Recombinant Human LRMP Protein

Lymphoid-restricted membrane protein (LRMP), also known as JSP.1 or BAT2. is a leucine-rich repeat-containing protein predominantly expressed in immune cells, particularly B and T lymphocytes. First identified in the 1990s, LRMP is anchored to the endoplasmic reticulum (ER) membrane and structurally characterized by multiple leucine-rich repeats (LRRs) and phosphorylation sites. Its primary function remains under investigation, but studies suggest roles in modulating immune responses, potentially through interactions with MHC class II molecules and ER-associated protein trafficking. LRMP has been linked to immune regulation, with evidence implicating it in autoimmunity, lymphocyte activation, and antigen presentation pathways. Recombinant human LRMP protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce purified, functional domains for mechanistic studies. Researchers utilize it to explore LRMP’s binding partners (e.g., BAT3), signaling cascades, and its influence on immune cell differentiation. Ongoing research focuses on its therapeutic potential in immune disorders and cancer, as dysregulated LRMP expression correlates with altered immune surveillance. Its recombinant form enables structural analysis, antibody development, and high-throughput screening for drug discovery. Despite limited natural abundance, recombinant LRMP provides critical insights into its enigmatic biological roles.