Human Lipocalin-2/NGAL Antibody Summary
Accession # P80188
This antibody functions as an ELISA detection antibody when paired with Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB17571).
This product is intended for assay development on various assay platforms requiring antibody pairs.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Human Lipocalin‑2/NGAL ELISA Standard Curve. Recombinant Human Lipocalin‑2/NGAL protein was serially diluted 2-fold and captured by Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB17571) coated on a Clear Polystyrene Microplate (Catalog # DY990). Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB17573) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Members of Lipocalin family share a highly conserved fold with an eight-stranded antiparallel beta barrel, and act as a transporters, carrying small molecules to specific cells (1). Lipocalin‑2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), was originally identified as a component of neutrophil granules (2). It is a 25 kDa protein existing in monomeric and homo- and heterodimeric forms, the latter as a dimer with human neutrophil gelatinases (MMP-9) (2). Its expression has been observed in most tissues normally exposed to microorganism, and its synthesis is induced in epithelial cells during inflammation (3). 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 sidropore bound to 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 by 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 epithelial to mesenchymal transition inducing activity of Ras, through restoration of E-cadherin expression, via effects on the Ras-MAPK signaling pathway (8).
- Flower, D.R. et al. (1994) FEBS Lett. 354:7.
- Kjeldsen, L. et al. (1993) J. Biol. Chem. 268:10426.
- Kjeldsen L, et al. (2000) Biochim Biophys Acta. 1482:272.
- Devireddy, L.R. et al. (2001) Science 293: 829.
- Yang, M.B. et al. (2002) Mol. Cell. 10:1045.
- Goetz, D.H. et al. (2002) Mol. Cell 10:1033.
- Flo, T.H. et al. (2004) Nature 432:917.
- Hanai, J. et al. (2005) J. Biol. Chem. 280:13641.
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