|Detection of Human Lipocalin‑2/NGAL by Western Blot. Western blot shows lysates of K562 human chronic myelogenous leukemia cell line. PVDF membrane was probed with 1 µg/mL of Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB1757) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Lipocalin‑2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Lipocalin‑2/NGAL in Human Pancreas. Lipocalin‑2/NGAL was detected in immersion fixed paraffin-embedded sections of human pancreas using Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB1757) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Rabbit HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS005) and counterstained with hematoxylin (blue). Specific staining was localized to plasma membrane of ductal cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
|Detection of Human Lipocalin‑2/NGAL by Western Blot. Western blot shows lysates of Capan‑1 human pancreatic adenocarcinoma cell line, HT‑29 human colon adenocarcinoma cell line, and human bone marrow tissue. PVDF membrane was probed with 0.2 µg/mL of Rat Anti-Human Lipocalin‑2/NGAL Monoclonal Antibody (Catalog # MAB1757) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Lipocalin‑2/NGAL at approximately 22 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
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).
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Western Blot: Human Lipocalin‑2/NGAL Antibody [MAB1757-100]