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Merck
모든 사진(1)

Key Documents

SRP5208

Sigma-Aldrich

Moesin (410-end), GST tagged human

recombinant, expressed in E. coli, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

동의어(들):

MSN

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About This Item

UNSPSC 코드:
12352202
NACRES:
NA.32

재조합

expressed in E. coli

분석

≥70% (SDS-PAGE)

형태

buffered aqueous glycerol solution

분자량

~50 kDa

NCBI 수납 번호

배송 상태

dry ice

저장 온도

−70°C

유전자 정보

human ... MSN(4478)

일반 설명

Moesin (or membrane-organizing extension spike protein) belongs to ERM family that modulates epithelial integrity by regulating cell-signalling events that affect actin organization and polarity. The effects of Moesin on epithelial cells appear to result from inhibition of Rho signaling. ERM proteins serve a structural role in linkage of the cytoskeletion to the plasma membrane and the rescue of cells lacking Moesin by modulation of Rho signaling indicates that inhibition of Rho activity may be a more critical function of Moesin. The negative feedback loop produced by Rho′s activation of ERM may be an important mechanism that prevents the excessive migratory and invasive properties characteristic of metastatic cancer cells.

물리적 형태

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

제조 메모

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


시험 성적서(COA)

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문서 라이브러리 방문

Olga Speck et al.
Nature, 421(6918), 83-87 (2003-01-04)
Two prominent characteristics of epithelial cells, apical-basal polarity and a highly ordered cytoskeleton, depend on the existence of precisely localized protein complexes associated with the apical plasma membrane, and on a separate machinery that regulates the spatial order of actin
W T Lankes et al.
Proceedings of the National Academy of Sciences of the United States of America, 88(19), 8297-8301 (1991-10-01)
Moesin (membrane-organizing extension spike protein, pronounced mó ez in) has previously been isolated from bovine uterus and characterized as a possible receptor protein for heparan sulfate. We now have cloned and sequenced its complete cDNA, which represents a single 4.2-kilobase

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