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The UFD1L gene encodes the human homolog of the yeast ubiquitin fusion degradation 1 (UFD1) protein . The human recombinant UFD1L protein is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 330 amino acids (1-307) with a molecular mass of approximately 36.9 kDa . The recombinant protein is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification using chromatographic techniques .
UFD1L is a subunit of the Cdc48-Ufd1-Npl4 complex, which is involved in the sorting of ubiquitylated substrates for degradation by the proteasome . This complex plays a significant role in the elimination of sumoylated factors through the coupled action of Sumo-targeted ubiquitin ligases (STUbLs) and UFD1 . The degradation of ubiquitin fusion proteins is a critical process for the regulation of protein quality control and the prevention of cellular stress.
Recombinant UFD1L protein is used in various research applications to study the ubiquitin-proteasome system and its role in cellular processes. It is also utilized in the investigation of protein degradation pathways and the development of therapeutic strategies for diseases associated with protein misfolding and aggregation.
The UFD1L human recombinant protein is typically stored at -20°C for long-term storage, with the addition of a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) to prevent degradation . It is recommended to avoid multiple freeze-thaw cycles to maintain the protein’s stability and functionality .