Thioester Activity Assay: UBE2D3 (UbcH5c) 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 UBE2D3.
Thioester Activity Assay: UBE2D3 (UbcH5c) 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 UBE2D3.
UBE2D3 [UbcH5c ] (human) (rec.) (untagged)
SBB-CE0019
Overview
- SupplierSouth Bay Bio
- Product NameUBE2D3 [UbcH5c ] (human) (rec.) (untagged)
- Delivery Days Customer10
- CertificationResearch Use Only
- Estimated Purity>95%
- Protein IDP61077
- Protein NameUbiquitin-conjugating enzyme E2 D3
- Scientific DescriptionProtein. Human UBE2D3 (aa1-147)is untagged. Source: E. coli. Formulation: Liquid. In 50mM HEPES pH 8, 200mM sodium chloride, 10% glycerol (v/v), 1mM TCEP. Purity: >95% (SDS-PAGE). UBE2D3 (UbcH5c) is an E2 ubiquitin conjugating enzyme. An E1 activating enzyme is required to attach ubiquitin to UBE2D3 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 UBE2D3-Ub thioester. UBE2D3 is capable of associating with numerous known E3 ligases including MDM2, which target proteins such as p53 for proteasomal degradation through polyubiquitination. - UBE2D3 [UbcH5c] is an E2 ubiquitin conjugating enzyme. An E1 activating enzyme is required to attach ubiquitin to UBE2D3 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 UBE2D3-Ub thioester. UBE2D3 is capable of associating with numerous known E3 ligases including MDM2, which target proteins such as p53 for proteasomal degradation through polyubiquitination.
- Storage Instruction-80°C
- UNSPSC12352202