UBE2D1 Human
Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.
Description
UBE2D1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 19kDa.
UBE2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.
MGSSHHHHHH SSGLVPRGSH MGSMALKRIQ KELSDLQRDP PAHCSAGPVG DDLFHWQATI MGPPDSAYQG GVFFLTVHFP TDYPFKPPKI AFTTKIYHPN INSNGSICLD ILRSQWSPAL TVSKVLLSIC SLLCDPNPDD PLVPDIAQIY KSDKEKYNRH AREWTQKYAM.
Product Science Overview
Ubiquitin Conjugating Enzyme E2D1, also known as UBE2D1, is a crucial component of the ubiquitin-proteasome system (UPS), which is responsible for the targeted degradation of proteins within eukaryotic cells. This enzyme plays a pivotal role in the ubiquitination process, acting as an intermediary that transfers ubiquitin from the E1 activating enzyme to the E3 ligase, which then attaches ubiquitin to the substrate protein.
Ubiquitination is a post-translational modification that involves the attachment of ubiquitin, a small regulatory protein, to lysine residues on target proteins. This process typically involves three main steps:
- Activation: Ubiquitin is activated by the E1 enzyme in an ATP-dependent manner, forming a thioester bond with a cysteine residue on the E1 enzyme.
- Conjugation: The activated ubiquitin is then transferred to the active-site cysteine of the E2 enzyme (UBE2D1) via a transthiolation reaction.
- Ligation: The E3 ligase facilitates the transfer of ubiquitin from the E2 enzyme to the target protein, forming an isopeptide bond between the ubiquitin and the lysine residue on the substrate .
UBE2D1 is involved in various cellular processes, including:
- Protein Degradation: By tagging proteins with ubiquitin, UBE2D1 marks them for degradation by the 26S proteasome, thus regulating protein turnover and maintaining cellular homeostasis .
- Signal Transduction: UBE2D1 plays a role in key signaling pathways, such as the NF-κB pathway, by regulating the ubiquitination of specific signaling proteins .
- DNA Repair: UBE2D1 is involved in the ubiquitination of histone proteins, which is crucial for DNA repair and chromatin remodeling .
Recombinant UBE2D1 is produced using recombinant DNA technology, which involves cloning the UBE2D1 gene into an expression vector, introducing the vector into a host cell (such as E. coli), and inducing the expression of the UBE2D1 protein. The recombinant protein is then purified for use in research and therapeutic applications.
Recombinant UBE2D1 is widely used in biochemical and structural studies to understand the mechanisms of ubiquitination and its role in various cellular processes. It is also used in drug discovery and development, particularly in the design of inhibitors that target the ubiquitin-proteasome system for the treatment of diseases such as cancer and neurodegenerative disorders .
