UbcH7/UBE2L3 Protein, Human (sf9, His, StrepⅡ)

UbcH7/UBE2L3 is a unique ubiquitin-conjugating E2 enzyme that cooperates with HECT-type and RBR family E3 ligases and lacks intrinsic E3-independent reactivity with lysine. It uniquely works with RBR family E3 enzymes such as PRKN, RNF31 and ARIH1, acting like a RING-HECT hybrid. UbcH7/UBE2L3 Protein, Human (sf9, His, Strep) is the recombinant human-derived UbcH7/UBE2L3 protein, expressed by sf9 insect cells , with N-Strep, N-8*His labeled tag.

UbcH7/UBE2L3, a ubiquitin-conjugating enzyme E2, exhibits specificity in collaboration with HECT-type and RBR family E3 ubiquitin-protein ligases. Notably, its unique characteristic is the absence of intrinsic E3-independent reactivity with lysine, rendering it incompatible with most RING-containing E3 ubiquitin-protein ligases. However, it demonstrates activity with RBR family E3 enzymes such as PRKN, RNF31, and ARIH1, functioning akin to RING-HECT hybrids. Acting downstream of the E1 complex, UbcH7 catalyzes the covalent attachment of ubiquitin to target proteins and, in vitro, facilitates 'Lys-11'-linked polyubiquitination. Its involvement in the selective degradation of short-lived and aberrant proteins highlights its role in cellular quality control. Additionally, down-regulation during the S-phase suggests a contribution to cell cycle progression, while its impact on nuclear hormone receptors' transcriptional activity and potential role in myelopoiesis further underscore its multifaceted functions.

Human

Sf9 insect cells

N-StrepⅡ;N-8*His

P68036 (A2-D154)

7332

Partial

AASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVD

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.