Rat Lipocalin-2/NGAL Antibody

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 (K_D = 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 K_D 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).