UBE2Q2 Human
Description
UBE2Q2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Ubiquitin Conjugating Enzyme E2Q2 (UBE2Q2) is a protein-coding gene that plays a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin, a small regulatory protein, is attached to substrate proteins. This process is essential for various cellular functions, including protein degradation, cell cycle regulation, and DNA repair.
UBE2Q2 belongs to the ubiquitin-conjugating enzyme family, also known as E2 enzymes. These enzymes are responsible for receiving ubiquitin from the E1 activating enzyme and transferring it to the target protein, often with the help of an E3 ligase. UBE2Q2 specifically catalyzes the covalent attachment of ubiquitin to various substrate proteins, marking them for degradation by the proteasome or altering their cellular location and activity .
The human recombinant UBE2Q2 is typically produced in Escherichia coli (E. coli) expression systems. The recombinant protein is a single, non-glycosylated polypeptide chain containing 398 amino acids and has a molecular mass of approximately 45.2 kDa. It is fused to a 23 amino acid His-tag at the N-terminus to facilitate purification using chromatographic techniques .
UBE2Q2 participates in the ubiquitination cascade, which involves three main steps:
- Activation: Ubiquitin is activated by the E1 enzyme in an ATP-dependent manner.
- Conjugation: The activated ubiquitin is transferred to the E2 enzyme (UBE2Q2).
- Ligation: The E3 ligase facilitates the transfer of ubiquitin from the E2 enzyme to the substrate protein.
The ubiquitination process can result in different types of ubiquitin linkages, leading to various cellular outcomes. For example, polyubiquitination typically targets proteins for degradation by the 26S proteasome, while monoubiquitination can regulate protein activity and localization .
