Lysenin
Earthworm, Eisenia foetida

4802-v 50 µg | 205.00 EUR

Lysenin from Peptide Institute is a natural product isolated from the coelomic fluid of earthworm

(M.W. 33 kDa)

Salt free lyphilized powder
The purity is guaranteed to be higher than 99% by HPLC

Sphingomyelin-Specific Binding Protein

Anti Lysenin Serum:

Lysenin Antiserum code 14802-s

Lysenin is a sphingomyelin-specific binding protein without any cross reactions with other sphingolipids, such as sphingosine, ceramide and sphingosyl phosphocholine¹⁾. Lysenin was isolated from the coelomic fluid of the earthworm Eisenia foetida by Sekizawa et al. in 1996^{2, 3)} and has a molecular size of 33 kDa as determined by size-exclusion chromatography²⁾. It has hemolytic and smooth muscle-contracting activity ⁴) 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 sphingomyelin^{1, 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.

References:

1. Y. Sekizawa, T. Kubo, H. Kobayashi, T. Nakajima, and S. Natori, Gene, 191, 97 (1997) (Original description of Lysenin; cDNA)
2. Y. Sekizawa, K. Hagiwara, T. Nakajima and H. Kobayashi, Biomed. Res., 17, 197 (1996) (Pharmacology and contractile activity of Lysenin)
3. M. Ito, S. Abe, Y. Sekizawa and H. Kobayashi, Biomed. Res., 18, 399 (1997) (Pharmacol.; Killing of Spermatozoa)
4. A. Yamaji, Y. Sekizawa, K. Emoto, H. Sakuraba, K. Inoue, H. Kobayashi and M. Umeda, J. Biol. Chem., 273, 5300 (1998) (Phramacol.; Sphingomyelin-Specific Binding / Hemolysis)
5. M. Ito, S. Abe, Y. Sekizawa and H. Kobayashi, Biomed. Res., 18, 399 (1997)
6. K. Hanada, T. Hara, M. Fukasawa, A Yamji, M. Umeda and M. Nishijima, J. Biol. Chem., 273, 33787 (1998)(lytic activity of Lysenin)