|Detection of Human NQO-2 by Western Blot. Western blot shows lysates of human liver tissue, human kidney tissue, HepG2 human hepatocellular carcinoma cell line, K562 human chronic myelogenous leukemia cell line, and A549 human lung carcinoma cell line. PVDF membrane was probed with 0.25 µg/mL of Sheep Anti-Human NQO-2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7868) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for NQO-2 at approximately 26 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
NQO-2 (NADPH Quinone acceptor Oxidoreductase 2; also QR2, melatonin receptor 3/MT3 and NRH dehydrogenase) is a 25-26 kDa cytoplasmic flavoprotein member of the NAD(P)H dehydrogenase family of enzymes. It shows restricted expression, being found in retinal pigment epithelium, prostatic fibroblasts, select CNS neurons and RBCs. Like NQO-1, NQO-2 would appear to reduce catechol quinones, but without the use of NADH. In contrast to NQO-1, NQO-2 would appear to activate some quinones, generating cytotoxic products. NQO-2 also reportedly binds and stabilizes key cell protection molecules such as p53, thus acting as a gatekeeper for proteosome-mediated protein turnover. Finally, NQO-2 reportedly binds to melatonin, an act that may promote the subsequent binding of the androgen receptor and an inhibition of cell proliferation. Human NQO-2 is 231 amino acids (aa) in length. It contains a flavodoxin-like domain (aa 4-212) and three utilized Ser phosphorylation sites. NQO-2 functions as a noncovalent homodimer. There are two potential isoform variants. One shows an alternative start site at Met117, while another shows a deletion of aa 102-139. Full length human NQO-2 shares 81% aa sequence identity with mouse NQO-2, and less than 50% aa sequence identity with human NQO-1.
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