NGAL/Lipocalin-2 Protein (His Tag) (recombinant mouse)

Protein Construction: Recombinant Mouse Neutrophil gelatinase-associated lipocalin is produced by our Mammalian expression system and the target gene encoding Gln21-Asn200 is expressed with a 6His tag at the C-terminus. Sequence: Gln21-Asn200. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 23 kDa. Protein function: Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), is a secretory protein of the lipocalin superfamily. Lipocalin-2 contains a signal peptide that enables it to be secreted and form complexes with matrix metalloproteinase-9 (MMP-9) through disulfide bonds. Similar to other lipocalin family members, Lipocalin-2 is involved in diverse cellular processes, including the transport of small hydrophobic molecules, protection of MMP-9 from proteolytic degradation, and cell signaling. Furthermore, Lipocalin-2 can tightly bind to bacterial siderophore through a cell surface receptor, possibly serving as a potent bacteriostatic agent by sequestering iron, regulating innate immunity and protecting kidney epithelial cells from ischemia-reperfusion injury. This protein is mainly expressed in neutrophils and in lower levels in the kidney, prostate, and epithelia of the respiratory and alimentary tracts. Recent evidence also suggests its role as a biomarker for renal injury and inflammation. Protein function: Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413). Binds iron through association with 2,5-dihydroxybenzoic acid (2,5- DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis. Involved in innate immunity, limits bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin (PubMed:15531878, PubMed:16446425). Can also bind siderophores from M.tuberculosis. [The UniProt Consortium]