Thioester Activity Assay: UBE2D1 (UbcH5a) forms a thioester with Ub in an ATP-dependent manner and the bond can be reduced with addition of access DTT. Confirms the activity of UBE2D1.
Thioester Activity Assay: UBE2D1 (UbcH5a) forms a thioester with Ub in an ATP-dependent manner and the bond can be reduced with addition of access DTT. Confirms the activity of UBE2D1.
UBE2D1 [UbcH5a] (human) (rec.) (untagged)
SBB-CE0021
Overview
- SupplierSouth Bay Bio
- Product NameUBE2D1 [UbcH5a] (human) (rec.) (untagged)
- Delivery Days Customer10
- CertificationResearch Use Only
- Estimated Purity>95%
- Protein IDP51668
- Protein NameUbiquitin-conjugating enzyme E2 D1
- Scientific DescriptionProtein. Human UBE2D1 (aa1-147)is untagged. Source: E. coli. Formulation: Liquid. In 50mM HEPES pH 7.5, 150mM sodium chloride, 10% glycerol (v/v), 2mM TCEP. Purity: >95% (SDS-PAGE). UBE2D1 (UbcH5a) 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. - UBE2D1 (UbcH5a) 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.
- Storage Instruction-80°C
- UNSPSC12352202