LRSAM1 was expressed at high level in Escherichia.coli as inclusion bodies.
LRSAM1 was purified from inclusion bodies through denaturation, renaturation and ammonium sulfate precipitation steps.
The E3 activity of LRSAM1 was pH-dependent in cooperation with UbcH5-type E2-enzymes.
LRSAM1-driven ubiquitination favored K6-, K27-, K29- and K48-linkages.