|Detection of Mouse and Rat Lipocalin‑2/NGAL by Western Blot. Western blot shows lysates of rat ovary tissue and mouse lung tissue. PVDF membrane was probed with 1 µg/mL of Mouse/Rat Lipocalin‑2/NGAL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3508) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for Lipocalin‑2/NGAL at approximately 25 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Lipocalin-2, also known as neutrophil gelatinase-associated Lipocalin and uterocalin (NGAL), has been implicated in a variety of processes including cell differentiation, tumorigenesis, and apoptosis (1‑3). It binds a bacterial catecholate sidropore bound to ferric ion such as enterobactin with a subnanomolar dissociation constant (KD = 0.41 nM) (4). The bound ferric enterobactin complex breaks down slowly in a month into dihydroxybenzoyl serine and dihydroxybenzoic acid (DHBA). It also binds to a ferric DHBA complex with much less KD values (7.9 nM) (4). Secretion of Lipocalin-2 in immune cells increases by stimulation of Toll-like receptor as a acute phase response to infection. As a result, it acts as a potent bacteriostatic reagents by sequestering iron (5). Moreover, Lipocalin-2 can alter the invasive and metastatic behavior of Ras-transformed breast cancer cells in vitro and in vivo by reversing epithelial to mesenchymal transition inducing activity of Ras, through restoration of E-cadherin expression, via effects on the Ras-MAPK signaling pathway (6). In the kidney, Lipocalin-2-mediated iron trafficking may be involved in protection from renal injury, and it has been implicated as a marker for early kidney failure (7, 8).
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