|Detection of Human Peroxiredoxin 6 by Western Blot. Western blot shows lysates of HEK293 human embryonic kidney cell line and HeLa human cervical epithelial carcinoma cell line. PVDF membrane was probed with 1 µg/mL of Human Peroxiredoxin 6 Monoclonal Antibody (Catalog # MAB3490) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for Peroxiredoxin 6 at approximately 26 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
|Detection of Human Peroxiredoxin 6 by Simple WesternTM. Simple Western lane view shows lysates of HEK293T human embryonic kidney cell line and HeLa human cervical epithelial carcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for Peroxiredoxin 6 at approximately 31 kDa (as indicated) using 5 µg/mL of Mouse Anti-Human Peroxiredoxin 6 Monoclonal Antibody (Catalog # MAB3490). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.|
Human Peroxiredoxin 6 (Prx-6) is a 26 kDa, cytosolic antioxidant enzyme that belongs to the 1-Cys class of the THP/ahpC family of proteins. This protein is 224 amino acids (aa) in length and has one catalytic cysteine at Cys46. Following an attack on peroxide, Cys46 is oxidized to cysteine sulfenic acid and exists in a stable conformation. Reduced, Prx-6 is a homotetramer. When activated, it apparently forms a covalently-associated homodimer. In addition to glutathione peroxidase activity, Prx-6 is also reported to demonstrate phospholipase A2 activity. Thus, Prx-6 likely plays a role in phospholipid turnover. Ser32 in a GWSWG motif is required for its enzymatic activity. Human Prx-6 is 92% and 90% aa identical to rat and mouse Prx-6, respectively.