UBE2G2 Human
Description
UBE2G2 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 E2G2, also known as UBE2G2 or UBC7, is a crucial component of the ubiquitin-proteasome system (UPS), which is responsible for protein degradation in eukaryotic cells. This enzyme plays a significant role in various cellular processes, including protein turnover, cell cycle regulation, and response to stress.
UBE2G2 is a member of the E2 ubiquitin-conjugating enzyme family. The crystal structure of human UBE2G2 was solved at a resolution of 2.56 angstroms, providing insights into its functional mechanisms . The enzyme operates by transferring ubiquitin from an E1 ubiquitin-activating enzyme to an E3 ubiquitin ligase, which then attaches ubiquitin to target proteins. This process tags the proteins for degradation by the 26S proteasome.
UBE2G2 is particularly involved in endoplasmic reticulum-associated degradation (ERAD), a pathway that targets misfolded or damaged proteins in the endoplasmic reticulum for degradation . This function is critical for maintaining cellular homeostasis and preventing the accumulation of defective proteins that could lead to diseases.
The ubiquitination process involves a cascade of enzymatic reactions:
- Activation: Ubiquitin is activated by an E1 enzyme in an ATP-dependent manner.
- Conjugation: The activated ubiquitin is transferred to the E2 enzyme (UBE2G2).
- Ligation: The E2 enzyme, in conjunction with an E3 ligase, transfers ubiquitin to the substrate protein .
UBE2G2 has been shown to direct polyubiquitination to preferred lysine residues on target proteins, influencing the type of polyubiquitin chains formed and thus determining the fate of the substrate .
Recent studies have explored the potential of UBE2G2 in targeted protein degradation. For instance, chimeric human E2 ubiquitin-conjugating enzymes have been engineered to induce the degradation of specific disease-associated proteins, such as SHP2 and KRAS, within cancer cell lines . This approach, known as bioPROTACs, leverages the natural role of E2 enzymes in the ubiquitination process to selectively degrade target proteins, offering a promising strategy for therapeutic intervention.
