The Recombinant Human Lipocalin-2/NGAL/LCN2 Protein is a biologically active recombinant protein that plays a significant role in various cellular processes and signaling pathways in human biology. This protein is widely employed in immunological research, cell biology studies, protein-protein interaction analyses, and therapeutic development, providing researchers with a reliable tool for investigating Lipocalin-2/NGAL/LCN2 function and its implications in health and disease.
This product (SKU: RPCB0006) is produced using advanced expression systems and features a C-His tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 21.39 kDa with an observed molecular weight of 20-25 kDa under denaturing conditions, achieving ≥ 95 % as determined by SDS-PAGE.. Functional bioactivity has been validated through rigorous quality control assays, confirming its suitability for demanding research applications.
High quality, high purity and low endotoxin recombinant Recombinant Human Lipocalin-2/NGAL/LCN2 Protein (RPCB0006), tested reactivity in HEK293 cells and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 0.01 EU/μg of the protein by LAL method
Purity:
≥ 95 % as determined by SDS-PAGE.
Formulation:
Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
Bio-Activity:
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 recombinant mouse Lipocalin-2. Recombinant human Lipocalin-2 can bind >0.60 μM of Fe(DHBA)3.
Reconstitution:
Centrifμge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃. Store the lyophilized protein at -20℃ to -80℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), was originally identified as a component of neutrophil granules. 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). Its expression has been observed in most tissues normally exposed to microorganism, and its synthesis is induced in epithelial cells during inflammation. Lipocalin-2 has been implicated in a variety of processes including cell differentiation, tumorigenesis, and apoptosis. Studies indicate that Lipocalin-2 binds a bacterial catecholate sidropore bound to ferric ion such as enterobactin with a subnanomolar dissociation constant. 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). 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. 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.
Recombinant Human Lipocalin-2/NGAL/LCN2 Protein was determined by SDS-PAGE under reducing.
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 recombinant mouse Lipocalin-2. Recombinant human Lipocalin-2 can bind >0.60 μM of Fe(DHBA)3.
