Mouse Lipocalin‑2/NGAL Antibody

Detection of Mouse Lipocalin-2/NGAL by Immunoprecipitation

Epitope mapping of LCN2 mAb. (A) ELISA quantification of relative binding of LCN2 mAb to 56 peptides covering the mouse LCN2 protein (n = 3); (B) The combined sequences of peptides 22–24 are shown in red at amino acids 64–84 of the mouse LCN2 protein. The N-terminal signal peptide that was cleaved prior to the secretion of the protein is underlined and not included in the epitope mapping. Cys-78 and Cys-177 forming an intramolecular disulfide bond (blue); (C) Alignment of the LCN2 mAb epitope sequences from mouse, rat, and human LCN2 homologs. Conserved amino acids are underlined. Amino acids interacting with siderophore are highlighted in pink. Conserved cysteines are highlighted in blue; (D) The crystal structure of human LCN2 protein containing a siderophore (black) and an iron (orange). The epitope of LCN2 mAb, highlighted in red, is located in the beta 3 and beta 4 strands. The side chains of amino acids bound with siderophore are colored in pink. An intramolecular disulfide bond formed between Cys-78 in the epitope and Cys-177 near the C-terminal (blue); (E) Representative Western blot showing that increased concentrations of epitope peptides from mouse (YNVTSILVRDQDQGCRYWIRT) and human (YNVTSVLFRKKKCDYWIRT) tissue reduced the level of immunoprecipitated mouse (mLCN2) or human LCN2 protein (hLCN2). Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/32872405), licensed under a CC-BY license. Not internally tested by R&D Systems.