UBE2E3 Human
Description
UBE2E3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Ubiquitin conjugating enzymes, also known as E2 enzymes, play a crucial role in the ubiquitination process, which is essential for protein degradation and regulation within cells. The Ubiquitin Conjugating Enzyme E2E3 (UBE2E3) is one such enzyme that is involved in the transfer of ubiquitin from the E1 activating enzyme to the substrate protein, facilitated by the E3 ligase. This article delves into the background, structure, function, and significance of the human recombinant UBE2E3.
UBE2E3 is a member of the E2 enzyme family, characterized by a conserved ubiquitin-conjugating (UBC) domain. This domain is responsible for the enzyme’s ability to bind ubiquitin and interact with E3 ligases. The human recombinant form of UBE2E3 is produced through recombinant DNA technology, allowing for the study and application of this enzyme in various research and therapeutic contexts.
The primary function of UBE2E3 is to facilitate the transfer of ubiquitin from the E1 enzyme to the target protein, a process that is mediated by the E3 ligase. This transfer is crucial for tagging proteins for degradation by the proteasome, a process that maintains cellular homeostasis by removing damaged or misfolded proteins .
The ubiquitination process involves three main steps:
- Activation: The ubiquitin-activating enzyme (E1) activates ubiquitin in an ATP-dependent manner.
- Conjugation: The activated ubiquitin is transferred to the ubiquitin-conjugating enzyme (E2), such as UBE2E3.
- Ligation: The ubiquitin ligase (E3) facilitates the transfer of ubiquitin from the E2 enzyme to the lysine residue on the target protein .
UBE2E3 specifically interacts with various E3 ligases to ensure the precise and regulated transfer of ubiquitin, which is essential for the targeted degradation of proteins.
The human recombinant UBE2E3 enzyme is invaluable in research due to its role in the ubiquitination pathway. It is used to study protein degradation mechanisms, cellular regulation, and the development of therapeutic strategies for diseases associated with protein misfolding and degradation, such as neurodegenerative disorders and cancers .
