Recombinant Human LMF1 protein

LMF1 (lipase maturation factor 1) is a critical endoplasmic reticulum (ER)-resident protein involved in the assembly and secretion of active lipoprotein lipase (LPL) and related enzymes. Discovered in 2007 through studies on combined lipase deficiency (CLD), LMF1 was identified as the gene mutated in a murine model of CLD, a condition characterized by defective lipid metabolism due to impaired lipase activity. Structurally, LMF1 is a 59 kDa membrane-associated protein containing an N-terminal signal peptide, a conserved DUF1222 domain, and a C-terminal transmembrane domain. It functions as a molecular chaperone, facilitating the folding and dimerization of lipases like LPL, hepatic lipase, and endothelial lipase within the ER. Without LMF1. these enzymes aggregate and undergo ER-associated degradation, leading to systemic lipid processing defects.

Recombinant LMF1 protein is produced using expression systems (e.g., mammalian cells or bacteria) to study its structural and functional properties. Research has shown that recombinant LMF1 can restore lipase activity in LMF1-deficient cells, highlighting its therapeutic potential for genetic disorders affecting lipid metabolism. Its role extends beyond lipase maturation, with implications in cardiovascular diseases, obesity, and diabetes. Current studies focus on characterizing post-translational modifications, interaction partners (e.g., GRP94), and tissue-specific regulatory mechanisms. The development of recombinant LMF1 has become pivotal for both basic research and clinical applications, offering insights into cellular protein quality control pathways and experimental therapies for metabolic disorders.