UBE2L3 [UbcH7] (human) (rec.) (untagged)

South Bay Bio

UBE2L3 [UbcH7] (human) (rec.) (untagged)

10

Research Use Only

>95%

Liquid

Ubiquitin-conjugating enzyme E2 L3

Protein. Human UBE2L3 (aa 1-154)is untagged. Source: E. coli. Formulation: Liquid. In 50mM HEPES pH 7.5, 150mM sodium chloride, 10% glycerol, 2mM TCEP. Purity: >95% (SDS-PAGE). UBE2L3 (UbcH7) is an E2 ubiquitin conjugating enzyme and accepts ubiquitin from an E1 activating enzyme via an active site cysteine. The mechanism of ubiquitin transfer involves the breaking of a E1-Ub thioester linkage, followed by a reformation of a UBE2L3-Ub thioester. UBE2L3 transfers active ubiquitin molecules via a final transthiolation reaction to a cysteine residue of HECT class or RBR class E3 ligases. UBE2L3 plays a critical role in the activation of NF-kappab signaling by working in conjugation with the RBR E3 ligase, LUBAC (linear ubiquitin assembly complex), to ubiquitinate NEMO of the IkappaB complex, which than facilitates the downstream immune response. - UBE2L3 (UbcH7) is an E2 ubiquitin conjugating enzyme and accepts ubiquitin from an E1 activating enzyme via an active site cysteine. The mechanism of ubiquitin transfer involves the breaking of a E1-Ub thioester linkage, followed by a reformation of a UBE2L3-Ub thioester. UBE2L3 transfers active ubiquitin molecules via a final transthiolation reaction to a cysteine residue of HECT class or RBR class E3 ligases. UBE2L3 plays a critical role in the activation of NF-kappab signaling by working in conjugation with the RBR E3 ligase, LUBAC (linear ubiquitin assembly complex), to ubiquitinate NEMO of the IkappaB complex, which than facilitates the downstream immune response.

-80°C

12352202