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L3038

Sigma-Aldrich

Lysenin from Eisenia foetida

solid

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MDL number:
NACRES:
NA.32

form

solid

Quality Level

mol wt

33 kDa

concentration

≥50% (SDS-PAGE)

storage temp.

−20°C

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This Item
S1135SRP6506SRP6507
Sigma-Aldrich

L3038

Lysenin from Eisenia foetida

Stroma from bovine erythrocytes source of stromal-bound enzymes

S1135

Stroma from bovine erythrocytes

form

solid

form

solid

form

lyophilized

form

lyophilized

mol wt

33 kDa

mol wt

-

mol wt

monomer 200 kDa (Hp 2-1), monomer 400 kDa (Hp 2-2), monomer 86 kDa (Hp 1-1)

mol wt

86 kDa

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

concentration

≥50% (SDS-PAGE)

concentration

-

concentration

-

concentration

-

General description

Lysenin is a superfamily of certain proteins including lysenin-related protein 1 (LRP-1, lysenin 2) and LRP-2 (lysenin 3).

Application

Lysenin from Eisenia foetida has been used to treat B cells and study lysenin′s effect on membrane diacylglycerol (DAG) and surface sphingomyelin (SM).

Biochem/physiol Actions

Lysenin is a 33kDa protein present in the coelomic fluid of the earthworm Eisenia foetida. It interacts with sphingomyelin in cell membranes. In vertebrates, this binding results in cytotoxicity and contraction of smooth muscle in vitro as well as vasodepressor activity and lethality under in vivo conditions.
Lysenin serves as a tool to explore membrane lipid organization. It is known to induce hemolysis in vertebrates and mammalian cells.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Reiko Ishitsuka et al.
Anatomical science international, 79(4), 184-190 (2005-01-07)
Sphingomyelin is a major sphingolipid species in animal cells and is a major lipid constituent of plasma membranes. Recent reports have established important roles for sphingomyelin and its metabolites as second messengers in signal transduction events during development and differentiation.
A Yamaji et al.
The Journal of biological chemistry, 273(9), 5300-5306 (1998-03-28)
Lysenin, a novel 41-kDa protein purified from coelomic fluid of the earthworm Eisenia foetida, induced erythrocyte lysis. Preincubation of lysenin with vesicles containing sphingomyelin inhibited lysenin-induced hemolysis completely, whereas vesicles containing phospholipids other than sphingomyelin showed no inhibitory activity, suggesting
Peiqi Ou et al.
Cell reports, 36(9), 109624-109624 (2021-09-02)
B cell tolerance prevents autoimmunity by deleting or deactivating autoreactive B cells that otherwise may cause autoantibody-driven disorders, including systemic lupus erythematosus (lupus). Lupus is characterized by immunoglobulin Gs carrying a double-stranded (ds)-DNA autospecificity derived mainly from somatic hypermutation in
Hideshi Kobayashi et al.
International review of cytology, 236, 45-99 (2004-07-21)
Lysenin is a protein of 33?kDa in the coelomic fluid (CF) of the earthworm Eisenia foetida. It differs from other biologically active proteins, such as fetidins, eiseniapore, and coelomic cytolytic factor (CCF-1), that have been found in Eisenia foetida, in

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