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Thromboxane A synthase (TXAS), also known as cytochrome P450 (CYP) isoform CYP5A1, is the enzyme that catalyzes the isomerization of prostaglandin H2 (PGH2; Item No. 17020) into thromboxane A2 (TXA2), a vasoconstrictor and an inducer of platelet aggregation.1,2 It also catalyzes the cleavage of PGH2 into malondialdehyde (MDA) and 12(S)-hydroxyheptadecatrienoic acid (12(S)-HHT; Item No. 34590), a leukotriene B4 (LTB4) receptor 2 (BLT2) agonist that also has a role in platelet aggregation.1 TXAS exists as a monomer and is composed of an N-terminal membrane anchor domain, a heme-binding catalytic residue, and several substrate-binding residues.3,4,5 It is expressed in numerous cells, including platelets, monocytes, and macrophages, as well as several tissues, and is localized to the endoplasmic reticulum.3 TXAS undergoes suicide inactivation during catalysis. Mice deficient in TXAS exhibit prolonged bleeding time and defective platelet aggregation.6 Cayman's Thromboxane A Synthase (human, recombinant) protein can be used for enzyme activity assay and Western blot (WB) applications. To construct this protein, the N-terminal amino acids 1-29 of human CYP5A1 were removed and replaced with a hydrophilic sequence. The F-G loop of TXAS was modified using sequences from rabbit CYP2C5 and CYP2C3. The C-terminal of this protein contains 6x-His tag followed by a stop codon.
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1. Biological functions of 12(S)-
2. The biosynthesis of enzymatically oxidized lipids. Front. Endocrinol. (Lausanne) 11, 591819 (2020).
3. A new insight into subinteractomes of functional antagonists: Thromboxane (CYP5A1) and prostacyclin (CYP8A1) synthases. Cell Biol. Int. 45(6), 1175-1182 (2021).
4. Comparison of the construction of a 3-
5. Prostaglandin synthases: Molecular characterization and involvement in prostaglandin biosynthesis. Prog. Lipid Res. 66, 50-68 (2017).
6. TXAS-