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Join us! · InformexUSA 2012 · New Orleans, Louisiana · February 14-17, 2012 · Booth 2514

15-Lipoxygenase-1 Western Ready Control Exclusive

Cayman Chemical Item Number 10011677

15-LOX-1 Western Ready Control; 15-LO-1 Western Ready Control

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Description

Application(s): positive control for WB · Source: human recombinant protein expressed in E. coli · Mr: 76 kDa · 15-Lipoxygenase-1 (15-LO-1) catalyzes the formation of 15(S)-HETE and 13(S)-HODE from arachidonic acid and linoleic acid, respectively.1,2 15-LO-1 is a monomer with a molecular mass of approximately 75 kDa and is found primarily in reticulocytes and eosinophils.2,3,4 Interleukin-4 and -13 induce the expression of 15-LO-1 mRNA in human monocytes.5,6 The induction of 15-LO-1 by both agents is inhibited by IFNγ.5,6 A second 15-LO, 15-LO-2, cloned from human hair roots, has been identified.7 15-LO-1 is expressed in prostate, lung, and cornea and exhibits approximately 40% identity to the 15-LO-2.

1 Schewe, T., and Kuhn, H. Do 15-lipoxygenases have a common biological role? Trends Biochem Sci 16 369-373 (1991).

2 Sigal, E., Craik, C.S., Highland, E., et al. Molecular cloning and primary structure of human 15-lipoxygenase. Biochem Biophys Res Commun 157 457-464 (1988).

3 missing reference text

4 missing reference text

5 Conrad, D.J., Kuhn, H., Mulkins, M., et al. Specific inflammatory cytokines regulate the expression of human monocyte 15-lipoxygenase. Proc Natl Acad Sci USA 89 217-221 (1992).

6 Nassar, G.M., Morrow, J.D., Roberts, L.J., et al. Induction of 15-lipoxygenase by interleukin-13 in human blood monocytes. J Biol Chem 269 27631-27634 (1994).

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

Synonyms
  • 15-LOX-1 Western Ready Control
  • 15-LO-1 Western Ready Control
Formulation Laemmli buffer (2% SDS, 10% glycerol, 62.5 mM Tris-HCl, pH 6.8, containing 5% 2-mercaptoethanol, bromophenol blue)
Purity Whole cell lysate
Stability 2 years
Storage -20°C
Shipping Wet ice in continental US; may vary elsewhere

Background Reading

Sigal, E., Grunberger, D., Craik, C.S., et al. Arachidonate 15-lipoxygenase (ω-6 lipoxygenase) from human leukocytes. Purification and strucutral homology to other mammalian lipoxygenases. J Biol Chem 263 5328-5332 (1988).

Conrad, D.J., Kuhn, H., Mulkins, M., et al. Specific inflammatory cytokines regulate the expression of human monocyte 15-lipoxygenase. Proc Natl Acad Sci USA 89 217-221 (1992).

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

Schewe, T., and Kuhn, H. Do 15-lipoxygenases have a common biological role? Trends Biochem Sci 16 369-373 (1991).

Sigal, E., Craik, C.S., Highland, E., et al. Molecular cloning and primary structure of human 15-lipoxygenase. Biochem Biophys Res Commun 157 457-464 (1988).

Fleming, I., Thiel, B.A., Chester, J., et al. The complete sequence of the rabbit erythroid cell-specific 15-lipoxygenase mRNA: Comparison of the predicted amino acid sequence of the erythrocyte lipoxygenase with other lipoxygenases. Gene 79 181-188 (1989).

Nassar, G.M., Morrow, J.D., Roberts, L.J., et al. Induction of 15-lipoxygenase by interleukin-13 in human blood monocytes. J Biol Chem 269 27631-27634 (1994).

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Pricing updated 2012-02-12. Prices are subject to change without notice.

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Warning This product is not for human or veterinary use.

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