Recombinant Human UBQLN1 protein

UBQLN1 (ubiquilin-1) is a multifunctional adaptor protein belonging to the ubiquitin-like protein family, primarily involved in regulating protein degradation pathways. It plays a critical role in the ubiquitin-proteasome system by linking ubiquitinated substrates to the proteasome for degradation. Structurally, UBQLN1 contains an N-terminal ubiquitin-like (UBL) domain that interacts with the 26S proteasome and a C-terminal ubiquitin-associated (UBA) domain that binds polyubiquitin chains on misfolded or damaged proteins. This dual-domain architecture enables UBQLN1 to act as a shuttle, recognizing ubiquitinated cargo and delivering it to degradation machinery.

Recombinant UBQLN1 protein is produced through genetic engineering, often expressed in bacterial (e.g., E. coli) or mammalian systems for research applications. It is commonly purified using affinity tags (e.g., His-tag) for studies on protein-protein interactions, substrate recognition, and proteasomal regulation. Researchers utilize recombinant UBQLN1 to investigate its role in cellular quality control, particularly in neurodegenerative diseases like Alzheimer's, Parkinson's, and ALS, where dysfunctional protein clearance contributes to pathological protein aggregation. Studies also explore its involvement in autophagy, DNA repair, and endoplasmic reticulum stress responses. Dysregulation of UBQLN1 expression or mutations in its coding sequence have been linked to disease progression, making it a potential therapeutic target. Its recombinant form serves as a vital tool for structural studies, inhibitor screening, and mechanistic insights into ubiquitin-dependent proteostasis.