Lipocalin-2/NGAL Protein, Mouse (HEK293, His, solution)

Lipocalin-2/NGAL, an iron-trafficking protein, participates in various biological processes, including apoptosis, innate immunity, and renal development. Through its interaction with the siderophore 2,3-dihydroxybenzoic acid (2,3-DHBA), reminiscent of bacterial enterobactin, Lipocalin-2/NGAL modulates cellular iron levels, acting as a conveyor or extractor of iron depending on the cellular context. The iron-bound form (holo-24p3) is internalized upon binding to the SLC22A17 (24p3R) receptor, releasing iron and elevating intracellular iron concentration. Conversely, the iron-free form (apo-24p3), upon binding to SLC22A17 (24p3R), associates with an intracellular siderophore, leading to iron chelation and subsequent extracellular iron transfer, thereby diminishing intracellular iron levels. In the realm of apoptosis induced by interleukin-3 (IL3) deprivation, the iron-loaded form averts apoptosis by increasing intracellular iron concentration, while the iron-free form fosters apoptosis by reducing intracellular iron levels, inducing the expression of the proapoptotic protein BCL2L11/BIM. Lipocalin-2/NGAL also plays a crucial role in innate immunity by restraining bacterial proliferation through the sequestration of iron bound to microbial siderophores like enterobactin. Moreover, it exhibits the ability to bind siderophores from M.tuberculosis. Lipocalin-2/NGAL can exist as a monomer, a homodimer linked by disulfide bonds, or a heterodimer with MMP9, further expanding its functional versatility.