Measured by its ability to bind Iron(III) dihydroxybenzoic acid [Fe(DHBA)3]. The binding of Fe(DHBA)3 results in the quenching of Trp fluorescence in Lipocalin-2. >1.0 µM of Fe(DHBA)3 can be bound under the described conditions.
Mouse myeloma cell line, NS0-derived mouse Lipocalin-2/NGAL protein Gln21-Asn200 with a C-terminal 10 His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
22 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Lipocalin-2/NGAL Protein, CF
25 kDa alpha-2-microglobulin-related subunit of MMP-9
lipocalin 2 (oncogene 24p3)
migration-stimulating factor inhibitor
neutrophil gelatinase-associated lipocalin
Mouse Lipocalin-2 was cloned from mouse kidney cells (1). Its very high level of expression at the post-stratum uterus gave it the name uterocalin (2). Lipocalin-2 has been implicated in a variety of processes including cell differentiation, tumorigenesis, and apoptosis (3‑5). Studies indicate that Lipocalin-2 binds a bacterial catecholate siderophore that is bound to a ferric ion, such as enterobactin, with a subnanomolar dissociation constant (KD = 0.41 nM) (6). 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) (6). Secretion of Lipocalin-2 in immune cells increases in response to stimulation of Toll-like receptor as an acute phase response to infection. As a result, it acts as a potent bacteriostatic reagent by sequestering iron (7). Moreover, Lipocalin-2 can alter the invasive and metastatic behavior of Ras-transformed breast cancer cells in vitro and in vivo by reversing the epithelial to mesenchymal transition inducing activity of Ras, through restoration of E-cadherin expression, via effects on the Ras-MAPK signaling pathway (8).
Hraba-Renevey, s. et al. (1989) Oncogene. 4:601.
Liu, Q. et al. (1993) Mol Reprod Dev. 46:507.
Kjeldsen L, et al. (2000) Biochim Biophys Acta. 1482:272.
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