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4802-v
Lysenin
Storage-20℃
Package50μg
Note(Earthworm, Eisenia foetida)
Lysenin is a sphingomyelin-specific binding protein without any cross reactions with other sphingolipids,
such as sphingosine, ceramide and sphingosyl phosphocholine1). It was isolated from the coelomic fluid of the
earthworm Eisenia foetida by Sekizawa et al. in 19962,3) and has a molecular size of 33 kDa as determined by
size-exclusion chromatography2). It has hemolytic and smooth muscle-contracting activity4) and lethal effects
on mouse and Xenopus spermatozoa5). The lethal effects may be brought about by the interaction of lysenin
with sphingomyelin present in the outer leaflets of plasma membranes of spermatozoa. It was shown that
lysenin required cell surface sphingomyelin for its lytic activity on Chinese hamster ovary cells6). In
combination with immunological techniques, it is possible to use lysenin as a tool for histochemical
identification and tissue distribution studies of sphingomyelin1,5). In view of the involvement of ceramide,
sphingosine, and sphingosine 1-phosphate, which are derived from sphingomyelin, in signal transduction,
mitogenesis and apoptosis7), lysenin may serve as a useful tool in elucidating specific reactions leading to
defined cellular responses.
1) A. Yamaji, Y. Sekizawa, K. Emoto, H. Sakuraba, K. Inoue, H. Kobayashi, and M. Umeda, J. Biol. Chem.,
273, 5300 (1998).
2) Y. Sekizawa, K. Hagiwara, T. Nakajima, and H. Kobayashi, Biomed. Res., 17, 197 (1996).
3) Y. Sekizawa, T. Kubo, H. Kobayashi, T. Nakajima, and S. Natori, Gene, 191, 97 (1997).
4) H. Kobayashi, Y. Sekizawa, S. Shioda, S. Natori, T. Nakajima, and M. Umeda, In, Neuroendocrinology-Retrospect
and Perspectives (H.-W. Korf and K.H. Usadel eds.), Springer, 1997, p. 255.
5) M. Ito, S. Abe, Y. Sekizawa, and H. Kobayashi, Biomed. Res., 18, 399 (1997).
6) K. Hanada, T. Hara, M. Fukasawa, A. Yamaji, M. Umeda, and M. Nishijima, J. Biol. Chem., 273, 33787 (1998).
7) L.R. Ballou, S.J.F. Laulederkind, E.F. Rosloniec, and R. Raghow, Biochim. Biophys. Acta, 1301, 273 (1996).
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