Lipocalin-2/NGAL Protein, Rat (sf9, His)

Lipocalin-2/NGAL, a multifaceted iron-trafficking protein, participates in diverse biological processes including apoptosis, innate immunity, and renal development. Through its association with the siderophore 2,3-dihydroxybenzoic acid (2,3-DHBA), Lipocalin-2 binds and shuttles iron, dynamically influencing cellular iron concentrations based on the holo-24p3 (iron-bound) or apo-24p3 (iron-free) forms. The interaction with the SLC22A17 receptor mediates iron release or chelation, finely regulating intracellular iron levels. In apoptosis triggered by interleukin-3 (IL3) deprivation, the iron-loaded form prevents apoptosis, while the iron-free form induces BCL2L11/BIM expression, leading to programmed cell death. Lipocalin-2 also contributes to innate immunity by sequestering bacterial siderophores, such as enterobactin, and exhibits the ability to bind siderophores from M. tuberculosis. Structurally, Lipocalin-2 exists as a monomer, homodimer (disulfide-linked), and forms a heterodimer (disulfide-linked) with MMP9. These diverse interactions underscore the versatility of Lipocalin-2 in orchestrating critical cellular and immune responses.