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主要文件

安全信息

L3038

Sigma-Aldrich

Lysenin from Eisenia foetida

solid

别名:

Eisenia Lysenin, Lysenin Protein

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About This Item

MDL编号:
UNSPSC代码:
12352200
NACRES:
NA.32

表单

solid

质量水平

分子量

33 kDa

浓度

≥50% (SDS-PAGE)

储存温度

−20°C

一般描述

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

应用

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

生化/生理作用

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.

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

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分析证书(COA)

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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.
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
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
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

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