recombinant full length human COX I, 599 amino acids.
Application
Monoclonal Anti-COX I antibody produced in mouse is suitable for ELISA and western blotting. It was used to detect mitochondrial cytochrome c oxidase protein markerin homogenate and lipid droplet fractions isolated from L-cells by western blot analysis.
Biochem/physiol Actions
COX-I, an isoform of COX enzyme with 599 amino acid residues, catalyzes the conversion of arachinodate to prostaglandin H2. It is expressed mainly in the gut for the production of prostaglandins, which inhibit gastric secretion. It is involved in the regulation of homeostatic functions throughout the body, such as vascular hemostasis, renal blood flow, and maintenance of glomerular function. It is a target of NSAID (non-steroidal anti-inflammatory drugs) such as aspirin. COX-I can be induced by IL-β and other cytokines in monocytes, macrophages, and other cells as part of the inflammatory response.
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Human prostaglandin G/H synthase (hPGHS)-1 and hPGHS-2, key enzymes in the formation of prostanoids from arachidonic acid, were expressed at high levels in COS-7 cells using a T7 RNA polymerase/vaccinia virus expression system. The open reading frame of hPGHS-2 cloned
Cyclooxygenases 1 and 2 (COX-1 and COX-2) are key enzymes in prostaglandin biosynthesis and the target enzymes for the widely used nonsteroidal anti-inflammatory drugs. To study the physiological roles of the individual isoforms, we have disrupted the mouse Ptgs1 gene
The rate-limiting step in the formation of prostanoids is the conversion of arachidonic acid to prostaglandin H2 by cyclooxygenase, also known as prostaglandin G/H synthase/cyclooxygenase. Two forms of cyclooxygenase have been characterized: a ubiquitously expressed form (COX-1) and a recently
The Journal of biological chemistry, 267(15), 10816-10822 (1992-05-25)
Prostaglandin G/H synthase (PGG/HS) is the rate-limiting enzyme in the conversion of arachidonic acid to prostaglandins and thromboxanes. We screened a human lung fibroblast cDNA library with an ovine PGG/HS cDNA and isolated a 2.3-kilobase clone (HCO-T9). Sequence analysis of
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