Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
UBE2W produced in E.Coli is a single, non-glycosylated polypeptide chain containing 171 amino acids (1-151 a.a.) and having a molecular mass of 19.5kDa.
UBE2W is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
The protein UBE2W, also known as ubiquitin-conjugating enzyme E2 W, plays a crucial role in the ubiquitin system, a cellular pathway for protein degradation. UBE2W receives ubiquitin, a small regulatory protein, from the E1 complex and facilitates its attachment to target proteins. This process, known as ubiquitination, can mark proteins for degradation or alter their activity. UBE2W exhibits specific activity in vitro, catalyzing both monoubiquitination (attachment of a single ubiquitin molecule) and 'Lys-11'-linked polyubiquitination (attachment of a chain of ubiquitin molecules linked through lysine residues at position 11). UBE2W is widely expressed throughout the body, with notably high levels found in the testis, suggesting its involvement in testis-specific functions.
This product consists of the human UBE2W protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 171 amino acids, with the UBE2W sequence spanning amino acids 1 to 151. To facilitate purification and detection, a 20 amino acid His-tag is fused to the N-terminus of the protein. The molecular weight of the UBE2W protein with the His-tag is 19.5 kDa. The protein has been purified using proprietary chromatographic techniques to ensure its high quality and purity.
Probable ubiquitin-conjugating enzyme E2 W, Ubiquitin carrier protein W, Ubiquitin-protein ligase W, UBE2W, hUBC-16, FLJ11011.
MGSSHHHHHH SSGLVPRGSH MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C.
Ubiquitin-conjugating enzyme E2W (UBE2W) is a protein-coding gene that plays a crucial role in the ubiquitination process, which is a post-translational modification essential for various cellular functions. UBE2W is involved in the attachment of ubiquitin to target proteins, a process that regulates protein degradation, DNA repair, cell cycle, and immune responses .
Ubiquitination is a highly conserved mechanism in eukaryotic cells, involving three main types of enzymes: E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin ligase). The E2 enzyme, such as UBE2W, acts as an intermediary, transferring ubiquitin from the E1 enzyme to the substrate protein, which is recognized by the E3 ligase .
UBE2W has been identified as a key player in the ubiquitination process, particularly in the repair of DNA damage. It is known to be involved in the ubiquitination of proteins that are crucial for maintaining genomic stability. Additionally, UBE2W has been implicated in the regulation of protein turnover, which is vital for cellular homeostasis .
Recent studies have highlighted the prognostic value of UBE2W in various cancers, including breast cancer. High expression levels of UBE2W have been associated with poor prognosis and resistance to endocrine therapy in breast cancer patients. This suggests that UBE2W could serve as a potential biomarker for cancer prognosis and a target for therapeutic interventions .
Human recombinant UBE2W is produced using recombinant DNA technology, which involves inserting the UBE2W gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study the ubiquitination process and its implications in diseases .