Ubiquitin-conjugating enzyme E2L6 (UBE2L6), also known as UbcH8, is a member of the E2 ubiquitin-conjugating enzyme family. The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination of a protein substrate requires the concerted action of 3 classes of enzymes: E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin protein ligases. The E2 ubiquitin-conjugating enzyme is highly similar in primary structure to the enzyme encoded by UBE2L3 gene. Recombinant human UBE2L6 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.