KDRLKZ-1

KDRLKZ-1 binds to the purified KLHDC2 kelch domain, with a K_d value of 0.36 µM, a 1:1 binding mode, and a half-life of 76 seconds^[1].
KDRLKZ-1 (15 min) can specifically displace the SelK peptide substrate from the purified KLHDC2 kelch domain, with an IC₅₀ of 0.21 µM, and shows no activity against VHL^[1].
KDRLKZ-1 (80 min) displaces the SelK peptide substrate from the purified KLHDC2 kelch domain in TR-FRET assays, with an IC₅₀ of 0.31 µM^[1].
Excessive KDRLKZ-1 competes with the natural USP1 peptide substrate for binding to the purified full-length KLHDC2-EloB-EloC complex, thereby inhibiting the ubiquitination modification of USP1^[1].
KDRLKZ-1 induces the dissociation of purified full-length KLHDC2-EloB-EloC tetramers into smaller oligomers^[1].
Excessive KDRLKZ-1 competitively inhibits the interaction between endogenous KLHDC2 and biotin-conjugated KLHDC2 ligand in HEK293 cell extracts^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only. Further protocols information, click here.