Cayman Chemical | 15-Lipoxygenase-2 (human recombinant)

10011263 15-Lipoxygenase-2 (human recombinant)

15-LO-2; 15-LOX-2

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Source: human recombinant C-terminal His-tagged protein expressed in E. coli · M_r: 76 kDa · Two types of 15-lipoxygenase (15-LO) have been discovered and characterized, both of which metabolize arachidonic acid (AA) to produce 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE). 15-LO-1 oxygenates AA at both C-15 and C-12,¹ whereas 15-LO-2 exclusively oxygenates C-15 of AA.² Human 15-LO-2 has a molecular mass of approximately 76 kDa and exhibits approximately 40% identity to the reticulocyte 15-LO-1.^2,3 Expression of 15-LO-2 appears to be restricted to prostate, lung, skin, and cornea and may play a role in the normal development of these tissues.⁴ The protein levels and enzymatic activity of 15-LO-2 are both down-regulated in prostate cancer compared with normal and benign prostate tissues, implicating a possible protective role for 15-LO-2 against tumor formation.^4,5,6 Cayman · s human recombinant 15-LO-2 is expressed and purified from E. coli. The purity was determined using gel electrophoresis followed by coomassie staining. 15-LO-2 specific activity was established using arachidonic acid as the substrate and monitoring diene formation by measuring absorbance 236 nm.

1 Kuhn, H., Barnett, J., Grunberger, D., et al. Overexpression, purification and characterization of human recombinant 15-lipoxygenase. Biochem Biophys Acta 1169(1) 80-89 (1993).

2 Brash, A.R., Chang, M.S., Boeglin, W.E. Discovery of a second 15S-lipoxygenase in humans. Proc Natl Acad Sci USA 94 6148-6152 (1997).

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4 Tang, S., Bhatia, B., Maldonado, C.J., et al. Evidence that arachidonate 15-lipoxygenase 2 is a negative cell cycle regulator in normal prostate epithelial cells. J Biol Chem 277(18) 16189-16201 (2002).

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Pricing updated 2010-03-19.
Prices are subject to change without notice.