer equilibrium for MBP-BAP1 CTD ."
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