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Description
The enzyme 5-lipoxygenase (5-LO) plays a key role in regulating the production of leukotrienes (LTs) (Funk, 2001). Overproduction of LTs contributes to several diseases, most notably chronic inflammatory diseases, including asthma (Drazen et al., 1994), fibrosis (Wilborn et al., 1996) and atherosclerosis (Dwyer et al., 2004). Recent work has demonstrated that the activity of 5-LO is regulated by PKA phosphorylation of serine-523 in 5-LO (Luo et al., 2004). Under normal conditions, this phosphorylation may be important in limiting inflammation. Abnormal signaling through cAMP and PKA, then, could contribute to a variety of diseases, including those characterized by chronic inflammation. The phospho-specific antibody to Ser523 on 5-LO is thus likely to provide a valuable tool for studies of the role of 5-LO regulation in diseases such as asthma, fibrosis and atherosclerosis. Anti-Phospho Ser523 5-Lipoxygenase Western blot of rat cortex lysate showing specific immunolabeling of the ~80k doublet of 5-LO phosphorylated at Ser523 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: (-Ptase). The blot is identical to the control except that it was incubated in (-Ptase (1200 units for 30 min) before being exposed to the 5-LO Ser523 antibody. The immunolabeling is completely eliminated by treatment with (-Ptase.