UBE2L3, human recombinant

Catalog number: SBB-CE0020, 100 μg

UBE2L3. E2 enzyme with specificity towards E3 ligases containing HECT (Homologous to the E6AP Carboxy-terminus) or RBR (Ring in-between ring) domains. This protein is recombinantly expressed in E.coli.[1][2]

In stock
SKU
0020
$179.00

Description

UBE2L3 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 N-kb signaling by working in conjugation with the RBR E3 ligase, LUBAC (linear ubiquitin assembly complex), to ubiquitinate NEMO of the IkB complex, which than facilitates the downstream immune response.

For Research Use Only, Not For Use In Humans.

Specifications

Product Overview
Quantity: 100 μg
Molecular Weight: 18 kDa
Purity: >95% by SDS-PAGE
Substrate Properties: Working concentrations of this enzyme range from 1 to 5µM.
Storage Buffer: 50 mM HEPES pH 7.5, 150mM NaCl, 10% glycerol, 2mM TCEP

Figures & Data

UBE2L3, human recombinant

Figure 1. UBE2L3, SDS-PAGE From left to right, increasing amounts of UBE2L3 loaded onto a 4-20% SDS-PAGE gel, stained with coomassie blue.

E2 Thioester Assay

Figure 2. Thioester Activity Assay. UBE2L3 forms a thioester with UB in an ATP dependent manner, and the bond can be reduced with addition of access DTT. The UBE2L3 is active.

Citations & References

1) Geisler, Sven, et al. "The ubiquitin-conjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy." J Cell Sci 127.15 (2014): 3280-3293.

2) Ardley, Helen Clare, et al. "Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1–4, including UBE2L3 which encodes UbcH7." Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression 1491.1 (2000): 57-64.