|Reactivity||Human, Mouse, Rat|
|Calculated MW||22875 Da|
|Other Names||Lipocalin2, Lipocalin 2, Lcn2, Lcn 2, Lcn-2, Neutrophil gelatinase associated lipocalin, NGAL|
|Format||100 µg (0.5 mg/ml) affinity purified rabbit anti-Lipocalin 2 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Precautions||Lipocalin-2 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. 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, possibly by sequestrating iron, leading to limit bacterial growth.|
|Cellular Location||Secreted. Note=Upon binding to the SLC22A17 (24p3R) receptor, it is internalized|
|Tissue Location||Detected in lung, spleen, uterus, vagina and epididymis.|
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Provided below are standard protocols that you may find useful for product applications.
Lipocalin 2 is from a family of proteins that are involved in the transportation of small hydrophobic molecules including steroids, retinoids, bilin and retinods. Lipocalins have been linked to many biolchemical processes such as immune response, pheromone transport, biological prostaglandin synthesis, retinoid binding, and cancer cell interactions.
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