UBE2D1, human recombinant

Catalog number: SBB-CE0021, 100 μg

UBE2D1 is an E2 conjugating enzyme which catalyzes the E3 mediated ubiquitination of a target substrate. It is known to interact with Parkin, and is involved in PINK1 mediated mitophagy. This protein is recombinantly expressed in E.coli. [1][2]

In stock
SKU
0021
$179.00

Description

UBE2D1 is an E2 ubiquitin conjugating enzyme. An E1 activating enzyme is required to attach ubiquitin to UBE2D1 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 UBE2D1-Ub thioester. UBE2D1 is capable of associating with numerous known E3 ligases which target abnormal proteins for proteasomal degradation through polyubiquitination. UBE2D1 is also known to interact with Parkin, and to be involved in PINK1 mediated mitophagy. This UBE2D1 is recombinantly expressed in E.coli. The purity of this enzyme is > 95% - determined by SDS-PAGE.

For Research Use Only, Not For Use In Humans.

Specifications

Product Overview
Quantity: 100 μg
Molecular Weight: 17 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
Storage Store at -80C. Avoid multiple freeze / thaws.

Figures & Data

UBE2D1, human recombinant

Figure 1. UBE2D1, SDS-PAGE From left to right, increasing amounts of UBE2D1loaded onto a 4-20% SDS-PAGE gel, stained with Coomassie Brilliant Blue. UBE2D1 is > 95% pure.

E2 Thioester Activity

Figure 2. Thioester Activity Assay. UBE2D1 forms a thioester with UB in an ATP dependent manner, and the bond can be reduced with addition of access DTT. The UBE2D1 is active.

Citations & References

1) Van Wijk, Sjoerd JL, and HT Marc Timmers. “The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins.” The FASEB Journal 24.4 (2010): 981-993.

2) Buetow, Lori, and Danny T. Huang. “Structural in sights into the catalysis and regulation of E3 ubiquitin ligases.” Nature Reviews Molecular Cell Biology (2016).