추천 제품
일반 설명
Lysenin is a superfamily of certain proteins including lysenin-related protein 1 (LRP-1, lysenin 2) and LRP-2 (lysenin 3).
애플리케이션
Lysenin from Eisenia foetida has been used to treat B cells and study lysenin′s effect on membrane diacylglycerol (DAG) and surface sphingomyelin (SM).
생화학적/생리학적 작용
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
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
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
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