Recombinant Rat Lipocalin-2/NGAL Protein, CF

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).