RPS27A Human

Ubiquitin is a globular protein with a compact structure. It contains multiple lysine residues and two C-terminal glycines, which are crucial for its function. The primary role of ubiquitin is to tag proteins for degradation via the ubiquitin-proteasome system. This process involves the attachment of ubiquitin molecules to substrate proteins, marking them for degradation by the proteasome. This tagging process is known as ubiquitination and is mediated by a series of enzymes: ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3) .

In humans, ubiquitin is encoded by four different genes located on chromosomes 17, 2, 19, and 12. These genes produce ubiquitin either as a single protein or as part of a larger precursor protein that is subsequently processed to release free ubiquitin . The high degree of conservation in ubiquitin’s amino acid sequence across different species underscores its fundamental importance in cellular biology.

Recombinant human ubiquitin is produced using genetic engineering techniques, typically in bacterial systems such as Escherichia coli. The recombinant protein is identical to the naturally occurring human ubiquitin in terms of its amino acid sequence and functional properties. It is widely used in research to study protein degradation, signal transduction, and other cellular processes involving ubiquitin .

Recombinant ubiquitin is a valuable tool in biochemical and cell biology research. It is used to investigate the mechanisms of ubiquitination and deubiquitination, the roles of ubiquitin in various signaling pathways, and the regulation of protein turnover. Additionally, recombinant ubiquitin can be conjugated to substrate proteins in vitro to study the effects of ubiquitination on protein function and stability .

Recombinant human ubiquitin is typically supplied as a lyophilized powder or in a solution. It should be stored at -20 to -70°C to maintain its stability. Once reconstituted, it should be used under sterile conditions and stored at the recommended temperature to avoid degradation .